Legume Lectins: Proteins with Diverse Applications
Identifieur interne : 000B05 ( Pmc/Corpus ); précédent : 000B04; suivant : 000B06Legume Lectins: Proteins with Diverse Applications
Auteurs : Irlanda Lagarda-Diaz ; Ana Maria Guzman-Partida ; Luz Vazquez-MorenoSource :
- International Journal of Molecular Sciences [ 1422-0067 ] ; 2017.
Abstract
Lectins are a diverse class of proteins distributed extensively in nature. Among these proteins; legume lectins display a variety of interesting features including antimicrobial; insecticidal and antitumor activities. Because lectins recognize and bind to specific glycoconjugates present on the surface of cells and intracellular structures; they can serve as potential target molecules for developing practical applications in the fields of food; agriculture; health and pharmaceutical research. This review presents the current knowledge of the main structural characteristics of legume lectins and the relationship of structure to the exhibited specificities; provides an overview of their particular antimicrobial; insecticidal and antitumor biological activities and describes possible applications based on the pattern of recognized glyco-targets.
Url:
DOI: 10.3390/ijms18061242
PubMed: 28604616
PubMed Central: 5486065
Links to Exploration step
PMC:5486065Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Legume Lectins: Proteins with Diverse Applications</title><author><name sortKey="Lagarda Diaz, Irlanda" sort="Lagarda Diaz, Irlanda" uniqKey="Lagarda Diaz I" first="Irlanda" last="Lagarda-Diaz">Irlanda Lagarda-Diaz</name><affiliation><nlm:aff id="af1-ijms-18-01242">CONACyT-Universidad de Sonora, Blvd. Luis Encinas y Rosales, Hermosillo, Sonora 83000, Mexico;<email>Irlanda.lagarda@unison.mx</email></nlm:aff></affiliation></author><author><name sortKey="Guzman Partida, Ana Maria" sort="Guzman Partida, Ana Maria" uniqKey="Guzman Partida A" first="Ana Maria" last="Guzman-Partida">Ana Maria Guzman-Partida</name><affiliation><nlm:aff id="af2-ijms-18-01242">Coordinacion de Ciencia de los Alimentos, Centro de Investigacion en Alimentacion y Desarrollo, A.C., Apartado Postal 1735, Hermosillo, Sonora 83304, Mexico;<email>gupa@ciad.mx</email></nlm:aff></affiliation></author><author><name sortKey="Vazquez Moreno, Luz" sort="Vazquez Moreno, Luz" uniqKey="Vazquez Moreno L" first="Luz" last="Vazquez-Moreno">Luz Vazquez-Moreno</name><affiliation><nlm:aff id="af2-ijms-18-01242">Coordinacion de Ciencia de los Alimentos, Centro de Investigacion en Alimentacion y Desarrollo, A.C., Apartado Postal 1735, Hermosillo, Sonora 83304, Mexico;<email>gupa@ciad.mx</email></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">28604616</idno><idno type="pmc">5486065</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5486065</idno><idno type="RBID">PMC:5486065</idno><idno type="doi">10.3390/ijms18061242</idno><date when="2017">2017</date><idno type="wicri:Area/Pmc/Corpus">000B05</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000B05</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Legume Lectins: Proteins with Diverse Applications</title><author><name sortKey="Lagarda Diaz, Irlanda" sort="Lagarda Diaz, Irlanda" uniqKey="Lagarda Diaz I" first="Irlanda" last="Lagarda-Diaz">Irlanda Lagarda-Diaz</name><affiliation><nlm:aff id="af1-ijms-18-01242">CONACyT-Universidad de Sonora, Blvd. Luis Encinas y Rosales, Hermosillo, Sonora 83000, Mexico;<email>Irlanda.lagarda@unison.mx</email></nlm:aff></affiliation></author><author><name sortKey="Guzman Partida, Ana Maria" sort="Guzman Partida, Ana Maria" uniqKey="Guzman Partida A" first="Ana Maria" last="Guzman-Partida">Ana Maria Guzman-Partida</name><affiliation><nlm:aff id="af2-ijms-18-01242">Coordinacion de Ciencia de los Alimentos, Centro de Investigacion en Alimentacion y Desarrollo, A.C., Apartado Postal 1735, Hermosillo, Sonora 83304, Mexico;<email>gupa@ciad.mx</email></nlm:aff></affiliation></author><author><name sortKey="Vazquez Moreno, Luz" sort="Vazquez Moreno, Luz" uniqKey="Vazquez Moreno L" first="Luz" last="Vazquez-Moreno">Luz Vazquez-Moreno</name><affiliation><nlm:aff id="af2-ijms-18-01242">Coordinacion de Ciencia de los Alimentos, Centro de Investigacion en Alimentacion y Desarrollo, A.C., Apartado Postal 1735, Hermosillo, Sonora 83304, Mexico;<email>gupa@ciad.mx</email></nlm:aff></affiliation></author></analytic><series><title level="j">International Journal of Molecular Sciences</title><idno type="eISSN">1422-0067</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Lectins are a diverse class of proteins distributed extensively in nature. Among these proteins; legume lectins display a variety of interesting features including antimicrobial; insecticidal and antitumor activities. Because lectins recognize and bind to specific glycoconjugates present on the surface of cells and intracellular structures; they can serve as potential target molecules for developing practical applications in the fields of food; agriculture; health and pharmaceutical research. This review presents the current knowledge of the main structural characteristics of legume lectins and the relationship of structure to the exhibited specificities; provides an overview of their particular antimicrobial; insecticidal and antitumor biological activities and describes possible applications based on the pattern of recognized glyco-targets.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Sharon, N" uniqKey="Sharon N">N. Sharon</name></author><author><name sortKey="Lis, H" uniqKey="Lis H">H. Lis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hamid, R" uniqKey="Hamid R">R. Hamid</name></author><author><name sortKey="Masood, A" uniqKey="Masood A">A. Masood</name></author><author><name sortKey="Wani, I H" uniqKey="Wani I">I.H. Wani</name></author><author><name sortKey="Rafiq, S" uniqKey="Rafiq S">S. Rafiq</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Loris, R" uniqKey="Loris R">R. Loris</name></author><author><name sortKey="Hamelryck, T" uniqKey="Hamelryck T">T. Hamelryck</name></author><author><name sortKey="Bouckaert, J" uniqKey="Bouckaert J">J. Bouckaert</name></author><author><name sortKey="Wyns, L" uniqKey="Wyns L">L. Wyns</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sharon, N" uniqKey="Sharon N">N. Sharon</name></author><author><name sortKey="Lis, H" uniqKey="Lis H">H. Lis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Vazquez Moreno, L" uniqKey="Vazquez Moreno L">L. Vázquez-Moreno</name></author><author><name sortKey="Ortega Nieblas, M" uniqKey="Ortega Nieblas M">M. Ortega-Nieblas</name></author><author><name sortKey="Robles Burgue O, M R" uniqKey="Robles Burgue O M">M.R. Robles-Burgueño</name></author><author><name sortKey="Ramos Clamont, G" uniqKey="Ramos Clamont G">G. Ramos-Clamont</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Guzman Partida, A M" uniqKey="Guzman Partida A">A.M. Guzman-Partida</name></author><author><name sortKey="Robles Burgueno, M R" uniqKey="Robles Burgueno M">M.R. Robles-Burgueno</name></author><author><name sortKey="Ortega Nieblas, M" uniqKey="Ortega Nieblas M">M. Ortega-Nieblas</name></author><author><name sortKey="Vazquez Moreno, I" uniqKey="Vazquez Moreno I">I. Vazquez-Moreno</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Nasi, A" uniqKey="Nasi A">A. Nasi</name></author><author><name sortKey="Picariello, G" uniqKey="Picariello G">G. Picariello</name></author><author><name sortKey="Ferranti, P" uniqKey="Ferranti P">P. Ferranti</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lagarda Diaz, I" uniqKey="Lagarda Diaz I">I. Lagarda-Diaz</name></author><author><name sortKey="Guzman Partida, A M" uniqKey="Guzman Partida A">A.M. Guzman-Partida</name></author><author><name sortKey="Urbano Hernandez, G" uniqKey="Urbano Hernandez G">G. Urbano-Hernandez</name></author><author><name sortKey="Ortega Neblas, M M" uniqKey="Ortega Neblas M">M.M. Ortega-Neblas</name></author><author><name sortKey="Robles Burgueno, M R" uniqKey="Robles Burgueno M">M.R. Robles-Burgueno</name></author><author><name sortKey="Winzerling, J" uniqKey="Winzerling J">J. Winzerling</name></author><author><name sortKey="Vazquez Moreno, L" uniqKey="Vazquez Moreno L">L. Vazquez-Moreno</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sharma, V" uniqKey="Sharma V">V. Sharma</name></author><author><name sortKey="Surolia, A" uniqKey="Surolia A">A. Surolia</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hamelryck, T W" uniqKey="Hamelryck T">T.W. Hamelryck</name></author><author><name sortKey="Loris, R" uniqKey="Loris R">R. Loris</name></author><author><name sortKey="Bouckaert, J" uniqKey="Bouckaert J">J. Bouckaert</name></author><author><name sortKey="Doa Thi, M H" uniqKey="Doa Thi M">M.H. Doa-Thi</name></author><author><name sortKey="Strecker, G" uniqKey="Strecker G">G. Strecker</name></author><author><name sortKey="Imberty, A" uniqKey="Imberty A">A. Imberty</name></author><author><name sortKey="Fernandez, E" uniqKey="Fernandez E">E. Fernandez</name></author><author><name sortKey="Wyns, L" uniqKey="Wyns L">L. Wyns</name></author><author><name sortKey="Etzer, M E" uniqKey="Etzer M">M.E. Etzer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Vijayan, M" uniqKey="Vijayan M">M. Vijayan</name></author><author><name sortKey="Chandra, N" uniqKey="Chandra N">N. Chandra</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sharon, N" uniqKey="Sharon N">N. Sharon</name></author><author><name sortKey="Lis, H" uniqKey="Lis H">H. Lis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hamelryck, T W" uniqKey="Hamelryck T">T.W. Hamelryck</name></author><author><name sortKey="Loris, R" uniqKey="Loris R">R. Loris</name></author><author><name sortKey="Bouckaert, J" uniqKey="Bouckaert J">J. Bouckaert</name></author><author><name sortKey="Wyns, L" uniqKey="Wyns L">L. Wyns</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bouckaert, J" uniqKey="Bouckaert J">J. Bouckaert</name></author><author><name sortKey="Hamelryck, T" uniqKey="Hamelryck T">T. Hamelryck</name></author><author><name sortKey="Wyns, L" uniqKey="Wyns L">L. Wyns</name></author><author><name sortKey="Loris, R" uniqKey="Loris R">R. Loris</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Buts, L" uniqKey="Buts L">L. Buts</name></author><author><name sortKey="Dao Thi, M H" uniqKey="Dao Thi M">M.H. Dao-Thi</name></author><author><name sortKey="Loris, R" uniqKey="Loris R">R. Loris</name></author><author><name sortKey="Wyns, L" uniqKey="Wyns L">L. Wyns</name></author><author><name sortKey="Etzler, M" uniqKey="Etzler M">M. Etzler</name></author><author><name sortKey="Hamelryck, T" uniqKey="Hamelryck T">T. Hamelryck</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Brinda, K V" uniqKey="Brinda K">K.V. Brinda</name></author><author><name sortKey="Mitra, N" uniqKey="Mitra N">N. Mitra</name></author><author><name sortKey="Surolia, A" uniqKey="Surolia A">A. Surolia</name></author><author><name sortKey="Vishveshwara, S" uniqKey="Vishveshwara S">S. Vishveshwara</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Etzler, M E" uniqKey="Etzler M">M.E. Etzler</name></author><author><name sortKey="Surolia, A" uniqKey="Surolia A">A. Surolia</name></author><author><name sortKey="Cummings, R D" uniqKey="Cummings R">R.D. Cummings</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ambrosi, M" uniqKey="Ambrosi M">M. Ambrosi</name></author><author><name sortKey="Cameron, N R" uniqKey="Cameron N">N.R. Cameron</name></author><author><name sortKey="Davis, B G" uniqKey="Davis B">B.G. Davis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Manoj, N" uniqKey="Manoj N">N. Manoj</name></author><author><name sortKey="Suguna, K" uniqKey="Suguna K">K. Suguna</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rudiger, H" uniqKey="Rudiger H">H. Rudiger</name></author><author><name sortKey="Gabius, H J" uniqKey="Gabius H">H.J. Gabius</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Felsted, R L" uniqKey="Felsted R">R.L. Felsted</name></author><author><name sortKey="Leavitt, R D" uniqKey="Leavitt R">R.D. Leavitt</name></author><author><name sortKey="Bachur, N R" uniqKey="Bachur N">N.R. Bachur</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Felsted, R L" uniqKey="Felsted R">R.L. Felsted</name></author><author><name sortKey="Li, J" uniqKey="Li J">J. Li</name></author><author><name sortKey="Pokrywka, G" uniqKey="Pokrywka G">G. Pokrywka</name></author><author><name sortKey="Egorin, M J" uniqKey="Egorin M">M.J. Egorin</name></author><author><name sortKey="Spiegel, J" uniqKey="Spiegel J">J. Spiegel</name></author><author><name sortKey="Dale, R M" uniqKey="Dale R">R.M. Dale</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cummings, R D" uniqKey="Cummings R">R.D. Cummings</name></author><author><name sortKey="Kornfeld, S" uniqKey="Kornfeld S">S. Kornfeld</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Fleischmann, G" uniqKey="Fleischmann G">G. Fleischmann</name></author><author><name sortKey="Mauder, I" uniqKey="Mauder I">I. Mauder</name></author><author><name sortKey="Illert, W" uniqKey="Illert W">W. Illert</name></author><author><name sortKey="Rudiger, H" uniqKey="Rudiger H">H. Rudiger</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hamelryck, T W" uniqKey="Hamelryck T">T.W. Hamelryck</name></author><author><name sortKey="Daothi, M H" uniqKey="Daothi M">M.H. DaoThi</name></author><author><name sortKey="Poortmans, F" uniqKey="Poortmans F">F. Poortmans</name></author><author><name sortKey="Chrispeels, M J" uniqKey="Chrispeels M">M.J. Chrispeels</name></author><author><name sortKey="Wyns, L" uniqKey="Wyns L">L. Wyns</name></author><author><name sortKey="Loris, R" uniqKey="Loris R">R. Loris</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Nagae, M" uniqKey="Nagae M">M. Nagae</name></author><author><name sortKey="Soga, K" uniqKey="Soga K">K. Soga</name></author><author><name sortKey="Morita Matsumoto, K" uniqKey="Morita Matsumoto K">K. Morita-Matsumoto</name></author><author><name sortKey="Hanashima, S" uniqKey="Hanashima S">S. Hanashima</name></author><author><name sortKey="Ikeda, A" uniqKey="Ikeda A">A. Ikeda</name></author><author><name sortKey="Yamamoto, K" uniqKey="Yamamoto K">K. Yamamoto</name></author><author><name sortKey="Yamaguchi, Y" uniqKey="Yamaguchi Y">Y. Yamaguchi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Perez, S" uniqKey="Perez S">S. Pérez</name></author><author><name sortKey="Sarkar, A" uniqKey="Sarkar A">A. Sarkar</name></author><author><name sortKey="Rivet, A" uniqKey="Rivet A">A. Rivet</name></author><author><name sortKey="Breton, C" uniqKey="Breton C">C. Breton</name></author><author><name sortKey="Imberty, A" uniqKey="Imberty A">A. Imberty</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bouckaert, J" uniqKey="Bouckaert J">J. Bouckaert</name></author><author><name sortKey="Loris, R" uniqKey="Loris R">R. Loris</name></author><author><name sortKey="Poortmans, F" uniqKey="Poortmans F">F. Poortmans</name></author><author><name sortKey="Wyns, L" uniqKey="Wyns L">L. Wyns</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Loris, R" uniqKey="Loris R">R. Loris</name></author><author><name sortKey="Casset, F" uniqKey="Casset F">F. Casset</name></author><author><name sortKey="Bouckaert, J" uniqKey="Bouckaert J">J. Bouckaert</name></author><author><name sortKey="Pletinckx, J" uniqKey="Pletinckx J">J. Pletinckx</name></author><author><name sortKey="Daothi, M H" uniqKey="Daothi M">M.H. Daothi</name></author><author><name sortKey="Poortmans, F" uniqKey="Poortmans F">F. Poortmans</name></author><author><name sortKey="Imberty, A" uniqKey="Imberty A">A. Imberty</name></author><author><name sortKey="Perez, S" uniqKey="Perez S">S. Perez</name></author><author><name sortKey="Wyns, L" uniqKey="Wyns L">L. Wyns</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ruzheinikov, S N" uniqKey="Ruzheinikov S">S.N. Ruzheinikov</name></author><author><name sortKey="Mikhailova, I Y" uniqKey="Mikhailova I">I.Y. Mikhailova</name></author><author><name sortKey="Tsygannik, I N" uniqKey="Tsygannik I">I.N. Tsygannik</name></author><author><name sortKey="Pangborn, W" uniqKey="Pangborn W">W. Pangborn</name></author><author><name sortKey="Duax, W" uniqKey="Duax W">W. Duax</name></author><author><name sortKey="Pletnev, V Z" uniqKey="Pletnev V">V.Z. Pletnev</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Babino, A" uniqKey="Babino A">A. Babino</name></author><author><name sortKey="Tello, D" uniqKey="Tello D">D. Tello</name></author><author><name sortKey="Rojas, A" uniqKey="Rojas A">A. Rojas</name></author><author><name sortKey="Bay, S" uniqKey="Bay S">S. Bay</name></author><author><name sortKey="Osinaga, E" uniqKey="Osinaga E">E. Osinaga</name></author><author><name sortKey="Alzari, P M" uniqKey="Alzari P">P.M. Alzari</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Imberty, A" uniqKey="Imberty A">A. Imberty</name></author><author><name sortKey="Gohier, A" uniqKey="Gohier A">A. Gohier</name></author><author><name sortKey="Jordan, E" uniqKey="Jordan E">E. Jordan</name></author><author><name sortKey="Goldstein, I J" uniqKey="Goldstein I">I.J. Goldstein</name></author><author><name sortKey="Perez, S" uniqKey="Perez S">S. Perez</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Felger, R S" uniqKey="Felger R">R.S. Felger</name></author><author><name sortKey="Nabhan, G P" uniqKey="Nabhan G">G.P. Nabhan</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sousa, M" uniqKey="Sousa M">M. Sousa</name></author><author><name sortKey="Delgado, A" uniqKey="Delgado A">A. Delgado</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sousa, S M" uniqKey="Sousa S">S.M. Sousa</name></author><author><name sortKey="Medina, R L" uniqKey="Medina R">R.L. Medina</name></author><author><name sortKey="Andrade, G" uniqKey="Andrade G">G. Andrade</name></author><author><name sortKey="Rico, M L" uniqKey="Rico M">M.L. Rico</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ortega Nieblas, M M" uniqKey="Ortega Nieblas M">M.M. Ortega-Nieblas</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Felipe Ortega, X" uniqKey="Felipe Ortega X">X. Felipe-Ortega</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="L Pez Laredo, A R" uniqKey="L Pez Laredo A">A.R. López-Laredo</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Felix Favela, F" uniqKey="Felix Favela F">F. Félix-Favela</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Quir S Quintero, C E" uniqKey="Quir S Quintero C">C.E. Quirós-Quintero</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Valadez Vega, C" uniqKey="Valadez Vega C">C. Valadez-Vega</name></author><author><name sortKey="Guzman Partida, A M" uniqKey="Guzman Partida A">A.M. Guzmán-Partida</name></author><author><name sortKey="Soto Cordova, F J" uniqKey="Soto Cordova F">F.J. Soto-Cordova</name></author><author><name sortKey="Alvarez Manilla, G" uniqKey="Alvarez Manilla G">G. Álvarez-Manilla</name></author><author><name sortKey="Morales Gonzalez, J A" uniqKey="Morales Gonzalez J">J.A. Morales-González</name></author><author><name sortKey="Madrigal Santillan, E" uniqKey="Madrigal Santillan E">E. Madrigal-Santillán</name></author><author><name sortKey="Villag Mez Ibarra, J R" uniqKey="Villag Mez Ibarra J">J.R. Villagómez-Ibarra</name></author><author><name sortKey="Zu Iga Perez, C" uniqKey="Zu Iga Perez C">C. Zúñiga-Pérez</name></author><author><name sortKey="Gutierrez Salinas, J" uniqKey="Gutierrez Salinas J">J. Gutiérrez-Salinas</name></author><author><name sortKey="Becerril Flores, M A" uniqKey="Becerril Flores M">M.A. Becerril-Flores</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Guzman Partida, A" uniqKey="Guzman Partida A">A. Guzmán-Partida</name></author><author><name sortKey="Felix Favela, F" uniqKey="Felix Favela F">F. Félix-Favela</name></author><author><name sortKey="Mata Haro, V" uniqKey="Mata Haro V">V. Mata-Haro</name></author><author><name sortKey="Lopez Laredo, A" uniqKey="Lopez Laredo A">A. Lopez-Laredo</name></author><author><name sortKey="Urbano Hernandez, G" uniqKey="Urbano Hernandez G">G. Urbano-Hernández</name></author><author><name sortKey="Robles Burgue O, M" uniqKey="Robles Burgue O M">M. Robles-Burgueño</name></author><author><name sortKey="Candia Plata, M" uniqKey="Candia Plata M">M. Candia-Plata</name></author><author><name sortKey="Vazquez Moreno, L" uniqKey="Vazquez Moreno L">L. Vázquez-Moreno</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Miller, J B" uniqKey="Miller J">J.B. Miller</name></author><author><name sortKey="Noyes, C" uniqKey="Noyes C">C. Noyes</name></author><author><name sortKey="Heinrikson, R" uniqKey="Heinrikson R">R. Heinrikson</name></author><author><name sortKey="Kingdon, H S" uniqKey="Kingdon H">H.S. Kingdon</name></author><author><name sortKey="Yachnin, S" uniqKey="Yachnin S">S. Yachnin</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Leavitt, R D" uniqKey="Leavitt R">R.D. Leavitt</name></author><author><name sortKey="Felsted, R L" uniqKey="Felsted R">R.L. Felsted</name></author><author><name sortKey="Bachur, N R" uniqKey="Bachur N">N.R. Bachur</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Roberts, D D" uniqKey="Roberts D">D.D. Roberts</name></author><author><name sortKey="Etzler, M E" uniqKey="Etzler M">M.E. Etzler</name></author><author><name sortKey="Goldstein, I J" uniqKey="Goldstein I">I.J. Goldstein</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sparvoli, F" uniqKey="Sparvoli F">F. Sparvoli</name></author><author><name sortKey="Lanave, C" uniqKey="Lanave C">C. Lanave</name></author><author><name sortKey="Santucci, A" uniqKey="Santucci A">A. Santucci</name></author><author><name sortKey="Bollini, R" uniqKey="Bollini R">R. Bollini</name></author><author><name sortKey="Lioi, L" uniqKey="Lioi L">L. Lioi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Castillo Villanueva, A" uniqKey="Castillo Villanueva A">A. Castillo-Villanueva</name></author><author><name sortKey="Caballero Ortega, H" uniqKey="Caballero Ortega H">H. Caballero-Ortega</name></author><author><name sortKey="Abdullaev Jafarova, F" uniqKey="Abdullaev Jafarova F">F. Abdullaev-Jafarova</name></author><author><name sortKey="Garfias, Y" uniqKey="Garfias Y">Y. Garfias</name></author><author><name sortKey="Jimenez Martinez, M D C" uniqKey="Jimenez Martinez M">M.D.C. Jimenez-Martinez</name></author><author><name sortKey="Bouquelet, S" uniqKey="Bouquelet S">S. Bouquelet</name></author><author><name sortKey="Martinez, G" uniqKey="Martinez G">G. Martinez</name></author><author><name sortKey="Mendoza Hernandez, G" uniqKey="Mendoza Hernandez G">G. Mendoza-Hernandez</name></author><author><name sortKey="Zenteno, E" uniqKey="Zenteno E">E. Zenteno</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Vazquez Moreno, L" uniqKey="Vazquez Moreno L">L. Vazquez-Moreno</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hoffman, L M" uniqKey="Hoffman L">L.M. Hoffman</name></author><author><name sortKey="Donaldson, D D" uniqKey="Donaldson D">D.D. Donaldson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lioi, L" uniqKey="Lioi L">L. Lioi</name></author><author><name sortKey="Sparvoli, F" uniqKey="Sparvoli F">F. Sparvoli</name></author><author><name sortKey="Galasso, I" uniqKey="Galasso I">I. Galasso</name></author><author><name sortKey="Lanave, C" uniqKey="Lanave C">C. Lanave</name></author><author><name sortKey="Bollini, R" uniqKey="Bollini R">R. Bollini</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Karnchanatat, A" uniqKey="Karnchanatat A">A. Karnchanatat</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Grandhi, N J" uniqKey="Grandhi N">N.J. Grandhi</name></author><author><name sortKey="Mamidi, A S" uniqKey="Mamidi A">A.S. Mamidi</name></author><author><name sortKey="Surolia, A" uniqKey="Surolia A">A. Surolia</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cruz, P H" uniqKey="Cruz P">P.H. Cruz</name></author><author><name sortKey="Campos, E P" uniqKey="Campos E">E.P. Campos</name></author><author><name sortKey="Martinez, L M" uniqKey="Martinez L">L.M. Martínez</name></author><author><name sortKey="Ortiz, B" uniqKey="Ortiz B">B. Ortiz</name></author><author><name sortKey="Martinez, G" uniqKey="Martinez G">G. Martínez</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sharon, N" uniqKey="Sharon N">N. Sharon</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Imberty, A" uniqKey="Imberty A">A. Imberty</name></author><author><name sortKey="Casset, F" uniqKey="Casset F">F. Casset</name></author><author><name sortKey="Gegg, C V" uniqKey="Gegg C">C.V. Gegg</name></author><author><name sortKey="Etzler, M E" uniqKey="Etzler M">M.E. Etzler</name></author><author><name sortKey="Perez, S" uniqKey="Perez S">S. Perez</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Young, N M" uniqKey="Young N">N.M. Young</name></author><author><name sortKey="Oomen, R P" uniqKey="Oomen R">R.P. Oomen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Benevides, R G" uniqKey="Benevides R">R.G. Benevides</name></author><author><name sortKey="Ganne, G" uniqKey="Ganne G">G. Ganne</name></author><author><name sortKey="Simoes Rda, C" uniqKey="Simoes Rda C">C. Simoes Rda</name></author><author><name sortKey="Schubert, V" uniqKey="Schubert V">V. Schubert</name></author><author><name sortKey="Niemietz, M" uniqKey="Niemietz M">M. Niemietz</name></author><author><name sortKey="Unverzagt, C" uniqKey="Unverzagt C">C. Unverzagt</name></author><author><name sortKey="Chazalet, V" uniqKey="Chazalet V">V. Chazalet</name></author><author><name sortKey="Breton, C" uniqKey="Breton C">C. Breton</name></author><author><name sortKey="Varrot, A" uniqKey="Varrot A">A. Varrot</name></author><author><name sortKey="Cavada, B S" uniqKey="Cavada B">B.S. Cavada</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Singha, S" uniqKey="Singha S">S. Singha</name></author><author><name sortKey="Bose, P P" uniqKey="Bose P">P.P. Bose</name></author><author><name sortKey="Ganguly, T" uniqKey="Ganguly T">T. Ganguly</name></author><author><name sortKey="Campana, P T" uniqKey="Campana P">P.T. Campana</name></author><author><name sortKey="Ghosh, R" uniqKey="Ghosh R">R. Ghosh</name></author><author><name sortKey="Chatterjee, B P" uniqKey="Chatterjee B">B.P. Chatterjee</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Chrispeels, M J" uniqKey="Chrispeels M">M.J. Chrispeels</name></author><author><name sortKey="Raikhel, N V" uniqKey="Raikhel N">N.V. Raikhel</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Peumans, W J" uniqKey="Peumans W">W.J. Peumans</name></author><author><name sortKey="Van Damme, E" uniqKey="Van Damme E">E. Van Damme</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Delbaere, L T J" uniqKey="Delbaere L">L.T.J. Delbaere</name></author><author><name sortKey="Vandonselaar, M" uniqKey="Vandonselaar M">M. Vandonselaar</name></author><author><name sortKey="Prasad, L" uniqKey="Prasad L">L. Prasad</name></author><author><name sortKey="Quail, J W" uniqKey="Quail J">J.W. Quail</name></author><author><name sortKey="Wilson, K S" uniqKey="Wilson K">K.S. Wilson</name></author><author><name sortKey="Dauter, Z" uniqKey="Dauter Z">Z. Dauter</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Imberty, A" uniqKey="Imberty A">A. Imberty</name></author><author><name sortKey="Gautier, C" uniqKey="Gautier C">C. Gautier</name></author><author><name sortKey="Lescar, J" uniqKey="Lescar J">J. Lescar</name></author><author><name sortKey="Perez, S" uniqKey="Perez S">S. Perez</name></author><author><name sortKey="Wyns, L" uniqKey="Wyns L">L. Wyns</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kolberg, J" uniqKey="Kolberg J">J. Kolberg</name></author><author><name sortKey="Michaelsen, T E" uniqKey="Michaelsen T">T.E. Michaelsen</name></author><author><name sortKey="Sletten, K" uniqKey="Sletten K">K. Sletten</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ray, S" uniqKey="Ray S">S. Ray</name></author><author><name sortKey="Chatterjee, B P" uniqKey="Chatterjee B">B.P. Chatterjee</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Irimura, T" uniqKey="Irimura T">T. Irimura</name></author><author><name sortKey="Tsuji, T" uniqKey="Tsuji T">T. Tsuji</name></author><author><name sortKey="Tagami, S" uniqKey="Tagami S">S. Tagami</name></author><author><name sortKey="Yamamoto, K" uniqKey="Yamamoto K">K. Yamamoto</name></author><author><name sortKey="Osawa, T" uniqKey="Osawa T">T. Osawa</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hammarstrom, S" uniqKey="Hammarstrom S">S. Hammarstrom</name></author><author><name sortKey="Hammarstrom, M L" uniqKey="Hammarstrom M">M.L. Hammarstrom</name></author><author><name sortKey="Sundblad, G" uniqKey="Sundblad G">G. Sundblad</name></author><author><name sortKey="Arnarp, J" uniqKey="Arnarp J">J. Arnarp</name></author><author><name sortKey="Lonngren, J" uniqKey="Lonngren J">J. Lonngren</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Yamashita, K" uniqKey="Yamashita K">K. Yamashita</name></author><author><name sortKey="Hitoi, A" uniqKey="Hitoi A">A. Hitoi</name></author><author><name sortKey="Kobata, A" uniqKey="Kobata A">A. Kobata</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kamemura, K" uniqKey="Kamemura K">K. Kamemura</name></author><author><name sortKey="Furuichi, Y" uniqKey="Furuichi Y">Y. Furuichi</name></author><author><name sortKey="Umekawa, H" uniqKey="Umekawa H">H. Umekawa</name></author><author><name sortKey="Takahashi, T" uniqKey="Takahashi T">T. Takahashi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kaneda, Y" uniqKey="Kaneda Y">Y. Kaneda</name></author><author><name sortKey="Whittier, R F" uniqKey="Whittier R">R.F. Whittier</name></author><author><name sortKey="Yamanaka, H" uniqKey="Yamanaka H">H. Yamanaka</name></author><author><name sortKey="Carredano, E" uniqKey="Carredano E">E. Carredano</name></author><author><name sortKey="Gotoh, M" uniqKey="Gotoh M">M. Gotoh</name></author><author><name sortKey="Sota, H" uniqKey="Sota H">H. Sota</name></author><author><name sortKey="Hasegawa, Y" uniqKey="Hasegawa Y">Y. Hasegawa</name></author><author><name sortKey="Shinohara, Y" uniqKey="Shinohara Y">Y. Shinohara</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Takeya, A" uniqKey="Takeya A">A. Takeya</name></author><author><name sortKey="Hosomi, O" uniqKey="Hosomi O">O. Hosomi</name></author><author><name sortKey="Nishijima, H" uniqKey="Nishijima H">H. Nishijima</name></author><author><name sortKey="Ohe, Y" uniqKey="Ohe Y">Y. Ohe</name></author><author><name sortKey="Sugahara, K" uniqKey="Sugahara K">K. Sugahara</name></author><author><name sortKey="Sagi, M" uniqKey="Sagi M">M. Sagi</name></author><author><name sortKey="Yamazaki, K" uniqKey="Yamazaki K">K. Yamazaki</name></author><author><name sortKey="Hayakawa, H" uniqKey="Hayakawa H">H. Hayakawa</name></author><author><name sortKey="Takeshita, H" uniqKey="Takeshita H">H. Takeshita</name></author><author><name sortKey="Sasaki, C" uniqKey="Sasaki C">C. Sasaki</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rinderle, S J" uniqKey="Rinderle S">S.J. Rinderle</name></author><author><name sortKey="Goldstein, I J" uniqKey="Goldstein I">I.J. Goldstein</name></author><author><name sortKey="Matta, K L" uniqKey="Matta K">K.L. Matta</name></author><author><name sortKey="Ratcliffe, R M" uniqKey="Ratcliffe R">R.M. Ratcliffe</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ramos, M V" uniqKey="Ramos M">M.V. Ramos</name></author><author><name sortKey="Sampaio, A H" uniqKey="Sampaio A">A.H. Sampaio</name></author><author><name sortKey="Cavada, B S" uniqKey="Cavada B">B.S. Cavada</name></author><author><name sortKey="Calvete, J J" uniqKey="Calvete J">J.J. Calvete</name></author><author><name sortKey="Grangeiro, T B" uniqKey="Grangeiro T">T.B. Grangeiro</name></author><author><name sortKey="Debray, H" uniqKey="Debray H">H. Debray</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Iskratsch, T" uniqKey="Iskratsch T">T. Iskratsch</name></author><author><name sortKey="Braun, A" uniqKey="Braun A">A. Braun</name></author><author><name sortKey="Paschinger, K" uniqKey="Paschinger K">K. Paschinger</name></author><author><name sortKey="Wilson, I B H" uniqKey="Wilson I">I.B.H. Wilson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Gomes, F S" uniqKey="Gomes F">F.S. Gomes</name></author><author><name sortKey="Procopio, T F" uniqKey="Procopio T">T.F. Procopio</name></author><author><name sortKey="Napoleao, T H" uniqKey="Napoleao T">T.H. Napoleao</name></author><author><name sortKey="Coelho, L C" uniqKey="Coelho L">L.C. Coelho</name></author><author><name sortKey="Paiva, P M" uniqKey="Paiva P">P.M. Paiva</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Marchaim, D" uniqKey="Marchaim D">D. Marchaim</name></author><author><name sortKey="Lemanek, L" uniqKey="Lemanek L">L. Lemanek</name></author><author><name sortKey="Bheemreddy, S" uniqKey="Bheemreddy S">S. Bheemreddy</name></author><author><name sortKey="Kaye, K S" uniqKey="Kaye K">K.S. Kaye</name></author><author><name sortKey="Sobel, J D" uniqKey="Sobel J">J.D. Sobel</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Yim, N H" uniqKey="Yim N">N.-H. Yim</name></author><author><name sortKey="Jung, Y P" uniqKey="Jung Y">Y.P. Jung</name></author><author><name sortKey="Cho, W K" uniqKey="Cho W">W.-K. Cho</name></author><author><name sortKey="Kim, T" uniqKey="Kim T">T. Kim</name></author><author><name sortKey="Kim, A" uniqKey="Kim A">A. Kim</name></author><author><name sortKey="Im, M" uniqKey="Im M">M. Im</name></author><author><name sortKey="Ma, J Y" uniqKey="Ma J">J.Y. Ma</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Srivastava, P" uniqKey="Srivastava P">P. Srivastava</name></author><author><name sortKey="Upreti, D K" uniqKey="Upreti D">D.K. Upreti</name></author><author><name sortKey="Dhole, T N" uniqKey="Dhole T">T.N. Dhole</name></author><author><name sortKey="Srivastava, A K" uniqKey="Srivastava A">A.K. Srivastava</name></author><author><name sortKey="Nayak, M T" uniqKey="Nayak M">M.T. Nayak</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Davies, J" uniqKey="Davies J">J. Davies</name></author><author><name sortKey="Davies, D" uniqKey="Davies D">D. Davies</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="De Brito Marques Ramos, D" uniqKey="De Brito Marques Ramos D">D. De Brito Marques Ramos</name></author><author><name sortKey="Gomes, F S" uniqKey="Gomes F">F.S. Gomes</name></author><author><name sortKey="Napoleao, T H" uniqKey="Napoleao T">T.H. Napoleão</name></author><author><name sortKey="Paiva, P M G" uniqKey="Paiva P">P.M.G. Paiva</name></author><author><name sortKey="Da Silva, M D C" uniqKey="Da Silva M">M.D.C. da Silva</name></author><author><name sortKey="Barroso Coelho, L C B" uniqKey="Barroso Coelho L">L.C.B. Barroso Coelho</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Broekaert, W F" uniqKey="Broekaert W">W.F. Broekaert</name></author><author><name sortKey="Cammue, B P A" uniqKey="Cammue B">B.P.A. Cammue</name></author><author><name sortKey="Debolle, M F C" uniqKey="Debolle M">M.F.C. DeBolle</name></author><author><name sortKey="Thevissen, K" uniqKey="Thevissen K">K. Thevissen</name></author><author><name sortKey="Desamblanx, G W" uniqKey="Desamblanx G">G.W. DeSamblanx</name></author><author><name sortKey="Osborn, R W" uniqKey="Osborn R">R.W. Osborn</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lehrer, R I" uniqKey="Lehrer R">R.I. Lehrer</name></author><author><name sortKey="Ganz, T" uniqKey="Ganz T">T. Ganz</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sharon, N" uniqKey="Sharon N">N. Sharon</name></author><author><name sortKey="Lis, H" uniqKey="Lis H">H. Lis</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Charungchitrak, S" uniqKey="Charungchitrak S">S. Charungchitrak</name></author><author><name sortKey="Petsom, A" uniqKey="Petsom A">A. Petsom</name></author><author><name sortKey="Sangvanich, P" uniqKey="Sangvanich P">P. Sangvanich</name></author><author><name sortKey="Karnchanatat, A" uniqKey="Karnchanatat A">A. Karnchanatat</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bah, C S F" uniqKey="Bah C">C.S.F. Bah</name></author><author><name sortKey="Fang, E F" uniqKey="Fang E">E.F. Fang</name></author><author><name sortKey="Ng, T B" uniqKey="Ng T">T.B. Ng</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Oliveira, M D L" uniqKey="Oliveira M">M.D.L. Oliveira</name></author><author><name sortKey="Andrade, C A S" uniqKey="Andrade C">C.A.S. Andrade</name></author><author><name sortKey="Santos Magalhaes, N S" uniqKey="Santos Magalhaes N">N.S. Santos-Magalhaes</name></author><author><name sortKey="Coelho, L C B B" uniqKey="Coelho L">L.C.B.B. Coelho</name></author><author><name sortKey="Teixeira, J A" uniqKey="Teixeira J">J.A. Teixeira</name></author><author><name sortKey="Carneiro Da Cunha, M G" uniqKey="Carneiro Da Cunha M">M.G. Carneiro-Da-Cunha</name></author><author><name sortKey="Correia, M T S" uniqKey="Correia M">M.T.S. Correia</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sammour, R H" uniqKey="Sammour R">R.H. Sammour</name></author><author><name sortKey="El Shanshoury, A" uniqKey="El Shanshoury A">A. El-Shanshoury</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ayouba, A" uniqKey="Ayouba A">A. Ayouba</name></author><author><name sortKey="Causse, H" uniqKey="Causse H">H. Causse</name></author><author><name sortKey="Vandamme, E J M" uniqKey="Vandamme E">E.J.M. Vandamme</name></author><author><name sortKey="Peumans, W J" uniqKey="Peumans W">W.J. Peumans</name></author><author><name sortKey="Bourne, Y" uniqKey="Bourne Y">Y. Bourne</name></author><author><name sortKey="Cambillau, C" uniqKey="Cambillau C">C. Cambillau</name></author><author><name sortKey="Rouge, P" uniqKey="Rouge P">P. Rouge</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Santi Gadelha, T" uniqKey="Santi Gadelha T">T. Santi-Gadelha</name></author><author><name sortKey="Rocha, B A M" uniqKey="Rocha B">B.A.M. Rocha</name></author><author><name sortKey="Gadelha, C A A" uniqKey="Gadelha C">C.A.A. Gadelha</name></author><author><name sortKey="Silva, H C" uniqKey="Silva H">H.C. Silva</name></author><author><name sortKey="Castellon, R E R" uniqKey="Castellon R">R.E.R. Castellon</name></author><author><name sortKey="Goncalves, F J T" uniqKey="Goncalves F">F.J.T. Goncalves</name></author><author><name sortKey="Toyama, D O" uniqKey="Toyama D">D.O. Toyama</name></author><author><name sortKey="Toyama, M H" uniqKey="Toyama M">M.H. Toyama</name></author><author><name sortKey="De Souza, A J F" uniqKey="De Souza A">A.J.F. de Souza</name></author><author><name sortKey="Beriam, L O S" uniqKey="Beriam L">L.O.S. Beriam</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Islam, B" uniqKey="Islam B">B. Islam</name></author><author><name sortKey="Khan, A U" uniqKey="Khan A">A.U. Khan</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bourne, Y" uniqKey="Bourne Y">Y. Bourne</name></author><author><name sortKey="Ayouba, A" uniqKey="Ayouba A">A. Ayouba</name></author><author><name sortKey="Rouge, P" uniqKey="Rouge P">P. Rouge</name></author><author><name sortKey="Cambillau, C" uniqKey="Cambillau C">C. Cambillau</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Qadir, S" uniqKey="Qadir S">S. Qadir</name></author><author><name sortKey="Wani, I H" uniqKey="Wani I">I.H. Wani</name></author><author><name sortKey="Rafiq, S" uniqKey="Rafiq S">S. Rafiq</name></author><author><name sortKey="Ganie, S A" uniqKey="Ganie S">S.A. Ganie</name></author><author><name sortKey="Masood, A" uniqKey="Masood A">A. Masood</name></author><author><name sortKey="Hamid, R" uniqKey="Hamid R">R. Hamid</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Yan, Q J" uniqKey="Yan Q">Q.J. Yan</name></author><author><name sortKey="Jiang, Z Q" uniqKey="Jiang Z">Z.Q. Jiang</name></author><author><name sortKey="Yang, S Q" uniqKey="Yang S">S.Q. Yang</name></author><author><name sortKey="Deng, W" uniqKey="Deng W">W. Deng</name></author><author><name sortKey="Han, L J" uniqKey="Han L">L.J. Han</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Chen, J" uniqKey="Chen J">J. Chen</name></author><author><name sortKey="Liu, B" uniqKey="Liu B">B. Liu</name></author><author><name sortKey="Ji, N" uniqKey="Ji N">N. Ji</name></author><author><name sortKey="Zhou, J" uniqKey="Zhou J">J. Zhou</name></author><author><name sortKey="Bian, H J" uniqKey="Bian H">H.J. Bian</name></author><author><name sortKey="Li, C Y" uniqKey="Li C">C.Y. Li</name></author><author><name sortKey="Chen, F" uniqKey="Chen F">F. Chen</name></author><author><name sortKey="Bao, J K" uniqKey="Bao J">J.K. Bao</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Silva, H C" uniqKey="Silva H">H.C. Silva</name></author><author><name sortKey="Pinto, L D" uniqKey="Pinto L">L.D. Pinto</name></author><author><name sortKey="Teixeira, E H" uniqKey="Teixeira E">E.H. Teixeira</name></author><author><name sortKey="Nascimento, K S" uniqKey="Nascimento K">K.S. Nascimento</name></author><author><name sortKey="Cavada, B S" uniqKey="Cavada B">B.S. Cavada</name></author><author><name sortKey="Silva, A L C" uniqKey="Silva A">A.L.C. Silva</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Barkai Golan, R" uniqKey="Barkai Golan R">R. Barkai-Golan</name></author><author><name sortKey="Mirelman, D" uniqKey="Mirelman D">D. Mirelman</name></author><author><name sortKey="Sharon, N" uniqKey="Sharon N">N. Sharon</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ye, X Y" uniqKey="Ye X">X.Y. Ye</name></author><author><name sortKey="Ng, T B" uniqKey="Ng T">T.B. Ng</name></author><author><name sortKey="Tsang, P W K" uniqKey="Tsang P">P.W.K. Tsang</name></author><author><name sortKey="Wang, J" uniqKey="Wang J">J. Wang</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Leal, A F" uniqKey="Leal A">A.F. Leal</name></author><author><name sortKey="Lopes, N E" uniqKey="Lopes N">N.E. Lopes</name></author><author><name sortKey="Clark, A T" uniqKey="Clark A">A.T. Clark</name></author><author><name sortKey="De Pontes Filho, N T" uniqKey="De Pontes Filho N">N.T. de Pontes Filho</name></author><author><name sortKey="Beltrao, E I" uniqKey="Beltrao E">E.I. Beltrao</name></author><author><name sortKey="Neves, R P" uniqKey="Neves R">R.P. Neves</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Akkouh, O" uniqKey="Akkouh O">O. Akkouh</name></author><author><name sortKey="Ng, T B" uniqKey="Ng T">T.B. Ng</name></author><author><name sortKey="Singh, S S" uniqKey="Singh S">S.S. Singh</name></author><author><name sortKey="Yin, C M" uniqKey="Yin C">C.M. Yin</name></author><author><name sortKey="Dan, X L" uniqKey="Dan X">X.L. Dan</name></author><author><name sortKey="Chan, Y S" uniqKey="Chan Y">Y.S. Chan</name></author><author><name sortKey="Pan, W L" uniqKey="Pan W">W.L. Pan</name></author><author><name sortKey="Cheung, R C F" uniqKey="Cheung R">R.C.F. Cheung</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ingale, A G" uniqKey="Ingale A">A.G. Ingale</name></author><author><name sortKey="Hivrale, A U" uniqKey="Hivrale A">A.U. Hivrale</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Mukhopadhyay, B" uniqKey="Mukhopadhyay B">B. Mukhopadhyay</name></author><author><name sortKey="Martins, M B" uniqKey="Martins M">M.B. Martins</name></author><author><name sortKey="Karamanska, R" uniqKey="Karamanska R">R. Karamanska</name></author><author><name sortKey="Russell, D A" uniqKey="Russell D">D.A. Russell</name></author><author><name sortKey="Field, R A" uniqKey="Field R">R.A. Field</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Charan, R D" uniqKey="Charan R">R.D. Charan</name></author><author><name sortKey="Munro, M H G" uniqKey="Munro M">M.H.G. Munro</name></author><author><name sortKey="O Eefe, B R" uniqKey="O Eefe B">B.R. O’Keefe</name></author><author><name sortKey="Sowder, R C" uniqKey="Sowder R">R.C. Sowder</name></author><author><name sortKey="Mckee, T C" uniqKey="Mckee T">T.C. McKee</name></author><author><name sortKey="Currens, M J" uniqKey="Currens M">M.J. Currens</name></author><author><name sortKey="Pannell, L K" uniqKey="Pannell L">L.K. Pannell</name></author><author><name sortKey="Boyd, M R" uniqKey="Boyd M">M.R. Boyd</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Matsui, T" uniqKey="Matsui T">T. Matsui</name></author><author><name sortKey="Kobayashi, S" uniqKey="Kobayashi S">S. Kobayashi</name></author><author><name sortKey="Yoshida, O" uniqKey="Yoshida O">O. Yoshida</name></author><author><name sortKey="Ishii, S" uniqKey="Ishii S">S. Ishii</name></author><author><name sortKey="Abe, Y" uniqKey="Abe Y">Y. Abe</name></author><author><name sortKey="Yamamoto, N" uniqKey="Yamamoto N">N. Yamamoto</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hansen, J E" uniqKey="Hansen J">J.E. Hansen</name></author><author><name sortKey="Nielsen, C M" uniqKey="Nielsen C">C.M. Nielsen</name></author><author><name sortKey="Nielsen, C" uniqKey="Nielsen C">C. Nielsen</name></author><author><name sortKey="Heegaard, P" uniqKey="Heegaard P">P. Heegaard</name></author><author><name sortKey="Mathiesen, L R" uniqKey="Mathiesen L">L.R. Mathiesen</name></author><author><name sortKey="Nielsen, J O" uniqKey="Nielsen J">J.O. Nielsen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Dan, X L" uniqKey="Dan X">X.L. Dan</name></author><author><name sortKey="Liu, W L" uniqKey="Liu W">W.L. Liu</name></author><author><name sortKey="Ng, T B" uniqKey="Ng T">T.B. Ng</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wong, J H" uniqKey="Wong J">J.H. Wong</name></author><author><name sortKey="Ng, T B" uniqKey="Ng T">T.B. Ng</name></author><author><name sortKey="Cheung, R C" uniqKey="Cheung R">R.C. Cheung</name></author><author><name sortKey="Ye, X J" uniqKey="Ye X">X.J. Ye</name></author><author><name sortKey="Wang, H X" uniqKey="Wang H">H.X. Wang</name></author><author><name sortKey="Lam, S K" uniqKey="Lam S">S.K. Lam</name></author><author><name sortKey="Lin, P" uniqKey="Lin P">P. Lin</name></author><author><name sortKey="Chan, Y S" uniqKey="Chan Y">Y.S. Chan</name></author><author><name sortKey="Fang, E F" uniqKey="Fang E">E.F. Fang</name></author><author><name sortKey="Ngai, P H" uniqKey="Ngai P">P.H. Ngai</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Adams, D J" uniqKey="Adams D">D.J. Adams</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lis, H" uniqKey="Lis H">H. Lis</name></author><author><name sortKey="Sharon, N" uniqKey="Sharon N">N. Sharon</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ciopraga, J" uniqKey="Ciopraga J">J. Ciopraga</name></author><author><name sortKey="Gozia, O" uniqKey="Gozia O">O. Gozia</name></author><author><name sortKey="Tudor, R" uniqKey="Tudor R">R. Tudor</name></author><author><name sortKey="Brezuica, L" uniqKey="Brezuica L">L. Brezuica</name></author><author><name sortKey="Doyle, R J" uniqKey="Doyle R">R.J. Doyle</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Van Parijs, J" uniqKey="Van Parijs J">J. Van Parijs</name></author><author><name sortKey="Broekaert, W F" uniqKey="Broekaert W">W.F. Broekaert</name></author><author><name sortKey="Goldstein, I J" uniqKey="Goldstein I">I.J. Goldstein</name></author><author><name sortKey="Peumans, W J" uniqKey="Peumans W">W.J. Peumans</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Boleti, A P D" uniqKey="Boleti A">A.P.D. Boleti</name></author><author><name sortKey="Freire, M D M" uniqKey="Freire M">M.D.M. Freire</name></author><author><name sortKey="Coelho, M B" uniqKey="Coelho M">M.B. Coelho</name></author><author><name sortKey="Da Silva, W" uniqKey="Da Silva W">W. da Silva</name></author><author><name sortKey="Baldasso, P A" uniqKey="Baldasso P">P.A. Baldasso</name></author><author><name sortKey="Gomes, V M" uniqKey="Gomes V">V.M. Gomes</name></author><author><name sortKey="Marangoni, S" uniqKey="Marangoni S">S. Marangoni</name></author><author><name sortKey="Novello, J C" uniqKey="Novello J">J.C. Novello</name></author><author><name sortKey="Macedo, M L R" uniqKey="Macedo M">M.L.R. Macedo</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rao, V S R" uniqKey="Rao V">V.S.R. Rao</name></author><author><name sortKey="Lam, K" uniqKey="Lam K">K. Lam</name></author><author><name sortKey="Qasba, P K" uniqKey="Qasba P">P.K. Qasba</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Vigerust, D J" uniqKey="Vigerust D">D.J. Vigerust</name></author><author><name sortKey="Shepherd, V L" uniqKey="Shepherd V">V.L. Shepherd</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ziolkowska, N E" uniqKey="Ziolkowska N">N.E. Ziolkowska</name></author><author><name sortKey="Wlodawer, A" uniqKey="Wlodawer A">A. Wlodawer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Keyaerts, E" uniqKey="Keyaerts E">E. Keyaerts</name></author><author><name sortKey="Vijgen, L" uniqKey="Vijgen L">L. Vijgen</name></author><author><name sortKey="Pannecouque, C" uniqKey="Pannecouque C">C. Pannecouque</name></author><author><name sortKey="Van Damme, E" uniqKey="Van Damme E">E. Van Damme</name></author><author><name sortKey="Peumans, W" uniqKey="Peumans W">W. Peumans</name></author><author><name sortKey="Egberink, H" uniqKey="Egberink H">H. Egberink</name></author><author><name sortKey="Balzarini, J" uniqKey="Balzarini J">J. Balzarini</name></author><author><name sortKey="Van Ranst, M" uniqKey="Van Ranst M">M. Van Ranst</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lusvarghi, S" uniqKey="Lusvarghi S">S. Lusvarghi</name></author><author><name sortKey="Bewley, C A" uniqKey="Bewley C">C.A. Bewley</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Fei Fang, E" uniqKey="Fei Fang E">E. Fei Fang</name></author><author><name sortKey="Ho Wong, J" uniqKey="Ho Wong J">J. Ho Wong</name></author><author><name sortKey="Lin, P" uniqKey="Lin P">P. Lin</name></author><author><name sortKey="Bun Ng, T" uniqKey="Bun Ng T">T. Bun Ng</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Macedo, M L R" uniqKey="Macedo M">M.L.R. Macedo</name></author><author><name sortKey="Das Gracas Machado Freire, M" uniqKey="Das Gracas Machado Freire M">M. das Graças Machado Freire</name></author><author><name sortKey="Da Silva, M B R" uniqKey="Da Silva M">M.B.R. da Silva</name></author><author><name sortKey="Coelho, L C B B" uniqKey="Coelho L">L.C.B.B. Coelho</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Melander, M" uniqKey="Melander M">M. Melander</name></author><author><name sortKey=" Hman, I" uniqKey=" Hman I">I. Åhman</name></author><author><name sortKey="Kamnert, I" uniqKey="Kamnert I">I. Kamnert</name></author><author><name sortKey="Stromdahl, A C" uniqKey="Stromdahl A">A.-C. Strömdahl</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Michiels, K" uniqKey="Michiels K">K. Michiels</name></author><author><name sortKey="Van Damme, E J" uniqKey="Van Damme E">E.J. Van Damme</name></author><author><name sortKey="Smagghe, G" uniqKey="Smagghe G">G. Smagghe</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Dandagi, P" uniqKey="Dandagi P">P. Dandagi</name></author><author><name sortKey="Mastiholimath, V" uniqKey="Mastiholimath V">V. Mastiholimath</name></author><author><name sortKey="Patil, M" uniqKey="Patil M">M. Patil</name></author><author><name sortKey="Gupta, M" uniqKey="Gupta M">M. Gupta</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Walski, T" uniqKey="Walski T">T. Walski</name></author><author><name sortKey="Van Damme, E J" uniqKey="Van Damme E">E.J. Van Damme</name></author><author><name sortKey="Smagghe, G" uniqKey="Smagghe G">G. Smagghe</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Roy, A" uniqKey="Roy A">A. Roy</name></author><author><name sortKey="Gupta, S" uniqKey="Gupta S">S. Gupta</name></author><author><name sortKey="Hess, D" uniqKey="Hess D">D. Hess</name></author><author><name sortKey="Das, K P" uniqKey="Das K">K.P. Das</name></author><author><name sortKey="Das, S" uniqKey="Das S">S. Das</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Francis, F" uniqKey="Francis F">F. Francis</name></author><author><name sortKey="Marty Detraves, C" uniqKey="Marty Detraves C">C. Marty-Detraves</name></author><author><name sortKey="Poincloux, R" uniqKey="Poincloux R">R. Poincloux</name></author><author><name sortKey="Baricault, L" uniqKey="Baricault L">L. Baricault</name></author><author><name sortKey="Fournier, D" uniqKey="Fournier D">D. Fournier</name></author><author><name sortKey="Paquereau, L" uniqKey="Paquereau L">L. Paquereau</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Caccia, S" uniqKey="Caccia S">S. Caccia</name></author><author><name sortKey="Van Damme, E J" uniqKey="Van Damme E">E.J. Van Damme</name></author><author><name sortKey="De Vos, W H" uniqKey="De Vos W">W.H. De Vos</name></author><author><name sortKey="Smagghe, G" uniqKey="Smagghe G">G. Smagghe</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zhu Salzman, K" uniqKey="Zhu Salzman K">K. Zhu-Salzman</name></author><author><name sortKey="Salzman, R A" uniqKey="Salzman R">R.A. Salzman</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Fitches, E" uniqKey="Fitches E">E. Fitches</name></author><author><name sortKey="Wiles, D" uniqKey="Wiles D">D. Wiles</name></author><author><name sortKey="Douglas, A E" uniqKey="Douglas A">A.E. Douglas</name></author><author><name sortKey="Hinchliffe, G" uniqKey="Hinchliffe G">G. Hinchliffe</name></author><author><name sortKey="Audsley, N" uniqKey="Audsley N">N. Audsley</name></author><author><name sortKey="Gatehouse, J A" uniqKey="Gatehouse J">J.A. Gatehouse</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Du, J" uniqKey="Du J">J. Du</name></author><author><name sortKey="Foissac, X" uniqKey="Foissac X">X. Foissac</name></author><author><name sortKey="Carss, A" uniqKey="Carss A">A. Carss</name></author><author><name sortKey="Gatehouse, A M" uniqKey="Gatehouse A">A.M. Gatehouse</name></author><author><name sortKey="Gatehouse, J A" uniqKey="Gatehouse J">J.A. Gatehouse</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sadeghi, A" uniqKey="Sadeghi A">A. Sadeghi</name></author><author><name sortKey="Smagghe, G" uniqKey="Smagghe G">G. Smagghe</name></author><author><name sortKey="Proost, P" uniqKey="Proost P">P. Proost</name></author><author><name sortKey="Van Damme, E J" uniqKey="Van Damme E">E.J. Van Damme</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Napoleao, T H" uniqKey="Napoleao T">T.H. Napoleão</name></author><author><name sortKey="Pontual, E V" uniqKey="Pontual E">E.V. Pontual</name></author><author><name sortKey="De Albuquerque Lima, T" uniqKey="De Albuquerque Lima T">T. de Albuquerque Lima</name></author><author><name sortKey="De Lima Santos, N D" uniqKey="De Lima Santos N">N.D. de Lima Santos</name></author><author><name sortKey="Sa, R A" uniqKey="Sa R">R.A. Sá</name></author><author><name sortKey="Coelho, L C B B" uniqKey="Coelho L">L.C.B.B. Coelho</name></author><author><name sortKey="Do Amaral Ferraz Navarro, D M" uniqKey="Do Amaral Ferraz Navarro D">D.M. do Amaral Ferraz Navarro</name></author><author><name sortKey="Paiva, P M G" uniqKey="Paiva P">P.M.G. Paiva</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sprawka, I" uniqKey="Sprawka I">I. Sprawka</name></author><author><name sortKey="Golawska, S" uniqKey="Golawska S">S. Goławska</name></author><author><name sortKey="Golawski, A" uniqKey="Golawski A">A. Goławski</name></author><author><name sortKey="Chrzanowski, G" uniqKey="Chrzanowski G">G. Chrzanowski</name></author><author><name sortKey="Czerniewicz, P" uniqKey="Czerniewicz P">P. Czerniewicz</name></author><author><name sortKey="Sytykiewicz, H" uniqKey="Sytykiewicz H">H. Sytykiewicz</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bala, A" uniqKey="Bala A">A. Bala</name></author><author><name sortKey="Roy, A" uniqKey="Roy A">A. Roy</name></author><author><name sortKey="Behura, N" uniqKey="Behura N">N. Behura</name></author><author><name sortKey="Hess, D" uniqKey="Hess D">D. Hess</name></author><author><name sortKey="Das, S" uniqKey="Das S">S. Das</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lagarda Diaz, I" uniqKey="Lagarda Diaz I">I. Lagarda-Diaz</name></author><author><name sortKey="Guzman Partida, A M" uniqKey="Guzman Partida A">A.M. Guzman-Partida</name></author><author><name sortKey="Huerta Ocampo, J A" uniqKey="Huerta Ocampo J">J.A. Huerta-Ocampo</name></author><author><name sortKey="Winzerling, J" uniqKey="Winzerling J">J. Winzerling</name></author><author><name sortKey="Vazquez Moreno, L" uniqKey="Vazquez Moreno L">L. Vazquez-Moreno</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lagarda Diaz, I" uniqKey="Lagarda Diaz I">I. Lagarda-Diaz</name></author><author><name sortKey="Robles Burge O, M R" uniqKey="Robles Burge O M">M.R. Robles-Burgeño</name></author><author><name sortKey="Guzman Partida, A M" uniqKey="Guzman Partida A">A.M. Guzman-Partida</name></author><author><name sortKey="Geiser, D" uniqKey="Geiser D">D. Geiser</name></author><author><name sortKey="Winzerling, J" uniqKey="Winzerling J">J. Winzerling</name></author><author><name sortKey="Vazquez Moreno, L" uniqKey="Vazquez Moreno L">L. Vazquez-Moreno</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Upadhyay, S K" uniqKey="Upadhyay S">S.K. Upadhyay</name></author><author><name sortKey="Singh, P K" uniqKey="Singh P">P.K. Singh</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Shen, L" uniqKey="Shen L">L. Shen</name></author><author><name sortKey="Luo, Z" uniqKey="Luo Z">Z. Luo</name></author><author><name sortKey="Wu, J" uniqKey="Wu J">J. Wu</name></author><author><name sortKey="Qiu, L" uniqKey="Qiu L">L. Qiu</name></author><author><name sortKey="Luo, M" uniqKey="Luo M">M. Luo</name></author><author><name sortKey="Ke, Q" uniqKey="Ke Q">Q. Ke</name></author><author><name sortKey="Dong, X" uniqKey="Dong X">X. Dong</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Litynska, A" uniqKey="Litynska A">A. Litynska</name></author><author><name sortKey="Przybyuulo, M" uniqKey="Przybyuulo M">M. Przybyuulo</name></author><author><name sortKey="Pochec, E" uniqKey="Pochec E">E. Pochec</name></author><author><name sortKey="Hoja Uulukowicz, D" uniqKey="Hoja Uulukowicz D">D. Hoja-uuLukowicz</name></author><author><name sortKey="Ciouulczyk, D" uniqKey="Ciouulczyk D">D. Ciouulczyk</name></author><author><name sortKey="Laidler, P" uniqKey="Laidler P">P. Laidler</name></author><author><name sortKey="Gil, D" uniqKey="Gil D">D. Gil</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Korourian, S" uniqKey="Korourian S">S. Korourian</name></author><author><name sortKey="Siegel, E" uniqKey="Siegel E">E. Siegel</name></author><author><name sortKey="Kieber Emmons, T" uniqKey="Kieber Emmons T">T. Kieber-Emmons</name></author><author><name sortKey="Monzavi Karbassi, B" uniqKey="Monzavi Karbassi B">B. Monzavi-Karbassi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Blomme, B" uniqKey="Blomme B">B. Blomme</name></author><author><name sortKey="Van Steenkiste, C" uniqKey="Van Steenkiste C">C. Van Steenkiste</name></author><author><name sortKey="Callewaert, N" uniqKey="Callewaert N">N. Callewaert</name></author><author><name sortKey="Van Vlierberghe, H" uniqKey="Van Vlierberghe H">H. Van Vlierberghe</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Fu, L L" uniqKey="Fu L">L.L. Fu</name></author><author><name sortKey="Zhou, C C" uniqKey="Zhou C">C.C. Zhou</name></author><author><name sortKey="Yao, S" uniqKey="Yao S">S. Yao</name></author><author><name sortKey="Yu, J Y" uniqKey="Yu J">J.Y. Yu</name></author><author><name sortKey="Liu, B" uniqKey="Liu B">B. Liu</name></author><author><name sortKey="Bao, J K" uniqKey="Bao J">J.K. Bao</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Stauder, H" uniqKey="Stauder H">H. Stauder</name></author><author><name sortKey="Kreuser, E D" uniqKey="Kreuser E">E.-D. Kreuser</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Jiang, Q L" uniqKey="Jiang Q">Q.L. Jiang</name></author><author><name sortKey="Zhang, S" uniqKey="Zhang S">S. Zhang</name></author><author><name sortKey="Tian, M" uniqKey="Tian M">M. Tian</name></author><author><name sortKey="Zhang, S Y" uniqKey="Zhang S">S.Y. Zhang</name></author><author><name sortKey="Xie, T" uniqKey="Xie T">T. Xie</name></author><author><name sortKey="Chen, D Y" uniqKey="Chen D">D.Y. Chen</name></author><author><name sortKey="Chen, Y J" uniqKey="Chen Y">Y.J. Chen</name></author><author><name sortKey="He, J" uniqKey="He J">J. He</name></author><author><name sortKey="Liu, J" uniqKey="Liu J">J. Liu</name></author><author><name sortKey="Ouyang, L" uniqKey="Ouyang L">L. Ouyang</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hajela, K" uniqKey="Hajela K">K. Hajela</name></author><author><name sortKey="Kojima, M" uniqKey="Kojima M">M. Kojima</name></author><author><name sortKey="Ambrus, G" uniqKey="Ambrus G">G. Ambrus</name></author><author><name sortKey="Wong, K H" uniqKey="Wong K">K.H. Wong</name></author><author><name sortKey="Moffatt, B E" uniqKey="Moffatt B">B.E. Moffatt</name></author><author><name sortKey="Ferluga, J" uniqKey="Ferluga J">J. Ferluga</name></author><author><name sortKey="Hajela, S" uniqKey="Hajela S">S. Hajela</name></author><author><name sortKey="Gal, P" uniqKey="Gal P">P. Gál</name></author><author><name sortKey="Sim, R B" uniqKey="Sim R">R.B. Sim</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Panda, P K" uniqKey="Panda P">P.K. Panda</name></author><author><name sortKey="Mukhopadhyay, S" uniqKey="Mukhopadhyay S">S. Mukhopadhyay</name></author><author><name sortKey="Behera, B" uniqKey="Behera B">B. Behera</name></author><author><name sortKey="Bhol, C S" uniqKey="Bhol C">C.S. Bhol</name></author><author><name sortKey="Dey, S" uniqKey="Dey S">S. Dey</name></author><author><name sortKey="Das, D N" uniqKey="Das D">D.N. Das</name></author><author><name sortKey="Sinha, N" uniqKey="Sinha N">N. Sinha</name></author><author><name sortKey="Bissoyi, A" uniqKey="Bissoyi A">A. Bissoyi</name></author><author><name sortKey="Pramanik, K" uniqKey="Pramanik K">K. Pramanik</name></author><author><name sortKey="Maiti, T K" uniqKey="Maiti T">T.K. Maiti</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kim, M" uniqKey="Kim M">M. Kim</name></author><author><name sortKey="Rao, M" uniqKey="Rao M">M. Rao</name></author><author><name sortKey="Tweardy, D" uniqKey="Tweardy D">D. Tweardy</name></author><author><name sortKey="Prakash, M" uniqKey="Prakash M">M. Prakash</name></author><author><name sortKey="Galili, U" uniqKey="Galili U">U. Galili</name></author><author><name sortKey="Gorelik, E" uniqKey="Gorelik E">E. Gorelik</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Chang, C P" uniqKey="Chang C">C.P. Chang</name></author><author><name sortKey="Lei, H Y" uniqKey="Lei H">H.Y. Lei</name></author></analytic></biblStruct></listBibl></div1></back></TEI><pmc article-type="review-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Int J Mol Sci</journal-id><journal-id journal-id-type="iso-abbrev">Int J Mol Sci</journal-id><journal-id journal-id-type="publisher-id">ijms</journal-id><journal-title-group><journal-title>International Journal of Molecular Sciences</journal-title></journal-title-group><issn pub-type="epub">1422-0067</issn><publisher><publisher-name>MDPI</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">28604616</article-id><article-id pub-id-type="pmc">5486065</article-id><article-id pub-id-type="doi">10.3390/ijms18061242</article-id><article-id pub-id-type="publisher-id">ijms-18-01242</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review</subject></subj-group></article-categories><title-group><article-title>Legume Lectins: Proteins with Diverse Applications</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Lagarda-Diaz</surname><given-names>Irlanda</given-names></name><xref ref-type="aff" rid="af1-ijms-18-01242">1</xref></contrib><contrib contrib-type="author"><name><surname>Guzman-Partida</surname><given-names>Ana Maria</given-names></name><xref ref-type="aff" rid="af2-ijms-18-01242">2</xref></contrib><contrib contrib-type="author"><name><surname>Vazquez-Moreno</surname><given-names>Luz</given-names></name><xref ref-type="aff" rid="af2-ijms-18-01242">2</xref><xref rid="c1-ijms-18-01242" ref-type="corresp">*</xref></contrib></contrib-group><contrib-group><contrib contrib-type="editor"><name><surname>Van Damme</surname><given-names>Els</given-names></name><role>Academic Editor</role></contrib></contrib-group><aff id="af1-ijms-18-01242"><label>1</label>CONACyT-Universidad de Sonora, Blvd. Luis Encinas y Rosales, Hermosillo, Sonora 83000, Mexico;<email>Irlanda.lagarda@unison.mx</email></aff><aff id="af2-ijms-18-01242"><label>2</label>Coordinacion de Ciencia de los Alimentos, Centro de Investigacion en Alimentacion y Desarrollo, A.C., Apartado Postal 1735, Hermosillo, Sonora 83304, Mexico;<email>gupa@ciad.mx</email></aff><author-notes><corresp id="c1-ijms-18-01242"><label>*</label>Correspondence: <email>lvazquez@ciad.mx</email>; Tel./Fax: +52-662-280-0058</corresp></author-notes><pub-date pub-type="epub"><day>12</day><month>6</month><year>2017</year></pub-date><pub-date pub-type="collection"><month>6</month><year>2017</year></pub-date><volume>18</volume><issue>6</issue><elocation-id>1242</elocation-id><history><date date-type="received"><day>29</day><month>4</month><year>2017</year></date><date date-type="accepted"><day>05</day><month>6</month><year>2017</year></date></history><permissions><copyright-statement>© 2017 by the authors.</copyright-statement><copyright-year>2017</copyright-year><license license-type="open-access"><license-p>Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</ext-link>).</license-p></license></permissions><abstract><p>Lectins are a diverse class of proteins distributed extensively in nature. Among these proteins; legume lectins display a variety of interesting features including antimicrobial; insecticidal and antitumor activities. Because lectins recognize and bind to specific glycoconjugates present on the surface of cells and intracellular structures; they can serve as potential target molecules for developing practical applications in the fields of food; agriculture; health and pharmaceutical research. This review presents the current knowledge of the main structural characteristics of legume lectins and the relationship of structure to the exhibited specificities; provides an overview of their particular antimicrobial; insecticidal and antitumor biological activities and describes possible applications based on the pattern of recognized glyco-targets.</p></abstract><kwd-group><kwd>lectin</kwd><kwd>legume</kwd><kwd>insecticidal</kwd><kwd>antimicrobial</kwd><kwd>cancer</kwd></kwd-group></article-meta></front><body><sec id="sec1-ijms-18-01242"><title>1. Introduction</title><p>Currently, lectins are defined as carbohydrate binding proteins of non-immune origin that can recognize and bind simple or complex carbohydrates in a reversible and highly specific manner. For a long time, these proteins were named hemagglutinins, due to their ability to agglutinate red blood cells. At present, this concept is used when the specificity is unknown. It is also known that monomeric lectins do not exhibit this agglutinating activity [<xref rid="B1-ijms-18-01242" ref-type="bibr">1</xref>]. Lectins are ubiquitously present in fungi, animals, bacteria, viruses and plants. Among plant lectins, those of legumes have been the most widely considered [<xref rid="B2-ijms-18-01242" ref-type="bibr">2</xref>]. These lectins are abundant in the seeds and belong to a group of highly homologous proteins. However, their carbohydrate specificities and quaternary structures vary extensively [<xref rid="B3-ijms-18-01242" ref-type="bibr">3</xref>], which greatly influences the type of recognized targets.</p><p>Throughout the history of lectin research, legume seeds have been screened for lectin activity. The existence of binding sites for specific carbohydrates, the main characteristic of lectins, is undoubtedly an important factor for determining their activity and future applications based on their properties. This review centers on the lectins of legumes, highlighting their specificity, particularities, main reported activities and potential applications.</p></sec><sec id="sec2-ijms-18-01242"><title>2. Structure of Legume Lectins</title><p>Legume lectins represent the largest family of carbohydrate binding proteins, and their physicochemical and biological properties have been broadly studied [<xref rid="B4-ijms-18-01242" ref-type="bibr">4</xref>,<xref rid="B5-ijms-18-01242" ref-type="bibr">5</xref>,<xref rid="B6-ijms-18-01242" ref-type="bibr">6</xref>,<xref rid="B7-ijms-18-01242" ref-type="bibr">7</xref>,<xref rid="B8-ijms-18-01242" ref-type="bibr">8</xref>]. Research of the plant lectin family using newer biochemical and biophysical strategies has significantly moved the field forward, and provided a model framework for studying protein–carbohydrate interactions. Although plant lectins share high sequence homology and exhibit comparable physicochemical and structural properties, the diversity of their carbohydrate recognition specificity is remarkable. Generally, the three-dimensional structure of plant lectins is characterized by β-sheets that are connected by α turns, β turns and bends. In addition to short loops, the quaternary interfaces are formed between β-sheets. The β-sheets are connected by loops forming antiparallel chains usually devoid of α helices (<xref ref-type="fig" rid="ijms-18-01242-f001">Figure 1</xref>) [<xref rid="B4-ijms-18-01242" ref-type="bibr">4</xref>,<xref rid="B5-ijms-18-01242" ref-type="bibr">5</xref>,<xref rid="B9-ijms-18-01242" ref-type="bibr">9</xref>,<xref rid="B10-ijms-18-01242" ref-type="bibr">10</xref>,<xref rid="B11-ijms-18-01242" ref-type="bibr">11</xref>,<xref rid="B12-ijms-18-01242" ref-type="bibr">12</xref>].</p><p>Analysis of legume lectin monomers reveals high similarity in sequence as well as structure, with only minor variations in the length of loops and strands. The monomer structures display a jellyroll motif best described as a sandwich of 25–30 kDa containing a carbohydrate recognition domain (CRD) and metal binding sites for divalent cations (Ca<sup>2+</sup> and Mn<sup>2+</sup>). However, in spite of strong similarities in primary, secondary and tertiary structures, the quaternary structures show considerable variations that lead to changes in the monomer–monomer interactions and the presence/absence of protein modifications, such as glycosylation. The impact of these variations has functional implications as they dictate the specificity of multivalent glycan binding [<xref rid="B1-ijms-18-01242" ref-type="bibr">1</xref>,<xref rid="B5-ijms-18-01242" ref-type="bibr">5</xref>,<xref rid="B11-ijms-18-01242" ref-type="bibr">11</xref>,<xref rid="B13-ijms-18-01242" ref-type="bibr">13</xref>,<xref rid="B14-ijms-18-01242" ref-type="bibr">14</xref>,<xref rid="B15-ijms-18-01242" ref-type="bibr">15</xref>,<xref rid="B16-ijms-18-01242" ref-type="bibr">16</xref>,<xref rid="B17-ijms-18-01242" ref-type="bibr">17</xref>,<xref rid="B18-ijms-18-01242" ref-type="bibr">18</xref>]. Most legume lectins appear to assemble as homodimers or homo-tetramers (dimers of dimers), the stability of which is attributed to hydrophobic cooperation, hydrogen bonds and salt links [<xref rid="B4-ijms-18-01242" ref-type="bibr">4</xref>,<xref rid="B9-ijms-18-01242" ref-type="bibr">9</xref>,<xref rid="B19-ijms-18-01242" ref-type="bibr">19</xref>].</p><p>Legume lectins are subdivided into two categories, those with indistinguishable or almost indistinguishable subunits, and those with a variety of subunits [<xref rid="B20-ijms-18-01242" ref-type="bibr">20</xref>]. <italic>Phaseolus vulgaris</italic> lectins (PHA) are well-studied lectins of the first group [<xref rid="B21-ijms-18-01242" ref-type="bibr">21</xref>,<xref rid="B22-ijms-18-01242" ref-type="bibr">22</xref>,<xref rid="B23-ijms-18-01242" ref-type="bibr">23</xref>,<xref rid="B24-ijms-18-01242" ref-type="bibr">24</xref>,<xref rid="B25-ijms-18-01242" ref-type="bibr">25</xref>,<xref rid="B26-ijms-18-01242" ref-type="bibr">26</xref>]. There are more than forty structures of legume lectins reported in either the apo (ligand-free) or holo (sugar-bound) form in the Protein Data Bank [<xref rid="B15-ijms-18-01242" ref-type="bibr">15</xref>,<xref rid="B26-ijms-18-01242" ref-type="bibr">26</xref>,<xref rid="B27-ijms-18-01242" ref-type="bibr">27</xref>,<xref rid="B28-ijms-18-01242" ref-type="bibr">28</xref>,<xref rid="B29-ijms-18-01242" ref-type="bibr">29</xref>,<xref rid="B30-ijms-18-01242" ref-type="bibr">30</xref>,<xref rid="B31-ijms-18-01242" ref-type="bibr">31</xref>,<xref rid="B32-ijms-18-01242" ref-type="bibr">32</xref>]. However, data about lectins from wild legumes is rare. </p><p>Mexico has roughly 1800 species of wild legumes confined to various regions, and more than 33 percent are within the Sonoran Desert [<xref rid="B5-ijms-18-01242" ref-type="bibr">5</xref>,<xref rid="B33-ijms-18-01242" ref-type="bibr">33</xref>,<xref rid="B34-ijms-18-01242" ref-type="bibr">34</xref>,<xref rid="B35-ijms-18-01242" ref-type="bibr">35</xref>,<xref rid="B36-ijms-18-01242" ref-type="bibr">36</xref>,<xref rid="B37-ijms-18-01242" ref-type="bibr">37</xref>,<xref rid="B38-ijms-18-01242" ref-type="bibr">38</xref>,<xref rid="B39-ijms-18-01242" ref-type="bibr">39</xref>,<xref rid="B40-ijms-18-01242" ref-type="bibr">40</xref>,<xref rid="B41-ijms-18-01242" ref-type="bibr">41</xref>,<xref rid="B42-ijms-18-01242" ref-type="bibr">42</xref>]. The isolation and purification of lectins from seeds of native plants such as <italic>Parkinsonia aculeata</italic>, <italic>Olneya tesota</italic>, <italic>Acacia constricta</italic>, <italic>Prosopis juliflora</italic>, <italic>Cercidium praecox</italic>, <italic>Caesalpinia caladenia</italic> and <italic>Phaseolus acutifolius</italic> has been described. Lectins from these plants have monomers of either 30 or 66 kDa that also can form tetramers or dimers. In addition, it has been shown that these lectins involve a group of different isolectins, compared to those found in lectins of the <italic>Phaseolus</italic> genus [<xref rid="B43-ijms-18-01242" ref-type="bibr">43</xref>,<xref rid="B44-ijms-18-01242" ref-type="bibr">44</xref>,<xref rid="B45-ijms-18-01242" ref-type="bibr">45</xref>,<xref rid="B46-ijms-18-01242" ref-type="bibr">46</xref>,<xref rid="B47-ijms-18-01242" ref-type="bibr">47</xref>].</p><p>On the other hand, the primary sequences of plant lectins have been used to infer evolutionary relationships, to reflect processing routes, to suggest folding patterns as well as to provide clues on how carbohydrate ligands fit into their binding pockets [<xref rid="B20-ijms-18-01242" ref-type="bibr">20</xref>]. Direct amino acid sequencing has revealed homology among the lectins from the wild desert legumes <italic>A. constricta</italic> [<xref rid="B6-ijms-18-01242" ref-type="bibr">6</xref>] and <italic>O. tesota</italic> [<xref rid="B5-ijms-18-01242" ref-type="bibr">5</xref>,<xref rid="B48-ijms-18-01242" ref-type="bibr">48</xref>], and more domesticated species like <italic>P. vulgaris</italic> and <italic>P. coccineus</italic> [<xref rid="B49-ijms-18-01242" ref-type="bibr">49</xref>,<xref rid="B50-ijms-18-01242" ref-type="bibr">50</xref>]. Furthermore, antibodies raised against PHA show reactivity with lectins from <italic>A. constricta</italic>, <italic>C. praecox</italic> and <italic>C. caladenia</italic> [<xref rid="B6-ijms-18-01242" ref-type="bibr">6</xref>]. From these studies, it is clear that lectins have been conserved during the evolution of legumes and that the extensive homologies reflect taxonomical relationships among these plants [<xref rid="B51-ijms-18-01242" ref-type="bibr">51</xref>].</p></sec><sec id="sec3-ijms-18-01242"><title>3. Specificity of Legume Lectins</title><p>Legume lectins represent a crucial point in the study of the molecular basis of protein–carbohydrate interactions. Each has a CRD with a basic architecture accessible to both monosaccharides and/or oligosaccharides that confers remarkable divergence in their specificities [<xref rid="B12-ijms-18-01242" ref-type="bibr">12</xref>,<xref rid="B52-ijms-18-01242" ref-type="bibr">52</xref>]. Lectins can non-covalently interact with carbohydrates in a manner that is usually reversible and highly specific. Recognition can occur in the terminal or intermediate position of the glycan structure [<xref rid="B53-ijms-18-01242" ref-type="bibr">53</xref>]. In all legume lectins, four invariant amino acid residues participate in the binding of the carbohydrate, yet each lectin shows different specificity [<xref rid="B18-ijms-18-01242" ref-type="bibr">18</xref>,<xref rid="B54-ijms-18-01242" ref-type="bibr">54</xref>,<xref rid="B55-ijms-18-01242" ref-type="bibr">55</xref>]. The CRD pocket is formed by four loops adjacent to each other, but the loops are not close in sequence. These regions exhibit the highest residue variability and appear to be involved in specificity determination [<xref rid="B56-ijms-18-01242" ref-type="bibr">56</xref>,<xref rid="B57-ijms-18-01242" ref-type="bibr">57</xref>]. The CRD of legume lectins lies in close proximity to the metal binding sites, which may aid in binding activity [<xref rid="B18-ijms-18-01242" ref-type="bibr">18</xref>], but are not often directly involved in carbohydrate binding [<xref rid="B18-ijms-18-01242" ref-type="bibr">18</xref>].</p><p>Most lectins bind to mono- and oligosaccharides; however, more recently discovered lectins show specificity for complex sugars and glycoproteins. Generally, lectins show specificity for di-, tri- and tetra-saccharides with association constants significantly higher than those for the corresponding monosaccharides [<xref rid="B5-ijms-18-01242" ref-type="bibr">5</xref>,<xref rid="B18-ijms-18-01242" ref-type="bibr">18</xref>,<xref rid="B58-ijms-18-01242" ref-type="bibr">58</xref>]. Some lectins have shown affinity towards carbohydrate structures not present in plants, such as the Thomsen-nouveau antigen or complex N-glycan structures with terminal galactose and sialic acid residues [<xref rid="B30-ijms-18-01242" ref-type="bibr">30</xref>]. The specificity of legume lectins for some typical animal glycans, has led to the suggestion that legume lectins play a role in plant defense against insects and/or predator animals [<xref rid="B59-ijms-18-01242" ref-type="bibr">59</xref>,<xref rid="B60-ijms-18-01242" ref-type="bibr">60</xref>].</p><p>The legume lectins that have been purified and characterized as members of the complex type include, <italic>Griffonia simplicifolia</italic> IV lectin (GS IV) [<xref rid="B5-ijms-18-01242" ref-type="bibr">5</xref>,<xref rid="B61-ijms-18-01242" ref-type="bibr">61</xref>], <italic>Maackia amurensis</italic> lectin (MAH and MAL-1) [<xref rid="B62-ijms-18-01242" ref-type="bibr">62</xref>], <italic>Cicer arietinum</italic> lectin [<xref rid="B63-ijms-18-01242" ref-type="bibr">63</xref>], <italic>Saraca indica</italic> lectin [<xref rid="B58-ijms-18-01242" ref-type="bibr">58</xref>,<xref rid="B64-ijms-18-01242" ref-type="bibr">64</xref>] and <italic>P. vulgaris</italic> E and L lectins (PHA-E and PHA-L) [<xref rid="B5-ijms-18-01242" ref-type="bibr">5</xref>,<xref rid="B23-ijms-18-01242" ref-type="bibr">23</xref>,<xref rid="B26-ijms-18-01242" ref-type="bibr">26</xref>,<xref rid="B65-ijms-18-01242" ref-type="bibr">65</xref>,<xref rid="B66-ijms-18-01242" ref-type="bibr">66</xref>,<xref rid="B67-ijms-18-01242" ref-type="bibr">67</xref>,<xref rid="B68-ijms-18-01242" ref-type="bibr">68</xref>,<xref rid="B69-ijms-18-01242" ref-type="bibr">69</xref>]. Wild legume lectins from the Sonoran Desert also have shown varying degrees of specificity for some complex carbohydrates of glycoproteins. The hemagglutinating activity of <italic>A. constricta</italic> isolectins (VLs) and the <italic>P. juliflora</italic> lectin is strongly inhibited in the presence of asialofetuin and to a lesser extent with fetuin and thyroglobulin [<xref rid="B6-ijms-18-01242" ref-type="bibr">6</xref>,<xref rid="B40-ijms-18-01242" ref-type="bibr">40</xref>]. <italic>C. praecox</italic> and <italic>C. caladenia</italic> lectins are inhibited by fetuin and mucine [<xref rid="B37-ijms-18-01242" ref-type="bibr">37</xref>]. <italic>O. tesota</italic> PF1 and PF3 lectins are inhibited by free monosaccharides and/or by complex carbohydrates of fetuin, thyroglobulin, immunoglobulin, mucine and ovalbumin, whereas PF2 is only inhibited by the intact glycoprotein [<xref rid="B5-ijms-18-01242" ref-type="bibr">5</xref>]. Although glycan structures present in glycoproteins are known to have N and O linked oligosaccharides, desialylation of the glycan can result in an increase or decrease in lectin binding affinity [<xref rid="B70-ijms-18-01242" ref-type="bibr">70</xref>]. The galactose residues found in glycosylated proteins are often capped with sialic acid, a characteristic that may alter the interaction with lectins, as is seen for <italic>Amaranthus caudatus</italic> and <italic>Abrus pulchellus</italic> [<xref rid="B71-ijms-18-01242" ref-type="bibr">71</xref>,<xref rid="B72-ijms-18-01242" ref-type="bibr">72</xref>].</p><p>Many studies on lectin–carbohydrate specificity have been published. Unfortunately, often specificity analyses are used to “specifically” determine structural motifs in glycoconjugates without taking into account the rather complex data on this subject. Furthermore, the choice of ligands used to assay lectin binding in some studies is limited either by natural or commercially available sources of glycans, or to simple mono- or disaccharides. Therefore, a critical re-evaluation of lectin binding specificities is required. Such studies using microarray techniques with immobilized glycans or immobilized lectins, dot blot assays to screen different lectins and antibodies with multiple oligosaccharides, combined with information gleaned using recombinant glycosyltransferases, are opening up new possibilities of generating a broader range of standard (neo)glycoconjugates with clearly defined structures [<xref rid="B73-ijms-18-01242" ref-type="bibr">73</xref>].</p></sec><sec id="sec4-ijms-18-01242"><title>4. Antimicrobial Activity</title><p>Antimicrobials have been used to treat diseases caused by bacteria and fungi and such treatments have significantly reduced the mortality rate from these infections in humans and animals. However, the extensive use of antimicrobial substances in medical, agricultural, and veterinary practices is a topic of great concern to clinical microbiologists all over the world due to the growing emergence of opportunistic microorganism strains resistant to drugs that cause serious infections [<xref rid="B74-ijms-18-01242" ref-type="bibr">74</xref>,<xref rid="B75-ijms-18-01242" ref-type="bibr">75</xref>,<xref rid="B76-ijms-18-01242" ref-type="bibr">76</xref>,<xref rid="B77-ijms-18-01242" ref-type="bibr">77</xref>]. Microbial resistance is a genetic phenomenon resulting in a reduction in effectiveness of drug therapy; it may be caused by mutations during the reproductive process of the microorganisms or by imported genes acquired through transduction, conjugation, and transformation mechanisms [<xref rid="B78-ijms-18-01242" ref-type="bibr">78</xref>]. Therefore, there is a growing interest in developing new strategies for inhibiting the growth or survival of microorganisms based on the screening of new sources of natural compounds as alternatives to commercially available drugs [<xref rid="B74-ijms-18-01242" ref-type="bibr">74</xref>,<xref rid="B79-ijms-18-01242" ref-type="bibr">79</xref>].</p><p>A large number of proteins with antibacterial, antifungal and/or antiviral activity have been isolated from the seeds, tubers, and rhizomes of different plants, where they accumulate to high levels and may function as a reserve source of amino acids and metal ions [<xref rid="B80-ijms-18-01242" ref-type="bibr">80</xref>]. These proteins may directly interfere with the growth, multiplication and spread of microbial agents by different mechanisms [<xref rid="B81-ijms-18-01242" ref-type="bibr">81</xref>], as in the case of lectins, by agglutination and/or microorganism immobilization. Plant lectins often are present at potential sites of microbial invasion and their binding to fungal structures led to the inhibition of fungal growth and germination. Studies carried out with soy bean and common lentil agglutinins provide evidence for these roles [<xref rid="B51-ijms-18-01242" ref-type="bibr">51</xref>,<xref rid="B82-ijms-18-01242" ref-type="bibr">82</xref>,<xref rid="B83-ijms-18-01242" ref-type="bibr">83</xref>,<xref rid="B84-ijms-18-01242" ref-type="bibr">84</xref>]. A main characteristic of lectins is their ability to interact with glyco-components present on the cell membrane surface, in cytoplasmic and nuclear structures and in the extracellular matrix of cells and tissues from almost all kingdoms of life [<xref rid="B85-ijms-18-01242" ref-type="bibr">85</xref>]. Therefore, plant lectins are thought to play important roles in the plant immune defense and emerge as potential antimicrobial candidates for drug therapies. The antimicrobial effect of legume lectins is shown in <xref ref-type="table" rid="ijms-18-01242-t001">Table 1</xref>. Although many lectins show antimicrobial activity, clinical trials are needed to establish therapeutic efficacy, to optimize dosage, delivery and bioavailability, and to assess potential allergic reactions [<xref rid="B86-ijms-18-01242" ref-type="bibr">86</xref>].</p><sec id="sec4dot1-ijms-18-01242"><title>4.1. Bacteria</title><p>The antibacterial activity of lectins results from their interaction with a wide variety of complex carbohydrates of the bacterial cell wall, such as teichoic and teichuronic acids, peptidoglycans and lipopolysaccharides [<xref rid="B2-ijms-18-01242" ref-type="bibr">2</xref>,<xref rid="B85-ijms-18-01242" ref-type="bibr">85</xref>]. Lectins of <italic>Triticum vulgare</italic>, <italic>Dolichos lablab</italic> L., <italic>Trigonella foenumgraecum</italic>, <italic>Trifolium alexandrium</italic> L., <italic>Bauhinia variegata</italic> L. and <italic>Delonix regia</italic> have shown antimicrobial activity against <italic>Mycobacterium rhodochrous</italic>, <italic>Bacillus cereus</italic>, <italic>B. megaterium</italic>, <italic>B. sphaericus</italic>, <italic>Escherichia coli</italic>, <italic>Serratia marcescens</italic>, <italic>Corynebacterium xerosis</italic> and <italic>Staphylococcus aureus</italic> [<xref rid="B86-ijms-18-01242" ref-type="bibr">86</xref>] Lectins from the <italic>Vicieae tribe</italic> strongly react with the bacterial cell wall components, muramic acid, <italic>N</italic>-acetylmuramic acid and muramyl dipeptides [<xref rid="B87-ijms-18-01242" ref-type="bibr">87</xref>]. Nevertheless, although legume seed lectins can recognize and bind to the constituents of the bacterial cell wall, such binding does not imply that these interactions occur in vivo, and certainly does not prove that these lectins are involved in the protection of seedlings against bacteria [<xref rid="B51-ijms-18-01242" ref-type="bibr">51</xref>].</p><p>It is thought that plant lectins do not alter the membrane structure and/or permeability nor disturb the normal intracellular processes of invading microbes, since they exert an indirect effect that is based on interactions with cell wall carbohydrates or extracellular glycans [<xref rid="B60-ijms-18-01242" ref-type="bibr">60</xref>]. However, electron microscopy studies revealed that treatment with <italic>Araucaria angustifolia</italic> lectin promoted morphologic alterations, including the presence of pores in the membrane of Gram-positive bacteria, and bubbling on the cell wall of Gram-negative bacteria [<xref rid="B88-ijms-18-01242" ref-type="bibr">88</xref>]. Others reported that the antibacterial activity of lectins occurred through the interactions of the lectins with <italic>N</italic>-acetylglucosamine, <italic>N</italic>-acetylmuramic acid and tetrapeptides linked to <italic>N</italic>-acetylmuramic acid present in the cell wall of Gram-positive bacteria, or to lipopolysaccharides present in the cell wall of Gram-negative bacteria [<xref rid="B87-ijms-18-01242" ref-type="bibr">87</xref>].</p><p>In addition to these findings, lectins from the legumes from <italic>Canavalia ensiformis</italic>, <italic>T. foenumgraecum</italic>, <italic>Arachis hypogaea</italic>, <italic>Cajanus cajan</italic>, <italic>P. vulgaris</italic> and <italic>Pisum sativum</italic> were shown to inhibit biofilm formation by <italic>Streptococcus mutans</italic>, but the growth of planktonic cells was not affected [<xref rid="B89-ijms-18-01242" ref-type="bibr">89</xref>]. Since bacterial biofilms make disinfection procedures more difficult by increasing bacterial resistance to detergents and antibiotics, the inhibition of biofilm formation and development by legume lectins could be a useful characteristic of these proteins. Furthermore, the rapid evolution of bacteria with antibiotic resistance (in particular, multidrug resistant bacteria or superbugs) has reduced the efficacy of conventional treatments against their biofilms. Hence, development of non-antibiotic alternatives that could efficiently treat or reduce biofilms should become a priority. Furthermore, research focused on finding lectins that reduce superbugs could represent an interesting alternative drug therapy that deserves further attention.</p></sec><sec id="sec4dot2-ijms-18-01242"><title>4.2. Fungi and Yeasts</title><p>Regardless of the considerable number of lectins that have been characterized, only a small number have shown antifungal effects. Because plant lectins do not penetrate the cell wall or the membrane to reach the cytoplasm of fungi, direct inhibition of fungal growth by lectins is unlikely. In spite of this, indirect responses produced by the attachment of lectins to chitin and other glycans on the fungal surface could affect fungal survival or other activities [<xref rid="B105-ijms-18-01242" ref-type="bibr">105</xref>,<xref rid="B106-ijms-18-01242" ref-type="bibr">106</xref>].</p><p>Lectin binding to hyphae could result in inhibition of fungi growth as a result of poor nutrient absorption as well as by interference with the spore germination process [<xref rid="B107-ijms-18-01242" ref-type="bibr">107</xref>]. Lectins can cause different morphological changes that render fungi more vulnerable to differing stress conditions [<xref rid="B108-ijms-18-01242" ref-type="bibr">108</xref>]. For example, in one study, lectin interactions resulted in swollen hyphae, vacuolization of the cell content and improved lysis of hyphal cell wall, that, in turn, increased susceptibility of fungi to osmotic shock [<xref rid="B107-ijms-18-01242" ref-type="bibr">107</xref>]. In another case, it was suggested that small antifungal lectins could penetrate the fungal cell wall and reach the cell membrane where blocking of active sites of enzymes could alter cell wall morphogenesis [<xref rid="B108-ijms-18-01242" ref-type="bibr">108</xref>,<xref rid="B109-ijms-18-01242" ref-type="bibr">109</xref>].</p><p>Some reports indicate that lectins from the legumes <italic>Astragalus mongholicus</italic>, <italic>P. coccineus</italic>, <italic>Archidendron jiringa</italic> Nielsen, <italic>B. ungulata</italic>, <italic>Glycine max</italic>, <italic>Indigofera heterantha</italic> and <italic>A. hypogaea</italic> can exhibit antifungal activity against various species of phytopathogenic fungi, such as <italic>Botrytis cinerea</italic>, <italic>Fusarium oxysporum</italic>, <italic>F. moniliforme</italic>, <italic>F. solani</italic>, <italic>Colletorichum</italic> sp., <italic>Drechslera turcia</italic>, and <italic>Exserohilum turcicum</italic>, as well as pathogenic fungi such as <italic>Candida albicans</italic>, <italic>Penicillium italicummm</italic>, and <italic>Aspergillus</italic> sp. [<xref rid="B82-ijms-18-01242" ref-type="bibr">82</xref>,<xref rid="B91-ijms-18-01242" ref-type="bibr">91</xref>,<xref rid="B92-ijms-18-01242" ref-type="bibr">92</xref>,<xref rid="B93-ijms-18-01242" ref-type="bibr">93</xref>,<xref rid="B110-ijms-18-01242" ref-type="bibr">110</xref>,<xref rid="B111-ijms-18-01242" ref-type="bibr">111</xref>]. Additional studies are required to elucidate the molecular basis for the antifungal activity of individual lectins as the ability of lectins to inhibit growth differs among fungal species.</p></sec><sec id="sec4dot3-ijms-18-01242"><title>4.3. Virus</title><p>Plant lectins with antiviral activity are of substantial therapeutic interest. Some of these carbohydrate binding proteins exhibit significant activity against human immunodeficiency virus (HIV) and other viruses [<xref rid="B97-ijms-18-01242" ref-type="bibr">97</xref>]. Retroviruses, such as HIV, have a surface covered by highly glycosylated virally-encoded glycoproteins, e.g., gp120 (that contains high mannose and/or hybrid glycans) and gp41. The carbohydrates on these proteins are particularly important because the glycans can be used as tools to render the virus easily recognized by the immune system, and thus susceptible to immunological neutralization [<xref rid="B112-ijms-18-01242" ref-type="bibr">112</xref>]. The interactions between host and proteins from the viral envelop also can be altered by compounds that specifically recognize and bind glycans. Furthermore, lectins can crosslink surface viral glycans and thereby prevent interactions with other co-receptors [<xref rid="B83-ijms-18-01242" ref-type="bibr">83</xref>].</p><p>Antiviral lectins used as therapeutic agents offer lower toxicity and can be included in topical applications. Generally, lectins are odorless, and resistant to high temperatures and low pH, ideal properties for development of microbicide drugs [<xref rid="B86-ijms-18-01242" ref-type="bibr">86</xref>].</p><p>Most current antiviral therapeutics prevent the viral life cycle, or inhibit the entrance of the virus into host cells [<xref rid="B113-ijms-18-01242" ref-type="bibr">113</xref>]. The antiviral action of plant lectins varies extensively depending upon their carbohydrate specificity. Corona virus are highly susceptible to mannose specific lectins that interfere with the viral attachment in early phases of the replication cycle and suppress viral development by binding towards the end of the viral infection cycle [<xref rid="B114-ijms-18-01242" ref-type="bibr">114</xref>]. Other antiviral non-legume lectins with encouraging properties include griffithsin (GRFT), cyanovirin (CV-N) and banana lectin (BanLec), and BanLec has been recommended as an antiviral microbicide. Most often antiviral lectins are recommended for incorporation into vaginal and rectal gels, creams or suppositories that act as a barrier to prevent HIV transmission. In such processes, lectins bind the virus preventing its entry and fusion to target cells, consequently averting contamination [<xref rid="B115-ijms-18-01242" ref-type="bibr">115</xref>].</p><p>Several legume lectins possess antiviral activity. Lectins like <italic>C. ensiformis</italic> agglutinin (Con A), <italic>Lens culinaris</italic> agglutinin (LCA), <italic>Vicia faba</italic> agglutinin, <italic>P. sativum</italic> agglutinin (PSA) and PHA-E bind to the envelope glycoprotein gp120 and to inhibit fusion of HIV-infected cells with CD4 cells by a carbohydrate-specific interaction with the HIV-infected cells [<xref rid="B103-ijms-18-01242" ref-type="bibr">103</xref>]. In addition, <italic>G. max</italic> agglutinins inhibit HIV-1 reverse transcriptase activity [<xref rid="B116-ijms-18-01242" ref-type="bibr">116</xref>]. Although glycan structures of viral proteins involve high mannose, further research in this area is needed to explore lectins that recognize structures with different sugars such as sialic acid, fucose and <italic>N</italic>-acetyl glucosamine with the aim of developing novel approaches and therapies in the field of virus biology. </p></sec></sec><sec id="sec5-ijms-18-01242"><title>5. Insecticidal Activity</title><p>Legume lectins are toxic to a broad spectrum of insects representing several orders including, Coleoptera, Diptera, Lepidoptera, Hymenoptera, Isoptera, Neuroptera and Homoptera. In this regard, the family of leguminous lectins is the most studied due to its insecticidal potential. A great number of legume lectins have shown insecticidal activity including those from <italic>C. ensiformis</italic>, <italic>P. sativum</italic>, <italic>P. vulgaris</italic>, <italic>Glechoma hederacea</italic>, <italic>G. simplicifolia</italic>, <italic>O. tesota</italic> (PF2) and <italic>B. monandra</italic> [<xref rid="B8-ijms-18-01242" ref-type="bibr">8</xref>,<xref rid="B117-ijms-18-01242" ref-type="bibr">117</xref>,<xref rid="B118-ijms-18-01242" ref-type="bibr">118</xref>].</p><p>These lectins showed harmful effects in the different developmental stages of insects (larvae and adults). In this regard, they may increase mortality, delay development and/or adult emergence and reduce fecundity. Usually, the effect of lectins on insects is evaluated by feeding larvae with artificial seeds containing the lectin or with transgenic plants that overexpress the lectin of interest. The expression of a given lectin in transgenic plants is only possible if the lectin molecular sequence is well characterized and also requires an available transformation protocol for the desired plant species [<xref rid="B119-ijms-18-01242" ref-type="bibr">119</xref>].</p><p>In the last twenty years, research has focused on elucidating the mode of action of insecticidal lectins. In general, lectins can exert a toxic effect via binding to the peritrophic membrane (PM), peritrophic gel (PG) or the brush-border microvilli of epithelial cells (<xref ref-type="fig" rid="ijms-18-01242-f002">Figure 2</xref>) [<xref rid="B120-ijms-18-01242" ref-type="bibr">120</xref>]. The PM or PG is a film surrounding the food bolus in most insects and is composed of chitin and proteins. Some non-legume lectins with insecticidal activity such as the <italic>Rhizoctonia solani</italic> agglutinin and <italic>Sambucus nigra</italic> agglutinin II can pass through the PM of the red flour beetle, <italic>Tribolium castaneum</italic>. This ability to reach the endoperitrophic space is governed by the dimensions of the molecule and the charge and size of the PM pores [<xref rid="B121-ijms-18-01242" ref-type="bibr">121</xref>]. </p><p>In the case of insects lacking a PM, the insecticidal effect of lectins may be exerted by their direct interaction with glycoconjugates present on the cell epithelium [<xref rid="B122-ijms-18-01242" ref-type="bibr">122</xref>]. In fact, the insecticidal activity of lectins relies on their binding properties to sugars present on the surface of the insect gut epithelial cells. In insects, the surface of epithelial cells is rich in glycoproteins that, in addition to their determinant roles for the proper gut function, provide a number of available targets for lectin binding.</p><p>The interaction of lectins with different glycoproteins or glycan structures in insects may interfere with important physiological processes (<xref ref-type="table" rid="ijms-18-01242-t002">Table 2</xref>). Although the key receptors for lectins could be localized on the surface of gut epithelial cells, if lectins are internalized, they may interact with a new set of targets located in the intracellular space, allowing the lectin to interfere with particular metabolic pathways. Such internalization has been more studied for non-legume lectins. For example, the garlic leaf lectin, which affects survival and development of the moth <italic>Helicoverpa armigera</italic>, was found to be internalized by binding to a glycosylated alkaline phosphatase anchored to the insect midgut membrane. In addition, <italic>Galantus nivalis</italic> lectin was reported to cross the midgut epithelium of <italic>Nilaparvata lugens</italic> and co-localize in the fat body and hemolymph. Such co-localization was proposed to occur via a carrier-receptor, ferritin. The internalization of the <italic>Colocasia esculenta</italic> tuber agglutinin into insect hemolymph also was demonstrated, suggesting it could interact with various <italic>N</italic>-glycosylated intracellular targets, which may, in part, explain the lectin toxicity [<xref rid="B122-ijms-18-01242" ref-type="bibr">122</xref>]. Although the complete mechanism by which some lectins are able to cross midgut epithelial cells is not yet fully understood, available evidence has highlighted the implication of clathrin-mediated endocytosis as part of this process [<xref rid="B123-ijms-18-01242" ref-type="bibr">123</xref>,<xref rid="B124-ijms-18-01242" ref-type="bibr">124</xref>].</p><p>Regardless of the mechanisms involved in lectin interactions with insect cells, in order to be toxic, a lectin must avoid degradation by the digestive enzymes from the insect gut. The insecticidal effect of some lectins is attributed to the resistance of these proteins to proteolysis and to their properties of stability in a wide pH range. For example, PF2, an insecticidal lectin to <italic>Zabrotes subfasciatus</italic>, is resistant to in vitro proteolysis by insect digestive enzymes. This is in contrast to PHA-E lectin that is digested after 4 h of incubation with these enzymes, and therefore is not toxic for this insect [<xref rid="B8-ijms-18-01242" ref-type="bibr">8</xref>]. Other lectins with insecticidal activity that share the common feature of resistance to proteolysis by different digestive enzymes include, <italic>G. simplicifolia II</italic> lectin (GS II)<italic>, Ulex europeus</italic> agglutinin (UEA) and <italic>B. monandra</italic> lectin [<xref rid="B117-ijms-18-01242" ref-type="bibr">117</xref>,<xref rid="B118-ijms-18-01242" ref-type="bibr">118</xref>]. The degree of resistance to digestive enzymes depends on the capacity of the lectin to bind to glycoconjugates of the insect gut. GS II mutant lectins lacking the ability to bind carbohydrates displayed sensitivity to proteolysis by digestive enzymes with a consequent loss of toxicity [<xref rid="B125-ijms-18-01242" ref-type="bibr">125</xref>].</p><p>In summary, the insecticidal effect exhibited by several plant lectins is a complex phenomenon that relies on the capacity of the lectin to interfere with critical physiological processes during insect development. Such interference often may be mediated by a lack of nutrient absorption that occurs when midgut epithelial cells are atrophied as a result of the interaction of lectins with glyco-targets located either on the surface or inside the cell. Studies of the recognition of plant lectins by insect gut glyco-targets can allow one to develop hypotheses on which cellular pathways are affected by the insecticidal activity. These pathways vary depending on the type of insect and the lectin, and could be as diverse as the type of recognized glycan or receptors, and might include the effectors of energy metabolism, and redox and ionic homeostasis (summarized in <xref ref-type="table" rid="ijms-18-01242-t002">Table 2</xref>).</p><p>Finally, the study of potential non-yet-identified insecticidal plant lectins may contribute to the development of distinctive tools for sustainable pest control. However, in this regard, care must be taken considering the effect lectins might exert on beneficial insects as well.</p></sec><sec id="sec6-ijms-18-01242"><title>6. Antitumor Activity</title><p>Recently, an increased interest in the potential of plant lectins as cancer therapeutic agents has become evident. Lectins can be used to study the metastatic distribution patterns, the expression profiles of cancer cells glycoconjugates and their biological effects in various tumors. It is well known that carbohydrates present on the cell membrane are important for cell recognition, communication and adhesion. In cancer, these interactions are essential for tumor progression and metastasis. In tumor cells, glycosylation is generally altered in comparison with normal cells and these alterations can be detected by lectins [<xref rid="B135-ijms-18-01242" ref-type="bibr">135</xref>,<xref rid="B136-ijms-18-01242" ref-type="bibr">136</xref>]. Litynska et al. compared the lectin-binding pattern in different human melanoma cell lines using the PHA-L lectin and other non-legume lectins, including the <italic>Galanthus nivalis</italic> lectin, <italic>S. nigra</italic> lectin, MAL, <italic>Datura stramonium</italic> agglutinin and wheat germ agglutinin (WGA). Studies demonstrated that acquisition of metastatic potential of tumor cells is correlated with the expression of branched and sialylated complex <italic>N</italic>-oligosaccharides [<xref rid="B137-ijms-18-01242" ref-type="bibr">137</xref>]. Interestingly, the binding of MAL-I to gastric cancer cells was proportional to their metastatic capacity, and a high expression of α (2,3)-linked sialic acids was closely correlated with lymph node metastasis [<xref rid="B137-ijms-18-01242" ref-type="bibr">137</xref>]. Korourian et al. used <italic>G. simplicifolia</italic> lectin-I (GS I) and <italic>Vicia vilosa</italic> agglutinin (VVA) to establish an expression analysis of carbohydrate antigens in human breast ductal carcinoma in situ (DCIS). Both lectins showed a significant association with nuclear grade (cell size and uniformity) of DCIS [<xref rid="B138-ijms-18-01242" ref-type="bibr">138</xref>]. Positive correlations also were found between the expression of VVA- and GSI-reactive structures and tumor grade in DCIS patients, suggesting that the glycoconjugates found in these antigens are associated with invasiveness in DCIS [<xref rid="B138-ijms-18-01242" ref-type="bibr">138</xref>]. PHA can be used to discriminate between hepatocellular carcinoma and benign liver disease [<xref rid="B139-ijms-18-01242" ref-type="bibr">139</xref>]. This suggests that lectins could potentially be used to develop prognostic tools for cancer diagnosis and the detection of metastasis, and to some extent to estimate the severity of the clinical case. </p><p>In addition to these uses, plant lectins have shown in vivo and in vitro antitumor activity. Lectins with the potential to induce inhibition of tumor cell growth, such as, Con A, Mistletoe type-I lectins and PHA are currently in different phases of clinical trials [<xref rid="B138-ijms-18-01242" ref-type="bibr">138</xref>,<xref rid="B140-ijms-18-01242" ref-type="bibr">140</xref>]. Plant lectins can modify the expression of interleukins and some protein kinases and in this way modulate the immune system. Furthermore, in cancers, lectins could alter the signaling pathways involved in the expression of members of the Bcl-2, Autophagy (ATG) related, and caspase families, as well as p53, ERK, Ras-Raf, and BNIP3, and thereby induce both apoptosis and autophagy [<xref rid="B141-ijms-18-01242" ref-type="bibr">141</xref>]. Soybean lectin produces reactive oxygen species in a dose-dependent manner in HeLa cells inducing apoptosis, autophagy and DNA damage in the cells [<xref rid="B142-ijms-18-01242" ref-type="bibr">142</xref>].</p><p>The cell surface carbohydrates are key targets for lectins; in cancer, a general pathway involves recognition of carbohydrate receptors triggering the activation of enzymes such as MBL-associated serine proteases [<xref rid="B143-ijms-18-01242" ref-type="bibr">143</xref>]. However, the binding of lectins to glycans on the cell membrane may not be sufficient to induce apoptosis. Kim et al. showed that cell death requires lectin endocytosis that triggers signaling for apoptosis [<xref rid="B143-ijms-18-01242" ref-type="bibr">143</xref>]. Con A is cytotoxic to hepatoma cell lines. Its toxicity is mediated primarily by its binding to the mannose moiety of cell membrane glycoproteins, with subsequent internalization and accumulation in the mitochondria. Autophagy is then activated, leading to lysosomal degradation of the affected mitochondria and, ultimately, cell death [<xref rid="B144-ijms-18-01242" ref-type="bibr">144</xref>,<xref rid="B145-ijms-18-01242" ref-type="bibr">145</xref>]. Overall, these findings of cancer research have revealed the mechanisms responsible for the antitumor action of different plant lectins. These mechanisms are varied and depend upon different factors such as the tumor cell origin and type as well as lectin concentration.</p></sec><sec id="sec7-ijms-18-01242"><title>7. Conclusions</title><p>The screening and characterization of novel lectins from legume resources has allowed the discovery of proteins with a great capacity to distinguish specific glycans from a diversity of glyco-targets found in a variety of organisms. Legume lectins could be potential candidates for developing tools based on protein–carbohydrate interactions with variable specificities. Lectin-mediated drugs focused on targeting specific cells could lead to promising anticancer and antimicrobial treatments, which would directly impact areas of economic importance, such as the pharmaceutical and food industries and agriculture. Additionally, the use of lectins against insect pests could provide a form of sustainable pest control.</p><p>More research is needed to explore and support the therapeutic effect of lectins. Studies of action mechanisms, the relationship between the role of the lectins and their molecular features, and finally, their effect in modulating the expression of proteins and genes are required to move forward the use of lectins for clinical applications.</p><p>Domesticated legumes provide an accessible and abundant source of lectins, unlike wild legumes, which, in some regions, may even be considered protected species. In some cases, successful recombinant production of lectins would be a key factor in whether a specific lectin could find use in a feasible industrial application. The overexpression of recombinant lectins remains a great challenge, even more so for those lectins where the lack of adequate post-translational modifications could compromise their activity.</p></sec></body><back><ack><title>Acknowledgements</title><p>The authors thank Joy Winzerling for her critical reading and editing of the manuscript.</p></ack><notes><title>Author Contributions</title><p>All authors compiled the information, wrote the review, read and approved the final manuscript.</p></notes><notes notes-type="COI-statement"><title>Conflicts of Interest</title><p>The authors declare no conflict of interest.</p></notes><glossary><title>Abbreviations</title><array orientation="portrait"><tbody><tr><td align="left" valign="middle" rowspan="1" colspan="1">CRD</td><td align="left" valign="middle" rowspan="1" colspan="1">Carbohydrate recognition domain</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">PM</td><td align="left" valign="middle" rowspan="1" colspan="1">Peritrophic membrane</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">PG</td><td align="left" valign="middle" rowspan="1" colspan="1">Peritrophic gel</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">PHA</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Phaseolous vulgaris</italic> agglutinin</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">MAL-1</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Maackia amurensis</italic> lectin 1</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">DCIS</td><td align="left" valign="middle" rowspan="1" colspan="1">Human breast ductal carcinoma in situ</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">GS IV</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Griffonia simplicifolia</italic> IV lectin</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">MAH and MAL-1</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Maackia amurensis</italic> lectins</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">VLs</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Acacia constricta</italic> isolectins</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">WGA</td><td align="left" valign="middle" rowspan="1" colspan="1">Wheat germ agglutinin</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">LCA</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Lens culinaris</italic> agglutinin</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">PSA</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Pisum sativum</italic> agglutinin</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">GS II</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Griffonia simplicifolia</italic> II lectin</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">UEA</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Ulex europeus</italic> agglutinin</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">ASAI and ASAII</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Allium sativum</italic> L. bulbs</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">MuLL</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Myracrodruon urundeuva</italic> leaf lectin</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">BmoLL</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Bauhinia monandra</italic> leaf lectin</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">ASAL</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Allium sativum</italic> Leaf Agglutinin</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">CEA</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Colocasia esculenta</italic> tuber agglutinin</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">GS I</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Griffonia simplicifolia</italic> lectin-I</td></tr><tr><td align="left" valign="middle" rowspan="1" colspan="1">VVA</td><td align="left" valign="middle" rowspan="1" colspan="1"><italic>Vicia vilosa</italic> agglutinin</td></tr></tbody></array></glossary><ref-list><title>References</title><ref id="B1-ijms-18-01242"><label>1.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sharon</surname><given-names>N.</given-names></name><name><surname>Lis</surname><given-names>H.</given-names></name></person-group><article-title>History of lectins: From hemagglutinins to biological recognition molecules</article-title><source>Glycobiology</source><year>2004</year><volume>14</volume><fpage>53r</fpage><lpage>62r</lpage><pub-id pub-id-type="doi">10.1093/glycob/cwh122</pub-id><pub-id pub-id-type="pmid">15229195</pub-id></element-citation></ref><ref id="B2-ijms-18-01242"><label>2.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hamid</surname><given-names>R.</given-names></name><name><surname>Masood</surname><given-names>A.</given-names></name><name><surname>Wani</surname><given-names>I.H.</given-names></name><name><surname>Rafiq</surname><given-names>S.</given-names></name></person-group><article-title>Lectins: Proteins with diverse applications</article-title><source>J. Appl. Pharm. Sci.</source><year>2013</year><volume>3</volume><fpage>S93</fpage><lpage>S103</lpage></element-citation></ref><ref id="B3-ijms-18-01242"><label>3.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Loris</surname><given-names>R.</given-names></name><name><surname>Hamelryck</surname><given-names>T.</given-names></name><name><surname>Bouckaert</surname><given-names>J.</given-names></name><name><surname>Wyns</surname><given-names>L.</given-names></name></person-group><article-title>Legume lectin structure</article-title><source>BBA-Protein Struct. Mol. Enzymol.</source><year>1998</year><volume>1383</volume><fpage>9</fpage><lpage>36</lpage><pub-id pub-id-type="doi">10.1016/S0167-4838(97)00182-9</pub-id></element-citation></ref><ref id="B4-ijms-18-01242"><label>4.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sharon</surname><given-names>N.</given-names></name><name><surname>Lis</surname><given-names>H.</given-names></name></person-group><article-title>Legume lectins a large family of homologous proteins</article-title><source>FASEB J.</source><year>1990</year><volume>4</volume><fpage>3198</fpage><lpage>3208</lpage><pub-id pub-id-type="pmid">2227211</pub-id></element-citation></ref><ref id="B5-ijms-18-01242"><label>5.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Vázquez-Moreno</surname><given-names>L.</given-names></name><name><surname>Ortega-Nieblas</surname><given-names>M.</given-names></name><name><surname>Robles-Burgueño</surname><given-names>M.R.</given-names></name><name><surname>Ramos-Clamont</surname><given-names>G.</given-names></name></person-group><article-title>Purification of complex carbohydrate specific lectins from <italic>Olneya tesota</italic> seeds using tandem affinity chromatography</article-title><source>Int. J. Biochromatogr.</source><year>2000</year><volume>5</volume><fpage>83</fpage><lpage>90</lpage></element-citation></ref><ref id="B6-ijms-18-01242"><label>6.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Guzman-Partida</surname><given-names>A.M.</given-names></name><name><surname>Robles-Burgueno</surname><given-names>M.R.</given-names></name><name><surname>Ortega-Nieblas</surname><given-names>M.</given-names></name><name><surname>Vazquez-Moreno</surname><given-names>I.</given-names></name></person-group><article-title>Purification and characterization of complex carbohydrate specific isolectins from wild legume seeds: <italic>Acacia constricta</italic> is (vinorama) highly homologous to <italic>Phaseolus Vulgaris</italic> lectins</article-title><source>Biochimie</source><year>2004</year><volume>86</volume><fpage>335</fpage><lpage>342</lpage><pub-id pub-id-type="doi">10.1016/j.biochi.2004.02.005</pub-id><pub-id pub-id-type="pmid">15194238</pub-id></element-citation></ref><ref id="B7-ijms-18-01242"><label>7.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Nasi</surname><given-names>A.</given-names></name><name><surname>Picariello</surname><given-names>G.</given-names></name><name><surname>Ferranti</surname><given-names>P.</given-names></name></person-group><article-title>Proteomic approaches to study structure, functions and toxicity of legume seeds lectins. Perspectives for the assessment of food quality and safety</article-title><source>J. Proteom.</source><year>2009</year><volume>72</volume><fpage>527</fpage><lpage>538</lpage><pub-id pub-id-type="doi">10.1016/j.jprot.2009.02.001</pub-id><pub-id pub-id-type="pmid">19217948</pub-id></element-citation></ref><ref id="B8-ijms-18-01242"><label>8.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lagarda-Diaz</surname><given-names>I.</given-names></name><name><surname>Guzman-Partida</surname><given-names>A.M.</given-names></name><name><surname>Urbano-Hernandez</surname><given-names>G.</given-names></name><name><surname>Ortega-Neblas</surname><given-names>M.M.</given-names></name><name><surname>Robles-Burgueno</surname><given-names>M.R.</given-names></name><name><surname>Winzerling</surname><given-names>J.</given-names></name><name><surname>Vazquez-Moreno</surname><given-names>L.</given-names></name></person-group><article-title>Insecticidal action of PF2 lectin from <italic>Olneya tesota</italic> (palo fierro) against Zabrotes subfasciatus larvae and midgut glycoconjugate binding</article-title><source>J. Agric. Food Chem.</source><year>2009</year><volume>57</volume><fpage>689</fpage><lpage>694</lpage><pub-id pub-id-type="doi">10.1021/jf802557m</pub-id><pub-id pub-id-type="pmid">19102651</pub-id></element-citation></ref><ref id="B9-ijms-18-01242"><label>9.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sharma</surname><given-names>V.</given-names></name><name><surname>Surolia</surname><given-names>A.</given-names></name></person-group><article-title>Analyses of carbohydrate recognition by legume lectins: Size of the combining site loops and their primary specificity</article-title><source>J. Mol. Biol.</source><year>1997</year><volume>267</volume><fpage>433</fpage><lpage>445</lpage><pub-id pub-id-type="doi">10.1006/jmbi.1996.0863</pub-id><pub-id pub-id-type="pmid">9096236</pub-id></element-citation></ref><ref id="B10-ijms-18-01242"><label>10.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hamelryck</surname><given-names>T.W.</given-names></name><name><surname>Loris</surname><given-names>R.</given-names></name><name><surname>Bouckaert</surname><given-names>J.</given-names></name><name><surname>Doa-Thi</surname><given-names>M.H.</given-names></name><name><surname>Strecker</surname><given-names>G.</given-names></name><name><surname>Imberty</surname><given-names>A.</given-names></name><name><surname>Fernandez</surname><given-names>E.</given-names></name><name><surname>Wyns</surname><given-names>L.</given-names></name><name><surname>Etzer</surname><given-names>M.E.</given-names></name></person-group><article-title>Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from <italic>Dolichos biflorus</italic></article-title><source>J. Mol. Biol.</source><year>1999</year><volume>288</volume><fpage>1037</fpage><pub-id pub-id-type="doi">10.1006/jmbi.1999.2799</pub-id><pub-id pub-id-type="pmid">10329197</pub-id></element-citation></ref><ref id="B11-ijms-18-01242"><label>11.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Vijayan</surname><given-names>M.</given-names></name><name><surname>Chandra</surname><given-names>N.</given-names></name></person-group><article-title>Lectins</article-title><source>Curr. Opin. Struct. Biol.</source><year>1999</year><volume>9</volume><fpage>707</fpage><lpage>714</lpage><pub-id pub-id-type="doi">10.1016/S0959-440X(99)00034-2</pub-id><pub-id pub-id-type="pmid">10607664</pub-id></element-citation></ref><ref id="B12-ijms-18-01242"><label>12.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sharon</surname><given-names>N.</given-names></name><name><surname>Lis</surname><given-names>H.</given-names></name></person-group><article-title>How proteins bind carbohydrates: Lessons from legume lectins</article-title><source>J. Agric. Food Chem.</source><year>2002</year><volume>50</volume><fpage>6586</fpage><lpage>6591</lpage><pub-id pub-id-type="doi">10.1021/jf020190s</pub-id><pub-id pub-id-type="pmid">12381156</pub-id></element-citation></ref><ref id="B13-ijms-18-01242"><label>13.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hamelryck</surname><given-names>T.W.</given-names></name><name><surname>Loris</surname><given-names>R.</given-names></name><name><surname>Bouckaert</surname><given-names>J.</given-names></name><name><surname>Wyns</surname><given-names>L.</given-names></name></person-group><article-title>Structural features of the legume lectins</article-title><source>Trends Glycosci. Glycotechnol.</source><year>1998</year><volume>10</volume><fpage>349</fpage><lpage>360</lpage><pub-id pub-id-type="doi">10.4052/tigg.10.349</pub-id></element-citation></ref><ref id="B14-ijms-18-01242"><label>14.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Bouckaert</surname><given-names>J.</given-names></name><name><surname>Hamelryck</surname><given-names>T.</given-names></name><name><surname>Wyns</surname><given-names>L.</given-names></name><name><surname>Loris</surname><given-names>R.</given-names></name></person-group><article-title>Novel structures of plant lectins and their complexes with carbohydrates</article-title><source>Curr. Opin. Struct. Biol.</source><year>1999</year><volume>9</volume><fpage>572</fpage><lpage>577</lpage><pub-id pub-id-type="doi">10.1016/S0959-440X(99)00007-X</pub-id><pub-id pub-id-type="pmid">10508764</pub-id></element-citation></ref><ref id="B15-ijms-18-01242"><label>15.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Buts</surname><given-names>L.</given-names></name><name><surname>Dao-Thi</surname><given-names>M.H.</given-names></name><name><surname>Loris</surname><given-names>R.</given-names></name><name><surname>Wyns</surname><given-names>L.</given-names></name><name><surname>Etzler</surname><given-names>M.</given-names></name><name><surname>Hamelryck</surname><given-names>T.</given-names></name></person-group><article-title>Weak protein–protein interactions in lectins: The crystal structure of a vegetative lectin from the legume Dolichos biflorus</article-title><source>J. Mol. Biol.</source><year>2001</year><volume>309</volume><fpage>193</fpage><lpage>201</lpage><pub-id pub-id-type="doi">10.1006/jmbi.2001.4639</pub-id><pub-id pub-id-type="pmid">11491289</pub-id></element-citation></ref><ref id="B16-ijms-18-01242"><label>16.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Brinda</surname><given-names>K.V.</given-names></name><name><surname>Mitra</surname><given-names>N.</given-names></name><name><surname>Surolia</surname><given-names>A.</given-names></name><name><surname>Vishveshwara</surname><given-names>S.</given-names></name></person-group><article-title>Determinants of quaternary association in legume lectins</article-title><source>Protein Sci.</source><year>2004</year><volume>13</volume><fpage>1735</fpage><lpage>1749</lpage><pub-id pub-id-type="doi">10.1110/ps.04651004</pub-id><pub-id pub-id-type="pmid">15215518</pub-id></element-citation></ref><ref id="B17-ijms-18-01242"><label>17.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Etzler</surname><given-names>M.E.</given-names></name><name><surname>Surolia</surname><given-names>A.</given-names></name><name><surname>Cummings</surname><given-names>R.D.</given-names></name></person-group><article-title>L-type lectins</article-title><source>Essentials of Glycobiology</source><edition>2nd ed.</edition><person-group person-group-type="editor"><name><surname>Varki</surname><given-names>A.</given-names></name><name><surname>Cummings</surname><given-names>R.</given-names></name><name><surname>Esko</surname><given-names>J.</given-names></name><name><surname>Freeze</surname><given-names>H.</given-names></name><name><surname>Stanley</surname><given-names>P.</given-names></name><name><surname>Bertozzi</surname><given-names>C.</given-names></name><name><surname>Hart</surname><given-names>G.</given-names></name><name><surname>Etzler</surname><given-names>M.</given-names></name></person-group><publisher-name>Cold Spring Harbor Laboratory Press</publisher-name><publisher-loc>New York, NY, USA</publisher-loc><year>2009</year><comment>Chapter 28</comment><fpage>403</fpage><lpage>414</lpage></element-citation></ref><ref id="B18-ijms-18-01242"><label>18.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ambrosi</surname><given-names>M.</given-names></name><name><surname>Cameron</surname><given-names>N.R.</given-names></name><name><surname>Davis</surname><given-names>B.G.</given-names></name></person-group><article-title>Lectins: Tools for the molecular understanding of the glycocode</article-title><source>Org. Biomol. Chem.</source><year>2005</year><volume>3</volume><fpage>1593</fpage><lpage>1608</lpage><pub-id pub-id-type="doi">10.1039/b414350g</pub-id><pub-id pub-id-type="pmid">15858635</pub-id></element-citation></ref><ref id="B19-ijms-18-01242"><label>19.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Manoj</surname><given-names>N.</given-names></name><name><surname>Suguna</surname><given-names>K.</given-names></name></person-group><article-title>Signature of quaternary structure in the sequences of legume lectins</article-title><source>Protein Eng.</source><year>2001</year><volume>14</volume><fpage>735</fpage><lpage>745</lpage><pub-id pub-id-type="doi">10.1093/protein/14.10.735</pub-id><pub-id pub-id-type="pmid">11739891</pub-id></element-citation></ref><ref id="B20-ijms-18-01242"><label>20.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Rudiger</surname><given-names>H.</given-names></name><name><surname>Gabius</surname><given-names>H.J.</given-names></name></person-group><article-title>Plant lectins: Occurrence, biochemistry, functions and applications</article-title><source>Glycoconj. J.</source><year>2001</year><volume>18</volume><fpage>589</fpage><lpage>613</lpage><pub-id pub-id-type="doi">10.1023/A:1020687518999</pub-id><pub-id pub-id-type="pmid">12376725</pub-id></element-citation></ref><ref id="B21-ijms-18-01242"><label>21.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Felsted</surname><given-names>R.L.</given-names></name><name><surname>Leavitt</surname><given-names>R.D.</given-names></name><name><surname>Bachur</surname><given-names>N.R.</given-names></name></person-group><article-title>Purification of the phytohemagglutinin family of proteins from red kidney beans (<italic>Phaseolus vulgaris</italic>) by affinity chromatography</article-title><source>Biochim. Biophys. Acta</source><year>1975</year><volume>405</volume><fpage>72</fpage><lpage>81</lpage><pub-id pub-id-type="doi">10.1016/0005-2795(75)90316-5</pub-id><pub-id pub-id-type="pmid">1174570</pub-id></element-citation></ref><ref id="B22-ijms-18-01242"><label>22.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Felsted</surname><given-names>R.L.</given-names></name><name><surname>Li</surname><given-names>J.</given-names></name><name><surname>Pokrywka</surname><given-names>G.</given-names></name><name><surname>Egorin</surname><given-names>M.J.</given-names></name><name><surname>Spiegel</surname><given-names>J.</given-names></name><name><surname>Dale</surname><given-names>R.M.</given-names></name></person-group><article-title>Comparison of <italic>Phaseolus vulgaris</italic> cultivars on the basis of isolectin differences</article-title><source>Int. J. Biochem.</source><year>1981</year><volume>13</volume><fpage>549</fpage><lpage>557</lpage><pub-id pub-id-type="doi">10.1016/0020-711X(81)90179-8</pub-id><pub-id pub-id-type="pmid">7238987</pub-id></element-citation></ref><ref id="B23-ijms-18-01242"><label>23.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Cummings</surname><given-names>R.D.</given-names></name><name><surname>Kornfeld</surname><given-names>S.</given-names></name></person-group><article-title>Characterization of the structural determinants required for the high affinity interaction of asparagine-linked oligosaccharides with immobilized <italic>Phaseolus vulgaris</italic> leukoagglutinating and erythroagglutinating lectins</article-title><source>J. Biol. Chem.</source><year>1982</year><volume>257</volume><fpage>11230</fpage><lpage>11234</lpage><pub-id pub-id-type="pmid">7118880</pub-id></element-citation></ref><ref id="B24-ijms-18-01242"><label>24.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Fleischmann</surname><given-names>G.</given-names></name><name><surname>Mauder</surname><given-names>I.</given-names></name><name><surname>Illert</surname><given-names>W.</given-names></name><name><surname>Rudiger</surname><given-names>H.</given-names></name></person-group><article-title>A one-step procedure for isolation and resolution of the <italic>Phaseolus vulgaris</italic> isolectins by affinity-chromatography</article-title><source>Biol. Chem. Hoppe-Seyler</source><year>1985</year><volume>366</volume><fpage>1029</fpage><lpage>1032</lpage><pub-id pub-id-type="doi">10.1515/bchm3.1985.366.2.1029</pub-id><pub-id pub-id-type="pmid">4074496</pub-id></element-citation></ref><ref id="B25-ijms-18-01242"><label>25.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hamelryck</surname><given-names>T.W.</given-names></name><name><surname>DaoThi</surname><given-names>M.H.</given-names></name><name><surname>Poortmans</surname><given-names>F.</given-names></name><name><surname>Chrispeels</surname><given-names>M.J.</given-names></name><name><surname>Wyns</surname><given-names>L.</given-names></name><name><surname>Loris</surname><given-names>R.</given-names></name></person-group><article-title>The crystallographic structure of phytohemagglutinin-l</article-title><source>J. Biol. Chem.</source><year>1996</year><volume>271</volume><fpage>20479</fpage><lpage>20485</lpage><pub-id pub-id-type="doi">10.1074/jbc.271.34.20479</pub-id><pub-id pub-id-type="pmid">8702788</pub-id></element-citation></ref><ref id="B26-ijms-18-01242"><label>26.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Nagae</surname><given-names>M.</given-names></name><name><surname>Soga</surname><given-names>K.</given-names></name><name><surname>Morita-Matsumoto</surname><given-names>K.</given-names></name><name><surname>Hanashima</surname><given-names>S.</given-names></name><name><surname>Ikeda</surname><given-names>A.</given-names></name><name><surname>Yamamoto</surname><given-names>K.</given-names></name><name><surname>Yamaguchi</surname><given-names>Y.</given-names></name></person-group><article-title>Phytohemagglutinin from <italic>Phaseolus vulgaris</italic> (PHA-E) displays a novel glycan recognition mode using a common legume lectin fold</article-title><source>Glycobiology</source><year>2014</year><volume>24</volume><fpage>368</fpage><lpage>378</lpage><pub-id pub-id-type="doi">10.1093/glycob/cwu004</pub-id><pub-id pub-id-type="pmid">24436051</pub-id></element-citation></ref><ref id="B27-ijms-18-01242"><label>27.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Pérez</surname><given-names>S.</given-names></name><name><surname>Sarkar</surname><given-names>A.</given-names></name><name><surname>Rivet</surname><given-names>A.</given-names></name><name><surname>Breton</surname><given-names>C.</given-names></name><name><surname>Imberty</surname><given-names>A.</given-names></name></person-group><article-title>Glyco3d: A portal for structural glycosciences</article-title><source>Glycoinformatics</source><year>2015</year><volume>1273</volume><fpage>241</fpage><lpage>258</lpage></element-citation></ref><ref id="B28-ijms-18-01242"><label>28.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Bouckaert</surname><given-names>J.</given-names></name><name><surname>Loris</surname><given-names>R.</given-names></name><name><surname>Poortmans</surname><given-names>F.</given-names></name><name><surname>Wyns</surname><given-names>L.</given-names></name></person-group><article-title>Crystallographic structure of metal-free concanavalin a at 2.5 angstrom resolution</article-title><source>Proteins</source><year>1995</year><volume>23</volume><fpage>510</fpage><lpage>524</lpage><pub-id pub-id-type="doi">10.1002/prot.340230406</pub-id><pub-id pub-id-type="pmid">8749847</pub-id></element-citation></ref><ref id="B29-ijms-18-01242"><label>29.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Loris</surname><given-names>R.</given-names></name><name><surname>Casset</surname><given-names>F.</given-names></name><name><surname>Bouckaert</surname><given-names>J.</given-names></name><name><surname>Pletinckx</surname><given-names>J.</given-names></name><name><surname>Daothi</surname><given-names>M.H.</given-names></name><name><surname>Poortmans</surname><given-names>F.</given-names></name><name><surname>Imberty</surname><given-names>A.</given-names></name><name><surname>Perez</surname><given-names>S.</given-names></name><name><surname>Wyns</surname><given-names>L.</given-names></name></person-group><article-title>The monosaccharide binding-site of lentil lectin: An X-ray and molecular modeling study</article-title><source>Glycoconj. J.</source><year>1994</year><volume>11</volume><fpage>507</fpage><lpage>517</lpage><pub-id pub-id-type="doi">10.1007/BF00731301</pub-id><pub-id pub-id-type="pmid">7696853</pub-id></element-citation></ref><ref id="B30-ijms-18-01242"><label>30.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ruzheinikov</surname><given-names>S.N.</given-names></name><name><surname>Mikhailova</surname><given-names>I.Y.</given-names></name><name><surname>Tsygannik</surname><given-names>I.N.</given-names></name><name><surname>Pangborn</surname><given-names>W.</given-names></name><name><surname>Duax</surname><given-names>W.</given-names></name><name><surname>Pletnev</surname><given-names>V.Z.</given-names></name></person-group><article-title>The structure of the pea lectin-<sc>d</sc>-mannopyranose complex at a 2.1 angstrom resolution</article-title><source>Bioorganicheskaya Khimiya</source><year>1998</year><volume>24</volume><fpage>313</fpage><lpage>315</lpage></element-citation></ref><ref id="B31-ijms-18-01242"><label>31.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Babino</surname><given-names>A.</given-names></name><name><surname>Tello</surname><given-names>D.</given-names></name><name><surname>Rojas</surname><given-names>A.</given-names></name><name><surname>Bay</surname><given-names>S.</given-names></name><name><surname>Osinaga</surname><given-names>E.</given-names></name><name><surname>Alzari</surname><given-names>P.M.</given-names></name></person-group><article-title>The crystal structure of a plant lectin in complex with the Tn antigen</article-title><source>FEBS. Lett.</source><year>2003</year><volume>536</volume><fpage>106</fpage><lpage>110</lpage><pub-id pub-id-type="doi">10.1016/S0014-5793(03)00037-1</pub-id><pub-id pub-id-type="pmid">12586347</pub-id></element-citation></ref><ref id="B32-ijms-18-01242"><label>32.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Imberty</surname><given-names>A.</given-names></name><name><surname>Gohier</surname><given-names>A.</given-names></name><name><surname>Jordan</surname><given-names>E.</given-names></name><name><surname>Goldstein</surname><given-names>I.J.</given-names></name><name><surname>Perez</surname><given-names>S.</given-names></name></person-group><article-title>Molecular modeling of native and mutated lima bean lectin: Dissection of lectin/blood group a trisaccharide interactions</article-title><source>Internet J. Chem.</source><year>1998</year><volume>1</volume><fpage>10</fpage></element-citation></ref><ref id="B33-ijms-18-01242"><label>33.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Felger</surname><given-names>R.S.</given-names></name><name><surname>Nabhan</surname><given-names>G.P.</given-names></name></person-group><article-title>Agroecosystem diversity: A model from the Sonoran Desert</article-title><source>Social and Technological Management in the Dry Lands, American Association for the Advancement of Sciences (AAAS) Selected Symposium 10</source><person-group person-group-type="editor"><name><surname>Gonzalez</surname><given-names>N.L.</given-names></name></person-group><publisher-name>Westview Press</publisher-name><publisher-loc>Boulder, CO, USA</publisher-loc><year>1978</year><fpage>128</fpage><lpage>149</lpage></element-citation></ref><ref id="B34-ijms-18-01242"><label>34.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Sousa</surname><given-names>M.</given-names></name><name><surname>Delgado</surname><given-names>A.</given-names></name></person-group><article-title>Mexican leguminosae: Phytogeography, endemism, and origins</article-title><source>Biological Diversity of Mexico: Origins and Distribution</source><publisher-name>Oxford University Press</publisher-name><publisher-loc>New York, NY, USA</publisher-loc><year>1993</year><fpage>459</fpage><lpage>511</lpage></element-citation></ref><ref id="B35-ijms-18-01242"><label>35.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Sousa</surname><given-names>S.M.</given-names></name><name><surname>Medina</surname><given-names>R.L.</given-names></name><name><surname>Andrade</surname><given-names>G.</given-names></name><name><surname>Rico</surname><given-names>M.L.</given-names></name></person-group><article-title>Leguminosas</article-title><source>Biodiversidad de Oaxaca</source><person-group person-group-type="editor"><name><surname>García</surname><given-names>A.</given-names></name><name><surname>Diaz</surname><given-names>M.</given-names></name><name><surname>Briones</surname><given-names>M.</given-names></name></person-group><publisher-name>Instituto de Biología, Universidad Nacional Autónoma de México, Fondo Oaxaqueño para la Conservación de la Naturaleza, World Wildlife Fund</publisher-name><publisher-loc>México, D.F., México</publisher-loc><year>2004</year><fpage>249</fpage><lpage>269</lpage></element-citation></ref><ref id="B36-ijms-18-01242"><label>36.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Ortega-Nieblas</surname><given-names>M.M.</given-names></name></person-group><article-title>Estudio de Algunas Semillas de Leguminosas del Desierto de Sonora. Factores Antinutricionales y Calidad de sus Proteínas y Aceites</article-title><source>Master’s Thesis</source><publisher-name>Centro de Investigación en Alimentación y Desarrollo, A.C.</publisher-name><publisher-loc>Sonora, México</publisher-loc><year>1993</year></element-citation></ref><ref id="B37-ijms-18-01242"><label>37.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Felipe-Ortega</surname><given-names>X.</given-names></name></person-group><article-title>Aislamiento y Caracterización de las Lectinas de Leguminosas Silvestres del Desierto de Sonora: <italic>Cercidium praecox</italic> (palo de brea) y <italic>Caesalpinia caladenia</italic> (palo dorado)</article-title><source>Bachelor´s Thesis</source><publisher-name>Universidad de Sonora</publisher-name><publisher-loc>Sonora, México</publisher-loc><month>8</month><year>1996</year></element-citation></ref><ref id="B38-ijms-18-01242"><label>38.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>López-Laredo</surname><given-names>A.R.</given-names></name></person-group><article-title>Caracterización de los oligosacáridos de las lectinas de <italic>Olneya tesota</italic> pf2 y su isoforma más abundante (IF2) y establecer la relación con la función de reconocimiento</article-title><source>Master´s Thesis</source><publisher-name>Centro de Investigación en Alimentación y Desarrollo, A.C.</publisher-name><publisher-loc>Sonora, México</publisher-loc><month>5</month><year>2005</year></element-citation></ref><ref id="B39-ijms-18-01242"><label>39.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Félix-Favela</surname><given-names>F.</given-names></name></person-group><article-title>Isoformas de la lectina PF2, Características Moleculares y Reconocimiento de Leucocitos de Sangre Periférica de Adultos</article-title><source>Master´s Thesis</source><publisher-name>Centro de Investigación en Alimentación y Desarrollo, A.C.</publisher-name><publisher-loc>Sonora, México</publisher-loc><month>4</month><year>2009</year></element-citation></ref><ref id="B40-ijms-18-01242"><label>40.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Quirós-Quintero</surname><given-names>C.E.</given-names></name></person-group><article-title>Purificación y Caracterización de la Lectina de Prosopis Juliflora y Evaluación del Desarrollo Larval de Zabrotes Subfasciatus en las Semillas</article-title><source>Bachelor´s Thesis</source><publisher-name>Universidad de la Sierra</publisher-name><publisher-loc>Sonora, México</publisher-loc><month>2</month><year>2010</year></element-citation></ref><ref id="B41-ijms-18-01242"><label>41.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Valadez-Vega</surname><given-names>C.</given-names></name><name><surname>Guzmán-Partida</surname><given-names>A.M.</given-names></name><name><surname>Soto-Cordova</surname><given-names>F.J.</given-names></name><name><surname>Álvarez-Manilla</surname><given-names>G.</given-names></name><name><surname>Morales-González</surname><given-names>J.A.</given-names></name><name><surname>Madrigal-Santillán</surname><given-names>E.</given-names></name><name><surname>Villagómez-Ibarra</surname><given-names>J.R.</given-names></name><name><surname>Zúñiga-Pérez</surname><given-names>C.</given-names></name><name><surname>Gutiérrez-Salinas</surname><given-names>J.</given-names></name><name><surname>Becerril-Flores</surname><given-names>M.A.</given-names></name></person-group><article-title>Purification, biochemical characterization, and bioactive properties of a lectin purified from the seeds of white tepary bean (Phaseolus acutifolius variety latifolius)</article-title><source>Molecules</source><year>2011</year><volume>16</volume><fpage>2561</fpage><lpage>2582</lpage><pub-id pub-id-type="doi">10.3390/molecules16032561</pub-id><pub-id pub-id-type="pmid">21441861</pub-id></element-citation></ref><ref id="B42-ijms-18-01242"><label>42.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Guzmán-Partida</surname><given-names>A.</given-names></name><name><surname>Félix-Favela</surname><given-names>F.</given-names></name><name><surname>Mata-Haro</surname><given-names>V.</given-names></name><name><surname>Lopez-Laredo</surname><given-names>A.</given-names></name><name><surname>Urbano-Hernández</surname><given-names>G.</given-names></name><name><surname>Robles-Burgueño</surname><given-names>M.</given-names></name><name><surname>Candia-Plata</surname><given-names>M.</given-names></name><name><surname>Vázquez-Moreno</surname><given-names>L.</given-names></name></person-group><article-title>Identificación de la interacción de monocitos humanos con las lectinas de <italic>Olneya tesota</italic> (IF2) y <italic>Phaseolus vulgaris</italic> (PHA-L) por citometría de flujo</article-title><source>Biotecnia</source><year>2013</year><volume>15</volume><fpage>3</fpage><lpage>7</lpage><pub-id pub-id-type="doi">10.18633/bt.v15i3.151</pub-id></element-citation></ref><ref id="B43-ijms-18-01242"><label>43.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Miller</surname><given-names>J.B.</given-names></name><name><surname>Noyes</surname><given-names>C.</given-names></name><name><surname>Heinrikson</surname><given-names>R.</given-names></name><name><surname>Kingdon</surname><given-names>H.S.</given-names></name><name><surname>Yachnin</surname><given-names>S.</given-names></name></person-group><article-title>Phytohemagglutinin mitogenic proteins. Structural evidence for a family of isomitogenic proteins</article-title><source>J. Exp. Med.</source><year>1973</year><volume>138</volume><fpage>939</fpage><lpage>951</lpage><pub-id pub-id-type="doi">10.1084/jem.138.4.939</pub-id><pub-id pub-id-type="pmid">4744013</pub-id></element-citation></ref><ref id="B44-ijms-18-01242"><label>44.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Leavitt</surname><given-names>R.D.</given-names></name><name><surname>Felsted</surname><given-names>R.L.</given-names></name><name><surname>Bachur</surname><given-names>N.R.</given-names></name></person-group><article-title>Biological and biochemical properties of <italic>Phaseolus vulgaris</italic> isolectins</article-title><source>J. Biol. Chem.</source><year>1977</year><volume>252</volume><fpage>2961</fpage><lpage>2966</lpage><pub-id pub-id-type="pmid">853039</pub-id></element-citation></ref><ref id="B45-ijms-18-01242"><label>45.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Roberts</surname><given-names>D.D.</given-names></name><name><surname>Etzler</surname><given-names>M.E.</given-names></name><name><surname>Goldstein</surname><given-names>I.J.</given-names></name></person-group><article-title>Subunit heterogeneity in the lima bean lectin</article-title><source>J. Biol. Chem.</source><year>1982</year><volume>257</volume><fpage>9198</fpage><lpage>9204</lpage><pub-id pub-id-type="pmid">7096360</pub-id></element-citation></ref><ref id="B46-ijms-18-01242"><label>46.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sparvoli</surname><given-names>F.</given-names></name><name><surname>Lanave</surname><given-names>C.</given-names></name><name><surname>Santucci</surname><given-names>A.</given-names></name><name><surname>Bollini</surname><given-names>R.</given-names></name><name><surname>Lioi</surname><given-names>L.</given-names></name></person-group><article-title>Lectin and lectin-related proteins in lima bean (<italic>Phaseolus lunatus</italic> L.) seeds: Biochemical and evolutionary studies</article-title><source>Plant Mol. Biol.</source><year>2001</year><volume>45</volume><fpage>587</fpage><lpage>597</lpage><pub-id pub-id-type="doi">10.1023/A:1010647310311</pub-id><pub-id pub-id-type="pmid">11414617</pub-id></element-citation></ref><ref id="B47-ijms-18-01242"><label>47.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Castillo-Villanueva</surname><given-names>A.</given-names></name><name><surname>Caballero-Ortega</surname><given-names>H.</given-names></name><name><surname>Abdullaev-Jafarova</surname><given-names>F.</given-names></name><name><surname>Garfias</surname><given-names>Y.</given-names></name><name><surname>Jimenez-Martinez</surname><given-names>M.D.C.</given-names></name><name><surname>Bouquelet</surname><given-names>S.</given-names></name><name><surname>Martinez</surname><given-names>G.</given-names></name><name><surname>Mendoza-Hernandez</surname><given-names>G.</given-names></name><name><surname>Zenteno</surname><given-names>E.</given-names></name></person-group><article-title>Lectin from Phaseolus acutifolius var. Escumite: Chemical characterization, sugar specificity, and effect on human T-lymphocytes</article-title><source>J. Agric. Food Chem.</source><year>2007</year><volume>55</volume><fpage>5781</fpage><lpage>5787</lpage><pub-id pub-id-type="doi">10.1021/jf063644k</pub-id><pub-id pub-id-type="pmid">17567024</pub-id></element-citation></ref><ref id="B48-ijms-18-01242"><label>48.</label><element-citation publication-type="other"><person-group person-group-type="author"><name><surname>Vazquez-Moreno</surname><given-names>L.</given-names></name></person-group><article-title>Analysis of <italic>Olneya tesota</italic> lectin peptides with liquid chromatography in two dimensions and tandem mass spectrometry (LC–MS/MS)</article-title><comment>Manuscript in preparation</comment><year>2017</year></element-citation></ref><ref id="B49-ijms-18-01242"><label>49.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hoffman</surname><given-names>L.M.</given-names></name><name><surname>Donaldson</surname><given-names>D.D.</given-names></name></person-group><article-title>Characterization of 2 <italic>Phaseolus</italic>-vugaris phytohemagglutinin genes closely linked on the chromosome</article-title><source>EMBO J.</source><year>1985</year><volume>4</volume><fpage>883</fpage><lpage>889</lpage><pub-id pub-id-type="pmid">2990911</pub-id></element-citation></ref><ref id="B50-ijms-18-01242"><label>50.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lioi</surname><given-names>L.</given-names></name><name><surname>Sparvoli</surname><given-names>F.</given-names></name><name><surname>Galasso</surname><given-names>I.</given-names></name><name><surname>Lanave</surname><given-names>C.</given-names></name><name><surname>Bollini</surname><given-names>R.</given-names></name></person-group><article-title>Lectin-related resistance factors against bruchids evolved through a number of duplication events</article-title><source>Theor. Appl. Genet.</source><year>2003</year><volume>107</volume><fpage>814</fpage><lpage>822</lpage><pub-id pub-id-type="doi">10.1007/s00122-003-1343-8</pub-id><pub-id pub-id-type="pmid">12819911</pub-id></element-citation></ref><ref id="B51-ijms-18-01242"><label>51.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Karnchanatat</surname><given-names>A.</given-names></name></person-group><article-title>Antimicrobial activity of lectins from antimicrobial activity of lectins from plants</article-title><source>Antimicrobial Agents</source><person-group person-group-type="editor"><name><surname>Bobbarala</surname><given-names>V.</given-names></name></person-group><publisher-name>InTech</publisher-name><publisher-loc>Rijeka, Croatia</publisher-loc><year>2012</year><fpage>145</fpage><lpage>177</lpage></element-citation></ref><ref id="B52-ijms-18-01242"><label>52.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Grandhi</surname><given-names>N.J.</given-names></name><name><surname>Mamidi</surname><given-names>A.S.</given-names></name><name><surname>Surolia</surname><given-names>A.</given-names></name></person-group><article-title>Pattern recognition in legume lectins to extrapolate amino acid variability to sugar specificity</article-title><source>Biochemical Roles of Eukaryotic Cell Surface Macromolecules</source><person-group person-group-type="editor"><name><surname>Chakrabarti</surname><given-names>A.</given-names></name><name><surname>Surolia</surname><given-names>A.</given-names></name></person-group><publisher-name>Springer International Publishing</publisher-name><publisher-loc>Cham, Switzerland</publisher-loc><year>2015</year><fpage>199</fpage><lpage>215</lpage></element-citation></ref><ref id="B53-ijms-18-01242"><label>53.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Cruz</surname><given-names>P.H.</given-names></name><name><surname>Campos</surname><given-names>E.P.</given-names></name><name><surname>Martínez</surname><given-names>L.M.</given-names></name><name><surname>Ortiz</surname><given-names>B.</given-names></name><name><surname>Martínez</surname><given-names>G.</given-names></name></person-group><article-title>Las lectinas vegetales como modelo de estudio de las interacciones proteína-carbohidrato</article-title><source>Revista de Educación Bioquímica</source><year>2005</year><volume>24</volume><fpage>21</fpage><lpage>27</lpage></element-citation></ref><ref id="B54-ijms-18-01242"><label>54.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sharon</surname><given-names>N.</given-names></name></person-group><article-title>Lectin-carbohydrate complexes of plants and animals: An atomic view</article-title><source>Trends Biochem. Sci.</source><year>1993</year><volume>18</volume><fpage>221</fpage><lpage>226</lpage><pub-id pub-id-type="doi">10.1016/0968-0004(93)90193-Q</pub-id><pub-id pub-id-type="pmid">8346557</pub-id></element-citation></ref><ref id="B55-ijms-18-01242"><label>55.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Imberty</surname><given-names>A.</given-names></name><name><surname>Casset</surname><given-names>F.</given-names></name><name><surname>Gegg</surname><given-names>C.V.</given-names></name><name><surname>Etzler</surname><given-names>M.E.</given-names></name><name><surname>Perez</surname><given-names>S.</given-names></name></person-group><article-title>Molecular modeling of the <italic>Dolichos</italic>-<italic>biflorus</italic> seed lectin and its specific interactions with carbohydrates: α-<sc>D</sc>N-Acetyl-Galactosamine, Forssman disaccharide and blood-group-a trisaccharide</article-title><source>Glycoconj. J.</source><year>1994</year><volume>11</volume><fpage>400</fpage><lpage>413</lpage><pub-id pub-id-type="doi">10.1007/BF00731275</pub-id><pub-id pub-id-type="pmid">7696844</pub-id></element-citation></ref><ref id="B56-ijms-18-01242"><label>56.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Young</surname><given-names>N.M.</given-names></name><name><surname>Oomen</surname><given-names>R.P.</given-names></name></person-group><article-title>Analysis of sequence variation among legume lectins: A ring of hypervariable residues forms the perimeter of the carbohydrate-binding site</article-title><source>J. Mol. Biol.</source><year>1992</year><volume>228</volume><fpage>924</fpage><lpage>934</lpage><pub-id pub-id-type="doi">10.1016/0022-2836(92)90875-K</pub-id><pub-id pub-id-type="pmid">1469724</pub-id></element-citation></ref><ref id="B57-ijms-18-01242"><label>57.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Benevides</surname><given-names>R.G.</given-names></name><name><surname>Ganne</surname><given-names>G.</given-names></name><name><surname>Simoes Rda</surname><given-names>C.</given-names></name><name><surname>Schubert</surname><given-names>V.</given-names></name><name><surname>Niemietz</surname><given-names>M.</given-names></name><name><surname>Unverzagt</surname><given-names>C.</given-names></name><name><surname>Chazalet</surname><given-names>V.</given-names></name><name><surname>Breton</surname><given-names>C.</given-names></name><name><surname>Varrot</surname><given-names>A.</given-names></name><name><surname>Cavada</surname><given-names>B.S.</given-names></name><etal></etal></person-group><article-title>A lectin from Platypodium elegans with unusual specificity and affinity for asymmetric complex <italic>N</italic>-glycans</article-title><source>J. Biol. Chem.</source><year>2012</year><volume>287</volume><fpage>26352</fpage><lpage>26364</lpage><pub-id pub-id-type="doi">10.1074/jbc.M112.375816</pub-id><pub-id pub-id-type="pmid">22692206</pub-id></element-citation></ref><ref id="B58-ijms-18-01242"><label>58.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Singha</surname><given-names>S.</given-names></name><name><surname>Bose</surname><given-names>P.P.</given-names></name><name><surname>Ganguly</surname><given-names>T.</given-names></name><name><surname>Campana</surname><given-names>P.T.</given-names></name><name><surname>Ghosh</surname><given-names>R.</given-names></name><name><surname>Chatterjee</surname><given-names>B.P.</given-names></name></person-group><article-title>Comparison of the nature of interactions of two sialic acid specific lectins <italic>Saraca indica</italic> and Sambucus nigra with <italic>N</italic>-acetylneuraminic acid by spectroscopic techniques</article-title><source>J. Lumin.</source><year>2015</year><volume>160</volume><fpage>119</fpage><lpage>127</lpage><pub-id pub-id-type="doi">10.1016/j.jlumin.2014.11.041</pub-id></element-citation></ref><ref id="B59-ijms-18-01242"><label>59.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Chrispeels</surname><given-names>M.J.</given-names></name><name><surname>Raikhel</surname><given-names>N.V.</given-names></name></person-group><article-title>Lectins, lectin genes, and their role in plant defense</article-title><source>Plant Cell</source><year>1991</year><volume>3</volume><fpage>1</fpage><lpage>9</lpage><pub-id pub-id-type="doi">10.1105/tpc.3.1.1</pub-id><pub-id pub-id-type="pmid">1824332</pub-id></element-citation></ref><ref id="B60-ijms-18-01242"><label>60.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Peumans</surname><given-names>W.J.</given-names></name><name><surname>Van Damme</surname><given-names>E.</given-names></name></person-group><article-title>Lectins as plant defense proteins</article-title><source>Plant Physiol.</source><year>1995</year><volume>109</volume><fpage>347</fpage><pub-id pub-id-type="doi">10.1104/pp.109.2.347</pub-id><pub-id pub-id-type="pmid">7480335</pub-id></element-citation></ref><ref id="B61-ijms-18-01242"><label>61.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Delbaere</surname><given-names>L.T.J.</given-names></name><name><surname>Vandonselaar</surname><given-names>M.</given-names></name><name><surname>Prasad</surname><given-names>L.</given-names></name><name><surname>Quail</surname><given-names>J.W.</given-names></name><name><surname>Wilson</surname><given-names>K.S.</given-names></name><name><surname>Dauter</surname><given-names>Z.</given-names></name></person-group><article-title>Structures of the lectin-iv of <italic>Griffonia simplicifolia</italic> and its complex with the Lewis b human blood-group determinant at 2.0-angstrom resolution</article-title><source>J. Mol. Biol.</source><year>1993</year><volume>230</volume><fpage>950</fpage><lpage>965</lpage><pub-id pub-id-type="doi">10.1006/jmbi.1993.1212</pub-id><pub-id pub-id-type="pmid">8478943</pub-id></element-citation></ref><ref id="B62-ijms-18-01242"><label>62.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Imberty</surname><given-names>A.</given-names></name><name><surname>Gautier</surname><given-names>C.</given-names></name><name><surname>Lescar</surname><given-names>J.</given-names></name><name><surname>Perez</surname><given-names>S.</given-names></name><name><surname>Wyns</surname><given-names>L.</given-names></name></person-group><article-title>An unusual carbohydrate binding site revealed by the structures of two <italic>Maackia amurensis</italic> lectins complexed with sialic acid-containing oligosaccharides</article-title><source>J. Biol. Chem.</source><year>2000</year><volume>275</volume><fpage>17541</fpage><lpage>17548</lpage><pub-id pub-id-type="doi">10.1074/jbc.M000560200</pub-id><pub-id pub-id-type="pmid">10747930</pub-id></element-citation></ref><ref id="B63-ijms-18-01242"><label>63.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kolberg</surname><given-names>J.</given-names></name><name><surname>Michaelsen</surname><given-names>T.E.</given-names></name><name><surname>Sletten</surname><given-names>K.</given-names></name></person-group><article-title>Properties of a lectin purified from the seeds of <italic>Cicer</italic>-<italic>arietinum</italic></article-title><source>Hope-Seyler’s Z. Physiol. Chem.</source><year>1983</year><volume>364</volume><fpage>655</fpage><lpage>664</lpage><pub-id pub-id-type="doi">10.1515/bchm2.1983.364.1.655</pub-id><pub-id pub-id-type="pmid">6884991</pub-id></element-citation></ref><ref id="B64-ijms-18-01242"><label>64.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ray</surname><given-names>S.</given-names></name><name><surname>Chatterjee</surname><given-names>B.P.</given-names></name></person-group><article-title>Saracin a lectin from saraca-indica seed integument recognizes complex carbohydrates</article-title><source>Phytochem.</source><year>1995</year><volume>40</volume><fpage>643</fpage><lpage>649</lpage><pub-id pub-id-type="doi">10.1016/0031-9422(95)98168-G</pub-id></element-citation></ref><ref id="B65-ijms-18-01242"><label>65.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Irimura</surname><given-names>T.</given-names></name><name><surname>Tsuji</surname><given-names>T.</given-names></name><name><surname>Tagami</surname><given-names>S.</given-names></name><name><surname>Yamamoto</surname><given-names>K.</given-names></name><name><surname>Osawa</surname><given-names>T.</given-names></name></person-group><article-title>Structure of a complex-type sugar chain of human <italic>glycophorin</italic> A</article-title><source>Biochemistry</source><year>1981</year><volume>20</volume><fpage>560</fpage><lpage>566</lpage><pub-id pub-id-type="doi">10.1021/bi00506a018</pub-id><pub-id pub-id-type="pmid">7213594</pub-id></element-citation></ref><ref id="B66-ijms-18-01242"><label>66.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hammarstrom</surname><given-names>S.</given-names></name><name><surname>Hammarstrom</surname><given-names>M.L.</given-names></name><name><surname>Sundblad</surname><given-names>G.</given-names></name><name><surname>Arnarp</surname><given-names>J.</given-names></name><name><surname>Lonngren</surname><given-names>J.</given-names></name></person-group><article-title>Mitogenic leukoagglutinin from <italic>Phaseolus</italic>-<italic>vulgaris</italic> binds to a pentasaccharide unit in <italic>N</italic>-acetyllactosamine-type glycoprotein glycans</article-title><source>Proc. Natl. Acad. Sci. USA</source><year>1982</year><volume>79</volume><fpage>1611</fpage><lpage>1615</lpage><pub-id pub-id-type="doi">10.1073/pnas.79.5.1611</pub-id><pub-id pub-id-type="pmid">6951200</pub-id></element-citation></ref><ref id="B67-ijms-18-01242"><label>67.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Yamashita</surname><given-names>K.</given-names></name><name><surname>Hitoi</surname><given-names>A.</given-names></name><name><surname>Kobata</surname><given-names>A.</given-names></name></person-group><article-title>Structural determinants of <italic>Phaseolus</italic>-<italic>vulgaris</italic> erythroagglutinating lectin for oligosaccharides</article-title><source>J. Biol. Chem.</source><year>1983</year><volume>258</volume><fpage>4753</fpage><lpage>4755</lpage></element-citation></ref><ref id="B68-ijms-18-01242"><label>68.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kamemura</surname><given-names>K.</given-names></name><name><surname>Furuichi</surname><given-names>Y.</given-names></name><name><surname>Umekawa</surname><given-names>H.</given-names></name><name><surname>Takahashi</surname><given-names>T.</given-names></name></person-group><article-title>Purification and characterization of novel lectins from great northern bean, <italic>Phaseolus vulgaris</italic> L.</article-title><source>BBA-Gen. Subj.</source><year>1993</year><volume>1158</volume><fpage>181</fpage><lpage>188</lpage><pub-id pub-id-type="doi">10.1016/0304-4165(93)90012-W</pub-id></element-citation></ref><ref id="B69-ijms-18-01242"><label>69.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kaneda</surname><given-names>Y.</given-names></name><name><surname>Whittier</surname><given-names>R.F.</given-names></name><name><surname>Yamanaka</surname><given-names>H.</given-names></name><name><surname>Carredano</surname><given-names>E.</given-names></name><name><surname>Gotoh</surname><given-names>M.</given-names></name><name><surname>Sota</surname><given-names>H.</given-names></name><name><surname>Hasegawa</surname><given-names>Y.</given-names></name><name><surname>Shinohara</surname><given-names>Y.</given-names></name></person-group><article-title>The high specificities of <italic>Phaseolus vulgaris</italic> erythro- and leukoagglutinating lectins for bisecting GlcNac or beta 1–6-linked branch structures, respectively, are attributable to loop B</article-title><source>J. Biol. Chem.</source><year>2002</year><volume>277</volume><fpage>16928</fpage><lpage>16935</lpage><pub-id pub-id-type="doi">10.1074/jbc.M112382200</pub-id><pub-id pub-id-type="pmid">11864980</pub-id></element-citation></ref><ref id="B70-ijms-18-01242"><label>70.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Takeya</surname><given-names>A.</given-names></name><name><surname>Hosomi</surname><given-names>O.</given-names></name><name><surname>Nishijima</surname><given-names>H.</given-names></name><name><surname>Ohe</surname><given-names>Y.</given-names></name><name><surname>Sugahara</surname><given-names>K.</given-names></name><name><surname>Sagi</surname><given-names>M.</given-names></name><name><surname>Yamazaki</surname><given-names>K.</given-names></name><name><surname>Hayakawa</surname><given-names>H.</given-names></name><name><surname>Takeshita</surname><given-names>H.</given-names></name><name><surname>Sasaki</surname><given-names>C.</given-names></name><etal></etal></person-group><article-title>Presence of beta-linked GalNac residues on <italic>N</italic>-glycans of human thyroglobulin</article-title><source>Life Sci.</source><year>2007</year><volume>80</volume><fpage>538</fpage><lpage>545</lpage><pub-id pub-id-type="doi">10.1016/j.lfs.2006.10.004</pub-id><pub-id pub-id-type="pmid">17097689</pub-id></element-citation></ref><ref id="B71-ijms-18-01242"><label>71.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Rinderle</surname><given-names>S.J.</given-names></name><name><surname>Goldstein</surname><given-names>I.J.</given-names></name><name><surname>Matta</surname><given-names>K.L.</given-names></name><name><surname>Ratcliffe</surname><given-names>R.M.</given-names></name></person-group><article-title>Isolation and characterization of amaranthin, a lectin present in the seeds of Amaranthus-caudatus, that recognizes the T-antigen (or cryptic-T)-antigen</article-title><source>J. Biol. Chem.</source><year>1989</year><volume>264</volume><fpage>16123</fpage><lpage>16131</lpage><pub-id pub-id-type="pmid">2777780</pub-id></element-citation></ref><ref id="B72-ijms-18-01242"><label>72.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ramos</surname><given-names>M.V.</given-names></name><name><surname>Sampaio</surname><given-names>A.H.</given-names></name><name><surname>Cavada</surname><given-names>B.S.</given-names></name><name><surname>Calvete</surname><given-names>J.J.</given-names></name><name><surname>Grangeiro</surname><given-names>T.B.</given-names></name><name><surname>Debray</surname><given-names>H.</given-names></name></person-group><article-title>Characterization of the sugar-binding specificity of the toxic lectins isolated from <italic>Abrus pulchellus</italic> seeds</article-title><source>Glycoconj. J.</source><year>2001</year><volume>18</volume><fpage>391</fpage><lpage>400</lpage><pub-id pub-id-type="doi">10.1023/A:1014812114450</pub-id><pub-id pub-id-type="pmid">11925506</pub-id></element-citation></ref><ref id="B73-ijms-18-01242"><label>73.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Iskratsch</surname><given-names>T.</given-names></name><name><surname>Braun</surname><given-names>A.</given-names></name><name><surname>Paschinger</surname><given-names>K.</given-names></name><name><surname>Wilson</surname><given-names>I.B.H.</given-names></name></person-group><article-title>Specificity analysis of lectins and antibodies using remodeled glycoproteins</article-title><source>Anal. Biochem.</source><year>2009</year><volume>386</volume><fpage>133</fpage><lpage>146</lpage><pub-id pub-id-type="doi">10.1016/j.ab.2008.12.005</pub-id><pub-id pub-id-type="pmid">19123999</pub-id></element-citation></ref><ref id="B74-ijms-18-01242"><label>74.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Gomes</surname><given-names>F.S.</given-names></name><name><surname>Procopio</surname><given-names>T.F.</given-names></name><name><surname>Napoleao</surname><given-names>T.H.</given-names></name><name><surname>Coelho</surname><given-names>L.C.</given-names></name><name><surname>Paiva</surname><given-names>P.M.</given-names></name></person-group><article-title>Antimicrobial lectin from Schinus terebinthifolius leaf</article-title><source>J. Appl. Microbiol.</source><year>2013</year><volume>114</volume><fpage>672</fpage><lpage>679</lpage><pub-id pub-id-type="doi">10.1111/jam.12086</pub-id><pub-id pub-id-type="pmid">23190078</pub-id></element-citation></ref><ref id="B75-ijms-18-01242"><label>75.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Marchaim</surname><given-names>D.</given-names></name><name><surname>Lemanek</surname><given-names>L.</given-names></name><name><surname>Bheemreddy</surname><given-names>S.</given-names></name><name><surname>Kaye</surname><given-names>K.S.</given-names></name><name><surname>Sobel</surname><given-names>J.D.</given-names></name></person-group><article-title>Fluconazole-resistant Candida albicans vulvovaginitis</article-title><source>Obstet. Gynecol.</source><year>2012</year><volume>120</volume><fpage>1407</fpage><lpage>1414</lpage><pub-id pub-id-type="doi">10.1097/AOG.0b013e31827307b2</pub-id><pub-id pub-id-type="pmid">23168767</pub-id></element-citation></ref><ref id="B76-ijms-18-01242"><label>76.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Yim</surname><given-names>N.-H.</given-names></name><name><surname>Jung</surname><given-names>Y.P.</given-names></name><name><surname>Cho</surname><given-names>W.-K.</given-names></name><name><surname>Kim</surname><given-names>T.</given-names></name><name><surname>Kim</surname><given-names>A.</given-names></name><name><surname>Im</surname><given-names>M.</given-names></name><name><surname>Ma</surname><given-names>J.Y.</given-names></name></person-group><article-title>Screening of aqueous extracts of medicinal herbs for antimicrobial activity against oral bacteria</article-title><source>Integr. Med. Res.</source><year>2013</year><volume>2</volume><fpage>18</fpage><lpage>24</lpage><pub-id pub-id-type="doi">10.1016/j.imr.2013.02.002</pub-id></element-citation></ref><ref id="B77-ijms-18-01242"><label>77.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Srivastava</surname><given-names>P.</given-names></name><name><surname>Upreti</surname><given-names>D.K.</given-names></name><name><surname>Dhole</surname><given-names>T.N.</given-names></name><name><surname>Srivastava</surname><given-names>A.K.</given-names></name><name><surname>Nayak</surname><given-names>M.T.</given-names></name></person-group><article-title>Antimicrobial property of extracts of Indian lichen against human pathogenic bacteria</article-title><source>Interdiscip. Perspect. Infect. Dis.</source><year>2013</year><volume>2013</volume><fpage>709348</fpage><pub-id pub-id-type="doi">10.1155/2013/709348</pub-id><pub-id pub-id-type="pmid">24062769</pub-id></element-citation></ref><ref id="B78-ijms-18-01242"><label>78.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Davies</surname><given-names>J.</given-names></name><name><surname>Davies</surname><given-names>D.</given-names></name></person-group><article-title>Origins and evolution of antibiotic resistance</article-title><source>Microbiol. Mol. Biol. Rev.</source><year>2010</year><volume>74</volume><fpage>417</fpage><lpage>433</lpage><pub-id pub-id-type="doi">10.1128/MMBR.00016-10</pub-id><pub-id pub-id-type="pmid">20805405</pub-id></element-citation></ref><ref id="B79-ijms-18-01242"><label>79.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>De Brito Marques Ramos</surname><given-names>D.</given-names></name><name><surname>Gomes</surname><given-names>F.S.</given-names></name><name><surname>Napoleão</surname><given-names>T.H.</given-names></name><name><surname>Paiva</surname><given-names>P.M.G.</given-names></name><name><surname>da Silva</surname><given-names>M.D.C.</given-names></name><name><surname>Barroso Coelho</surname><given-names>L.C.B.</given-names></name></person-group><article-title>Antimicrobial activity of <italic>Cladonia verticillaris</italic> lichen preparations on bacteria and fungi of medical importance</article-title><source>Chin. J. Biol.</source><year>2014</year><volume>2014</volume><pub-id pub-id-type="doi">10.1155/2014/219392</pub-id></element-citation></ref><ref id="B80-ijms-18-01242"><label>80.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Broekaert</surname><given-names>W.F.</given-names></name><name><surname>Cammue</surname><given-names>B.P.A.</given-names></name><name><surname>DeBolle</surname><given-names>M.F.C.</given-names></name><name><surname>Thevissen</surname><given-names>K.</given-names></name><name><surname>DeSamblanx</surname><given-names>G.W.</given-names></name><name><surname>Osborn</surname><given-names>R.W.</given-names></name></person-group><article-title>Antimicrobial peptides from plants</article-title><source>Crit. Rev. Plant Sci.</source><year>1997</year><volume>16</volume><fpage>297</fpage><lpage>323</lpage><pub-id pub-id-type="doi">10.1080/07352689709701952</pub-id></element-citation></ref><ref id="B81-ijms-18-01242"><label>81.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lehrer</surname><given-names>R.I.</given-names></name><name><surname>Ganz</surname><given-names>T.</given-names></name></person-group><article-title>Antimicrobial peptides in mammalian and insect host defence</article-title><source>Curr. Opin. Immunol.</source><year>1999</year><volume>11</volume><fpage>23</fpage><lpage>27</lpage><pub-id pub-id-type="doi">10.1016/S0952-7915(99)80005-3</pub-id><pub-id pub-id-type="pmid">10047545</pub-id></element-citation></ref><ref id="B82-ijms-18-01242"><label>82.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sharon</surname><given-names>N.</given-names></name><name><surname>Lis</surname><given-names>H.</given-names></name></person-group><article-title>The structural basis for carbohydrate recognition by lectins</article-title><source>Adv. Exp. Med. Biol.</source><year>2001</year><volume>491</volume><fpage>1</fpage><lpage>16</lpage><pub-id pub-id-type="pmid">14533786</pub-id></element-citation></ref><ref id="B83-ijms-18-01242"><label>83.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Charungchitrak</surname><given-names>S.</given-names></name><name><surname>Petsom</surname><given-names>A.</given-names></name><name><surname>Sangvanich</surname><given-names>P.</given-names></name><name><surname>Karnchanatat</surname><given-names>A.</given-names></name></person-group><article-title>Antifungal and antibacterial activities of lectin from the seeds of <italic>Archidendron jiringa</italic> Nielsen</article-title><source>Food Chem.</source><year>2011</year><volume>126</volume><fpage>1025</fpage><lpage>1032</lpage><pub-id pub-id-type="doi">10.1016/j.foodchem.2010.11.114</pub-id></element-citation></ref><ref id="B84-ijms-18-01242"><label>84.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Bah</surname><given-names>C.S.F.</given-names></name><name><surname>Fang</surname><given-names>E.F.</given-names></name><name><surname>Ng</surname><given-names>T.B.</given-names></name></person-group><article-title>Medicinal applications of plant lectins</article-title><source>Antitumor Potential and Other Emerging Medicinal Properties of Natural Compounds</source><person-group person-group-type="editor"><name><surname>Fang</surname><given-names>E.</given-names></name><name><surname>Tzi</surname><given-names>B.</given-names></name></person-group><publisher-name>Springer International Publishing</publisher-name><publisher-loc>Dordrecht, The Netherlands</publisher-loc><year>2013</year><fpage>55</fpage><lpage>74</lpage></element-citation></ref><ref id="B85-ijms-18-01242"><label>85.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Oliveira</surname><given-names>M.D.L.</given-names></name><name><surname>Andrade</surname><given-names>C.A.S.</given-names></name><name><surname>Santos-Magalhaes</surname><given-names>N.S.</given-names></name><name><surname>Coelho</surname><given-names>L.C.B.B.</given-names></name><name><surname>Teixeira</surname><given-names>J.A.</given-names></name><name><surname>Carneiro-Da-Cunha</surname><given-names>M.G.</given-names></name><name><surname>Correia</surname><given-names>M.T.S.</given-names></name></person-group><article-title>Purification of a lectin from <italic>Eugenia uniflora</italic> L. seeds and its potential antibacterial activity</article-title><source>Lett. Appl. Microbiol.</source><year>2008</year><volume>46</volume><fpage>371</fpage><lpage>376</lpage><pub-id pub-id-type="doi">10.1111/j.1472-765X.2007.02319.x</pub-id><pub-id pub-id-type="pmid">18266644</pub-id></element-citation></ref><ref id="B86-ijms-18-01242"><label>86.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sammour</surname><given-names>R.H.</given-names></name><name><surname>El-Shanshoury</surname><given-names>A.</given-names></name></person-group><article-title>Antimicrobial activity of legume seed proteins</article-title><source>Bot. Bull. Acad. Sin.</source><year>1992</year><volume>31</volume><fpage>185</fpage><lpage>190</lpage></element-citation></ref><ref id="B87-ijms-18-01242"><label>87.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ayouba</surname><given-names>A.</given-names></name><name><surname>Causse</surname><given-names>H.</given-names></name><name><surname>Vandamme</surname><given-names>E.J.M.</given-names></name><name><surname>Peumans</surname><given-names>W.J.</given-names></name><name><surname>Bourne</surname><given-names>Y.</given-names></name><name><surname>Cambillau</surname><given-names>C.</given-names></name><name><surname>Rouge</surname><given-names>P.</given-names></name></person-group><article-title>Interactions of plant-lectins with the components of the bacterial-cell wall peptidoglycan</article-title><source>Biochem. Syst. Ecol.</source><year>1994</year><volume>22</volume><fpage>153</fpage><lpage>159</lpage><pub-id pub-id-type="doi">10.1016/0305-1978(94)90005-1</pub-id></element-citation></ref><ref id="B88-ijms-18-01242"><label>88.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Santi-Gadelha</surname><given-names>T.</given-names></name><name><surname>Rocha</surname><given-names>B.A.M.</given-names></name><name><surname>Gadelha</surname><given-names>C.A.A.</given-names></name><name><surname>Silva</surname><given-names>H.C.</given-names></name><name><surname>Castellon</surname><given-names>R.E.R.</given-names></name><name><surname>Goncalves</surname><given-names>F.J.T.</given-names></name><name><surname>Toyama</surname><given-names>D.O.</given-names></name><name><surname>Toyama</surname><given-names>M.H.</given-names></name><name><surname>de Souza</surname><given-names>A.J.F.</given-names></name><name><surname>Beriam</surname><given-names>L.O.S.</given-names></name><etal></etal></person-group><article-title>Effects of a lectin-like protein isolated from <italic>Acacia Farnesiana</italic> seeds on phytopathogenic bacterial strains and root-knot nematode</article-title><source>Pestic. Biochem. Phys.</source><year>2012</year><volume>103</volume><fpage>15</fpage><lpage>22</lpage><pub-id pub-id-type="doi">10.1016/j.pestbp.2012.02.003</pub-id></element-citation></ref><ref id="B89-ijms-18-01242"><label>89.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Islam</surname><given-names>B.</given-names></name><name><surname>Khan</surname><given-names>A.U.</given-names></name></person-group><article-title>Lectins: To combat infections</article-title><source>Protein Purification</source><person-group person-group-type="editor"><name><surname>Ahmad</surname><given-names>R.</given-names></name></person-group><publisher-name>InTech</publisher-name><publisher-loc>Rijeka, Croatia</publisher-loc><year>2012</year><fpage>167</fpage><lpage>188</lpage></element-citation></ref><ref id="B90-ijms-18-01242"><label>90.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Bourne</surname><given-names>Y.</given-names></name><name><surname>Ayouba</surname><given-names>A.</given-names></name><name><surname>Rouge</surname><given-names>P.</given-names></name><name><surname>Cambillau</surname><given-names>C.</given-names></name></person-group><article-title>Interaction of a legume lectin with two components of the bacterial cell wall. A crystallographic study</article-title><source>J. Biol. Chem.</source><year>1994</year><volume>269</volume><fpage>9429</fpage><lpage>9435</lpage><pub-id pub-id-type="pmid">8144527</pub-id></element-citation></ref><ref id="B91-ijms-18-01242"><label>91.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Qadir</surname><given-names>S.</given-names></name><name><surname>Wani</surname><given-names>I.H.</given-names></name><name><surname>Rafiq</surname><given-names>S.</given-names></name><name><surname>Ganie</surname><given-names>S.A.</given-names></name><name><surname>Masood</surname><given-names>A.</given-names></name><name><surname>Hamid</surname><given-names>R.</given-names></name></person-group><article-title>Evaluation of antimicrobial activity of a lectin isolated and purified from <italic>Indigofera Heterantha</italic></article-title><source>Adv. Biosci. Biotechnol.</source><year>2013</year><volume>4</volume><fpage>999</fpage><pub-id pub-id-type="doi">10.4236/abb.2013.411133</pub-id></element-citation></ref><ref id="B92-ijms-18-01242"><label>92.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Yan</surname><given-names>Q.J.</given-names></name><name><surname>Jiang</surname><given-names>Z.Q.</given-names></name><name><surname>Yang</surname><given-names>S.Q.</given-names></name><name><surname>Deng</surname><given-names>W.</given-names></name><name><surname>Han</surname><given-names>L.J.</given-names></name></person-group><article-title>A novel homodimeric lectin from <italic>Astragalus Mongholicus</italic> with antifungal activity</article-title><source>Arch. Biochem. Biophys.</source><year>2005</year><volume>442</volume><fpage>72</fpage><lpage>81</lpage><pub-id pub-id-type="doi">10.1016/j.abb.2005.07.019</pub-id><pub-id pub-id-type="pmid">16140255</pub-id></element-citation></ref><ref id="B93-ijms-18-01242"><label>93.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Chen</surname><given-names>J.</given-names></name><name><surname>Liu</surname><given-names>B.</given-names></name><name><surname>Ji</surname><given-names>N.</given-names></name><name><surname>Zhou</surname><given-names>J.</given-names></name><name><surname>Bian</surname><given-names>H.J.</given-names></name><name><surname>Li</surname><given-names>C.Y.</given-names></name><name><surname>Chen</surname><given-names>F.</given-names></name><name><surname>Bao</surname><given-names>J.K.</given-names></name></person-group><article-title>A novel sialic acid-specific lectin from Phaseolus coccineus seeds with potent antineoplastic and antifungal activities</article-title><source>Phytomedicine</source><year>2009</year><volume>16</volume><fpage>352</fpage><lpage>360</lpage><pub-id pub-id-type="doi">10.1016/j.phymed.2008.07.003</pub-id><pub-id pub-id-type="pmid">18757189</pub-id></element-citation></ref><ref id="B94-ijms-18-01242"><label>94.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Silva</surname><given-names>H.C.</given-names></name><name><surname>Pinto</surname><given-names>L.D.</given-names></name><name><surname>Teixeira</surname><given-names>E.H.</given-names></name><name><surname>Nascimento</surname><given-names>K.S.</given-names></name><name><surname>Cavada</surname><given-names>B.S.</given-names></name><name><surname>Silva</surname><given-names>A.L.C.</given-names></name></person-group><article-title>Bul: A novel lectin from <italic>Bauhinia Ungulata</italic> L. Seeds with fungistatic and antiproliferative activities</article-title><source>Process. Biochem.</source><year>2014</year><volume>49</volume><fpage>203</fpage><lpage>209</lpage><pub-id pub-id-type="doi">10.1016/j.procbio.2013.10.020</pub-id></element-citation></ref><ref id="B95-ijms-18-01242"><label>95.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Barkai-Golan</surname><given-names>R.</given-names></name><name><surname>Mirelman</surname><given-names>D.</given-names></name><name><surname>Sharon</surname><given-names>N.</given-names></name></person-group><article-title>Studies on growth inhibition by lectins of penicillia and aspergilli</article-title><source>Arch. Microbiol.</source><year>1978</year><volume>116</volume><fpage>119</fpage><lpage>121</lpage><pub-id pub-id-type="doi">10.1007/BF00406026</pub-id><pub-id pub-id-type="pmid">637658</pub-id></element-citation></ref><ref id="B96-ijms-18-01242"><label>96.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ye</surname><given-names>X.Y.</given-names></name><name><surname>Ng</surname><given-names>T.B.</given-names></name><name><surname>Tsang</surname><given-names>P.W.K.</given-names></name><name><surname>Wang</surname><given-names>J.</given-names></name></person-group><article-title>Isolation of a homodimeric lectin with antifungal and antiviral activities from red kidney bean (<italic>Phaseolus vulgaris</italic>) seeds</article-title><source>J. Protein Chem.</source><year>2001</year><volume>20</volume><fpage>367</fpage><lpage>375</lpage><pub-id pub-id-type="doi">10.1023/A:1012276619686</pub-id><pub-id pub-id-type="pmid">11732688</pub-id></element-citation></ref><ref id="B97-ijms-18-01242"><label>97.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Leal</surname><given-names>A.F.</given-names></name><name><surname>Lopes</surname><given-names>N.E.</given-names></name><name><surname>Clark</surname><given-names>A.T.</given-names></name><name><surname>de Pontes Filho</surname><given-names>N.T.</given-names></name><name><surname>Beltrao</surname><given-names>E.I.</given-names></name><name><surname>Neves</surname><given-names>R.P.</given-names></name></person-group><article-title>Carbohydrate profiling of fungal cell wall surface glycoconjugates of Aspergillus species in brain and lung tissues using lectin histochemistry</article-title><source>Med. Mycol.</source><year>2012</year><volume>50</volume><fpage>756</fpage><lpage>759</lpage><pub-id pub-id-type="doi">10.3109/13693786.2011.631946</pub-id><pub-id pub-id-type="pmid">22103341</pub-id></element-citation></ref><ref id="B98-ijms-18-01242"><label>98.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Akkouh</surname><given-names>O.</given-names></name><name><surname>Ng</surname><given-names>T.B.</given-names></name><name><surname>Singh</surname><given-names>S.S.</given-names></name><name><surname>Yin</surname><given-names>C.M.</given-names></name><name><surname>Dan</surname><given-names>X.L.</given-names></name><name><surname>Chan</surname><given-names>Y.S.</given-names></name><name><surname>Pan</surname><given-names>W.L.</given-names></name><name><surname>Cheung</surname><given-names>R.C.F.</given-names></name></person-group><article-title>Lectins with anti-hiv activity: A review</article-title><source>Molecules</source><year>2015</year><volume>20</volume><fpage>648</fpage><lpage>668</lpage><pub-id pub-id-type="doi">10.3390/molecules20010648</pub-id><pub-id pub-id-type="pmid">25569520</pub-id></element-citation></ref><ref id="B99-ijms-18-01242"><label>99.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ingale</surname><given-names>A.G.</given-names></name><name><surname>Hivrale</surname><given-names>A.U.</given-names></name></person-group><article-title>Plant as a plenteous reserve of lectin</article-title><source>Plant Signal Behav.</source><year>2013</year><volume>8</volume><elocation-id>e26595</elocation-id><pub-id pub-id-type="doi">10.4161/psb.26595</pub-id><pub-id pub-id-type="pmid">24084524</pub-id></element-citation></ref><ref id="B100-ijms-18-01242"><label>100.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Mukhopadhyay</surname><given-names>B.</given-names></name><name><surname>Martins</surname><given-names>M.B.</given-names></name><name><surname>Karamanska</surname><given-names>R.</given-names></name><name><surname>Russell</surname><given-names>D.A.</given-names></name><name><surname>Field</surname><given-names>R.A.</given-names></name></person-group><article-title>Bacterial detection using carbohydrate-functionalised cds quantum dots: A model study exploiting E. coli recognition of mannosides</article-title><source>Tetrahedron Lett.</source><year>2009</year><volume>50</volume><fpage>886</fpage><lpage>889</lpage><pub-id pub-id-type="doi">10.1016/j.tetlet.2008.12.029</pub-id></element-citation></ref><ref id="B101-ijms-18-01242"><label>101.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Charan</surname><given-names>R.D.</given-names></name><name><surname>Munro</surname><given-names>M.H.G.</given-names></name><name><surname>O’Keefe</surname><given-names>B.R.</given-names></name><name><surname>Sowder</surname><given-names>R.C.</given-names></name><name><surname>McKee</surname><given-names>T.C.</given-names></name><name><surname>Currens</surname><given-names>M.J.</given-names></name><name><surname>Pannell</surname><given-names>L.K.</given-names></name><name><surname>Boyd</surname><given-names>M.R.</given-names></name></person-group><article-title>Isolation and characterization of Myrianthus holstii lectin, a potent HIV-1 inhibitory protein from the plant <italic>Myrianthus Holstii</italic></article-title><source>J. Nat. Prod.</source><year>2000</year><volume>63</volume><fpage>1170</fpage><lpage>1174</lpage><pub-id pub-id-type="doi">10.1021/np000039h</pub-id><pub-id pub-id-type="pmid">10978222</pub-id></element-citation></ref><ref id="B102-ijms-18-01242"><label>102.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Matsui</surname><given-names>T.</given-names></name><name><surname>Kobayashi</surname><given-names>S.</given-names></name><name><surname>Yoshida</surname><given-names>O.</given-names></name><name><surname>Ishii</surname><given-names>S.</given-names></name><name><surname>Abe</surname><given-names>Y.</given-names></name><name><surname>Yamamoto</surname><given-names>N.</given-names></name></person-group><article-title>Effects of succinylated concanavalin a on infectivity and syncytial formation of human-immunodeficiency-virus</article-title><source>Med. Microbiol. Immun.</source><year>1990</year><volume>179</volume><fpage>225</fpage><lpage>235</lpage><pub-id pub-id-type="doi">10.1007/BF00192460</pub-id></element-citation></ref><ref id="B103-ijms-18-01242"><label>103.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hansen</surname><given-names>J.E.</given-names></name><name><surname>Nielsen</surname><given-names>C.M.</given-names></name><name><surname>Nielsen</surname><given-names>C.</given-names></name><name><surname>Heegaard</surname><given-names>P.</given-names></name><name><surname>Mathiesen</surname><given-names>L.R.</given-names></name><name><surname>Nielsen</surname><given-names>J.O.</given-names></name></person-group><article-title>Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins</article-title><source>Aids</source><year>1989</year><volume>3</volume><fpage>635</fpage><lpage>641</lpage><pub-id pub-id-type="doi">10.1097/00002030-198910000-00003</pub-id><pub-id pub-id-type="pmid">2574581</pub-id></element-citation></ref><ref id="B104-ijms-18-01242"><label>104.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Dan</surname><given-names>X.L.</given-names></name><name><surname>Liu</surname><given-names>W.L.</given-names></name><name><surname>Ng</surname><given-names>T.B.</given-names></name></person-group><article-title>Development and applications of lectins as biological tools in biomedical research</article-title><source>Med. Res. Rev.</source><year>2016</year><volume>36</volume><fpage>221</fpage><lpage>247</lpage><pub-id pub-id-type="doi">10.1002/med.21363</pub-id><pub-id pub-id-type="pmid">26290041</pub-id></element-citation></ref><ref id="B105-ijms-18-01242"><label>105.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Wong</surname><given-names>J.H.</given-names></name><name><surname>Ng</surname><given-names>T.B.</given-names></name><name><surname>Cheung</surname><given-names>R.C.</given-names></name><name><surname>Ye</surname><given-names>X.J.</given-names></name><name><surname>Wang</surname><given-names>H.X.</given-names></name><name><surname>Lam</surname><given-names>S.K.</given-names></name><name><surname>Lin</surname><given-names>P.</given-names></name><name><surname>Chan</surname><given-names>Y.S.</given-names></name><name><surname>Fang</surname><given-names>E.F.</given-names></name><name><surname>Ngai</surname><given-names>P.H.</given-names></name><etal></etal></person-group><article-title>Proteins with antifungal properties and other medicinal applications from plants and mushrooms</article-title><source>Appl. Microbiol. Biotechnol.</source><year>2010</year><volume>87</volume><fpage>1221</fpage><lpage>1235</lpage><pub-id pub-id-type="doi">10.1007/s00253-010-2690-4</pub-id><pub-id pub-id-type="pmid">20532758</pub-id></element-citation></ref><ref id="B106-ijms-18-01242"><label>106.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Adams</surname><given-names>D.J.</given-names></name></person-group><article-title>Fungal cell wall chitinases and glucanases</article-title><source>Microbiology</source><year>2004</year><volume>150</volume><fpage>2029</fpage><lpage>2035</lpage><pub-id pub-id-type="doi">10.1099/mic.0.26980-0</pub-id><pub-id pub-id-type="pmid">15256547</pub-id></element-citation></ref><ref id="B107-ijms-18-01242"><label>107.</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Lis</surname><given-names>H.</given-names></name><name><surname>Sharon</surname><given-names>N.</given-names></name></person-group><article-title>Lectins in higher plants</article-title><source>The Biochemistry of Plants</source><person-group person-group-type="editor"><name><surname>Marcus</surname><given-names>A.</given-names></name></person-group><publisher-name>Academic Press Inc.</publisher-name><publisher-loc>New York, NY, USA</publisher-loc><year>1981</year><volume>Volume 6</volume><fpage>371</fpage><lpage>447</lpage></element-citation></ref><ref id="B108-ijms-18-01242"><label>108.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ciopraga</surname><given-names>J.</given-names></name><name><surname>Gozia</surname><given-names>O.</given-names></name><name><surname>Tudor</surname><given-names>R.</given-names></name><name><surname>Brezuica</surname><given-names>L.</given-names></name><name><surname>Doyle</surname><given-names>R.J.</given-names></name></person-group><article-title>Fusarium sp growth inhibition by wheat germ agglutinin</article-title><source>BBA-Gen. Subj.</source><year>1999</year><volume>1428</volume><fpage>424</fpage><lpage>432</lpage><pub-id pub-id-type="doi">10.1016/S0304-4165(99)00085-9</pub-id></element-citation></ref><ref id="B109-ijms-18-01242"><label>109.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Van Parijs</surname><given-names>J.</given-names></name><name><surname>Broekaert</surname><given-names>W.F.</given-names></name><name><surname>Goldstein</surname><given-names>I.J.</given-names></name><name><surname>Peumans</surname><given-names>W.J.</given-names></name></person-group><article-title>Hevein: An antifungal protein from rubber-tree (Hevea brasiliensis) latex</article-title><source>Planta</source><year>1991</year><volume>183</volume><fpage>258</fpage><lpage>264</lpage><pub-id pub-id-type="doi">10.1007/BF00197797</pub-id><pub-id pub-id-type="pmid">24193629</pub-id></element-citation></ref><ref id="B110-ijms-18-01242"><label>110.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Boleti</surname><given-names>A.P.D.</given-names></name><name><surname>Freire</surname><given-names>M.D.M.</given-names></name><name><surname>Coelho</surname><given-names>M.B.</given-names></name><name><surname>da Silva</surname><given-names>W.</given-names></name><name><surname>Baldasso</surname><given-names>P.A.</given-names></name><name><surname>Gomes</surname><given-names>V.M.</given-names></name><name><surname>Marangoni</surname><given-names>S.</given-names></name><name><surname>Novello</surname><given-names>J.C.</given-names></name><name><surname>Macedo</surname><given-names>M.L.R.</given-names></name></person-group><article-title>Insecticidal and antifungal activity of a protein from Pouteria torta seeds with lectin-like properties</article-title><source>J. Agric. Food Chem.</source><year>2007</year><volume>55</volume><fpage>2653</fpage><lpage>2658</lpage><pub-id pub-id-type="doi">10.1021/jf0636317</pub-id><pub-id pub-id-type="pmid">17348680</pub-id></element-citation></ref><ref id="B111-ijms-18-01242"><label>111.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Rao</surname><given-names>V.S.R.</given-names></name><name><surname>Lam</surname><given-names>K.</given-names></name><name><surname>Qasba</surname><given-names>P.K.</given-names></name></person-group><article-title>Three dimensional structure of the soybean agglutinin-Gal/GalNac complexes by homology modeling</article-title><source>J. Biomol. Struct. Dyn.</source><year>1998</year><volume>15</volume><fpage>853</fpage><lpage>860</lpage><pub-id pub-id-type="doi">10.1080/07391102.1998.10508207</pub-id><pub-id pub-id-type="pmid">9619508</pub-id></element-citation></ref><ref id="B112-ijms-18-01242"><label>112.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Vigerust</surname><given-names>D.J.</given-names></name><name><surname>Shepherd</surname><given-names>V.L.</given-names></name></person-group><article-title>Virus glycosylation: Role in virulence and immune interactions</article-title><source>Trends Microbiol.</source><year>2007</year><volume>15</volume><fpage>211</fpage><lpage>218</lpage><pub-id pub-id-type="doi">10.1016/j.tim.2007.03.003</pub-id><pub-id pub-id-type="pmid">17398101</pub-id></element-citation></ref><ref id="B113-ijms-18-01242"><label>113.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ziolkowska</surname><given-names>N.E.</given-names></name><name><surname>Wlodawer</surname><given-names>A.</given-names></name></person-group><article-title>Structural studies of algal lectins with anti-hiv activity</article-title><source>Acta Biochim. Pol.</source><year>2006</year><volume>53</volume><fpage>617</fpage><lpage>626</lpage><pub-id pub-id-type="pmid">17128290</pub-id></element-citation></ref><ref id="B114-ijms-18-01242"><label>114.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Keyaerts</surname><given-names>E.</given-names></name><name><surname>Vijgen</surname><given-names>L.</given-names></name><name><surname>Pannecouque</surname><given-names>C.</given-names></name><name><surname>Van Damme</surname><given-names>E.</given-names></name><name><surname>Peumans</surname><given-names>W.</given-names></name><name><surname>Egberink</surname><given-names>H.</given-names></name><name><surname>Balzarini</surname><given-names>J.</given-names></name><name><surname>Van Ranst</surname><given-names>M.</given-names></name></person-group><article-title>Plant lectins are potent inhibitors of coronaviruses by interfering with two targets in the viral replication cycle</article-title><source>Antivir. Res.</source><year>2007</year><volume>75</volume><fpage>179</fpage><lpage>187</lpage><pub-id pub-id-type="doi">10.1016/j.antiviral.2007.03.003</pub-id><pub-id pub-id-type="pmid">17428553</pub-id></element-citation></ref><ref id="B115-ijms-18-01242"><label>115.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lusvarghi</surname><given-names>S.</given-names></name><name><surname>Bewley</surname><given-names>C.A.</given-names></name></person-group><article-title>Griffithsin: An antiviral lectin with outstanding therapeutic potential</article-title><source>Viruses</source><year>2016</year><volume>8</volume><elocation-id>296</elocation-id><pub-id pub-id-type="doi">10.3390/v8100296</pub-id><pub-id pub-id-type="pmid">27783038</pub-id></element-citation></ref><ref id="B116-ijms-18-01242"><label>116.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Fei Fang</surname><given-names>E.</given-names></name><name><surname>Ho Wong</surname><given-names>J.</given-names></name><name><surname>Lin</surname><given-names>P.</given-names></name><name><surname>Bun Ng</surname><given-names>T.</given-names></name></person-group><article-title>Biochemical and functional properties of a lectin purified from korean large black soybeans a cultivar of glycine max</article-title><source>Protein Pept. Lett.</source><year>2010</year><volume>17</volume><fpage>690</fpage><lpage>698</lpage><pub-id pub-id-type="doi">10.2174/092986610791190309</pub-id><pub-id pub-id-type="pmid">19715533</pub-id></element-citation></ref><ref id="B117-ijms-18-01242"><label>117.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Macedo</surname><given-names>M.L.R.</given-names></name><name><surname>das Graças Machado Freire</surname><given-names>M.</given-names></name><name><surname>da Silva</surname><given-names>M.B.R.</given-names></name><name><surname>Coelho</surname><given-names>L.C.B.B.</given-names></name></person-group><article-title>Insecticidal action of Bauhinia monandra leaf lectin (bmoll) against Anagasta kuehniella (lepidoptera: Pyralidae), Zabrotes subfasciatus and Callosobruchus maculatus (coleoptera: Bruchidae)</article-title><source>Comp. Biochem. Physiol. A Mol. Integr. Physiol.</source><year>2007</year><volume>146</volume><fpage>486</fpage><lpage>498</lpage><pub-id pub-id-type="doi">10.1016/j.cbpa.2006.01.020</pub-id><pub-id pub-id-type="pmid">16488638</pub-id></element-citation></ref><ref id="B118-ijms-18-01242"><label>118.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Melander</surname><given-names>M.</given-names></name><name><surname>Åhman</surname><given-names>I.</given-names></name><name><surname>Kamnert</surname><given-names>I.</given-names></name><name><surname>Strömdahl</surname><given-names>A.-C.</given-names></name></person-group><article-title>Pea lectin expressed transgenically in oilseed rape reduces growth rate of pollen beetle larvae</article-title><source>Transgenic Res.</source><year>2003</year><volume>12</volume><fpage>555</fpage><lpage>567</lpage><pub-id pub-id-type="doi">10.1023/A:1025813526283</pub-id><pub-id pub-id-type="pmid">14601654</pub-id></element-citation></ref><ref id="B119-ijms-18-01242"><label>119.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Michiels</surname><given-names>K.</given-names></name><name><surname>Van Damme</surname><given-names>E.J.</given-names></name><name><surname>Smagghe</surname><given-names>G.</given-names></name></person-group><article-title>Plant–insect interactions: What can we learn from plant lectins?</article-title><source>Arch. Insect Biochem. Physiol.</source><year>2010</year><volume>73</volume><fpage>193</fpage><lpage>212</lpage><pub-id pub-id-type="doi">10.1002/arch.20351</pub-id><pub-id pub-id-type="pmid">20151457</pub-id></element-citation></ref><ref id="B120-ijms-18-01242"><label>120.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Dandagi</surname><given-names>P.</given-names></name><name><surname>Mastiholimath</surname><given-names>V.</given-names></name><name><surname>Patil</surname><given-names>M.</given-names></name><name><surname>Gupta</surname><given-names>M.</given-names></name></person-group><article-title>Biodegradable microparticulate system of captopril</article-title><source>Int. J. Pharm.</source><year>2006</year><volume>307</volume><fpage>83</fpage><lpage>88</lpage><pub-id pub-id-type="doi">10.1016/j.ijpharm.2005.10.025</pub-id><pub-id pub-id-type="pmid">16310990</pub-id></element-citation></ref><ref id="B121-ijms-18-01242"><label>121.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Walski</surname><given-names>T.</given-names></name><name><surname>Van Damme</surname><given-names>E.J.</given-names></name><name><surname>Smagghe</surname><given-names>G.</given-names></name></person-group><article-title>Penetration through the peritrophic matrix is a key to lectin toxicity against Tribolium castaneum</article-title><source>J. Insect Physiol.</source><year>2014</year><volume>70</volume><fpage>94</fpage><lpage>101</lpage><pub-id pub-id-type="doi">10.1016/j.jinsphys.2014.09.004</pub-id><pub-id pub-id-type="pmid">25240534</pub-id></element-citation></ref><ref id="B122-ijms-18-01242"><label>122.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Roy</surname><given-names>A.</given-names></name><name><surname>Gupta</surname><given-names>S.</given-names></name><name><surname>Hess</surname><given-names>D.</given-names></name><name><surname>Das</surname><given-names>K.P.</given-names></name><name><surname>Das</surname><given-names>S.</given-names></name></person-group><article-title>Binding of insecticidal lectin Colocasia esculenta tuber agglutinin (cea) to midgut receptors of Bemisia tabaci and Lipaphis erysimi provides clues to its insecticidal potential</article-title><source>Proteomics</source><year>2014</year><volume>14</volume><fpage>1646</fpage><lpage>1659</lpage><pub-id pub-id-type="doi">10.1002/pmic.201300408</pub-id><pub-id pub-id-type="pmid">24753494</pub-id></element-citation></ref><ref id="B123-ijms-18-01242"><label>123.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Francis</surname><given-names>F.</given-names></name><name><surname>Marty-Detraves</surname><given-names>C.</given-names></name><name><surname>Poincloux</surname><given-names>R.</given-names></name><name><surname>Baricault</surname><given-names>L.</given-names></name><name><surname>Fournier</surname><given-names>D.</given-names></name><name><surname>Paquereau</surname><given-names>L.</given-names></name></person-group><article-title>Fungal lectin, xcl, is internalized via clathrin-dependent endocytosis and facilitates uptake of other molecules</article-title><source>Eur. J. Cell Biol.</source><year>2003</year><volume>82</volume><fpage>515</fpage><lpage>522</lpage><pub-id pub-id-type="doi">10.1078/0171-9335-00338</pub-id><pub-id pub-id-type="pmid">14629119</pub-id></element-citation></ref><ref id="B124-ijms-18-01242"><label>124.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Caccia</surname><given-names>S.</given-names></name><name><surname>Van Damme</surname><given-names>E.J.</given-names></name><name><surname>De Vos</surname><given-names>W.H.</given-names></name><name><surname>Smagghe</surname><given-names>G.</given-names></name></person-group><article-title>Mechanism of entomotoxicity of the plant lectin from Hippeastrum hybrid (amaryllis) in spodoptera Littoralis larvae</article-title><source>J. Insect Physiol.</source><year>2012</year><volume>58</volume><fpage>1177</fpage><lpage>1183</lpage><pub-id pub-id-type="doi">10.1016/j.jinsphys.2012.05.014</pub-id><pub-id pub-id-type="pmid">22677323</pub-id></element-citation></ref><ref id="B125-ijms-18-01242"><label>125.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Zhu-Salzman</surname><given-names>K.</given-names></name><name><surname>Salzman</surname><given-names>R.A.</given-names></name></person-group><article-title>Functional mechanics of the plant defensive <italic>Griffonia simplicifolia</italic> lectin II: Resistance to proteolysis is independent of glycoconjugate binding in the insect gut</article-title><source>J. Econ. Entomol.</source><year>2001</year><volume>94</volume><fpage>1280</fpage><lpage>1284</lpage><pub-id pub-id-type="doi">10.1603/0022-0493-94.5.1280</pub-id><pub-id pub-id-type="pmid">11681694</pub-id></element-citation></ref><ref id="B126-ijms-18-01242"><label>126.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Fitches</surname><given-names>E.</given-names></name><name><surname>Wiles</surname><given-names>D.</given-names></name><name><surname>Douglas</surname><given-names>A.E.</given-names></name><name><surname>Hinchliffe</surname><given-names>G.</given-names></name><name><surname>Audsley</surname><given-names>N.</given-names></name><name><surname>Gatehouse</surname><given-names>J.A.</given-names></name></person-group><article-title>The insecticidal activity of recombinant garlic lectins towards aphids</article-title><source>Insect Biochem. Mol. Biol.</source><year>2008</year><volume>38</volume><fpage>905</fpage><lpage>915</lpage><pub-id pub-id-type="doi">10.1016/j.ibmb.2008.07.002</pub-id><pub-id pub-id-type="pmid">18707000</pub-id></element-citation></ref><ref id="B127-ijms-18-01242"><label>127.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Du</surname><given-names>J.</given-names></name><name><surname>Foissac</surname><given-names>X.</given-names></name><name><surname>Carss</surname><given-names>A.</given-names></name><name><surname>Gatehouse</surname><given-names>A.M.</given-names></name><name><surname>Gatehouse</surname><given-names>J.A.</given-names></name></person-group><article-title>Ferritin acts as the most abundant binding protein for snowdrop lectin in the midgut of rice brown planthoppers (Nilaparvata lugens)</article-title><source>Insect Biochem. Mol. Biol.</source><year>2000</year><volume>30</volume><fpage>297</fpage><lpage>305</lpage><pub-id pub-id-type="doi">10.1016/S0965-1748(99)00130-7</pub-id><pub-id pub-id-type="pmid">10727896</pub-id></element-citation></ref><ref id="B128-ijms-18-01242"><label>128.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sadeghi</surname><given-names>A.</given-names></name><name><surname>Smagghe</surname><given-names>G.</given-names></name><name><surname>Proost</surname><given-names>P.</given-names></name><name><surname>Van Damme</surname><given-names>E.J.</given-names></name></person-group><article-title>Ferritin acts as a target site for the snowdrop lectin (gna) in the midgut of the cotton leafworm spodoptera littoralis</article-title><source>Insect Sci.</source><year>2008</year><volume>15</volume><fpage>513</fpage><lpage>519</lpage><pub-id pub-id-type="doi">10.1111/j.1744-7917.2008.00240.x</pub-id></element-citation></ref><ref id="B129-ijms-18-01242"><label>129.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Napoleão</surname><given-names>T.H.</given-names></name><name><surname>Pontual</surname><given-names>E.V.</given-names></name><name><surname>de Albuquerque Lima</surname><given-names>T.</given-names></name><name><surname>de Lima Santos</surname><given-names>N.D.</given-names></name><name><surname>Sá</surname><given-names>R.A.</given-names></name><name><surname>Coelho</surname><given-names>L.C.B.B.</given-names></name><name><surname>do Amaral Ferraz Navarro</surname><given-names>D.M.</given-names></name><name><surname>Paiva</surname><given-names>P.M.G.</given-names></name></person-group><article-title>Effect of myracrodruon urundeuva leaf lectin on survival and digestive enzymes of Aedes aegypti larvae</article-title><source>Parasitol. Res.</source><year>2012</year><volume>110</volume><fpage>609</fpage><lpage>616</lpage><pub-id pub-id-type="doi">10.1007/s00436-011-2529-7</pub-id><pub-id pub-id-type="pmid">21735148</pub-id></element-citation></ref><ref id="B130-ijms-18-01242"><label>130.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sprawka</surname><given-names>I.</given-names></name><name><surname>Goławska</surname><given-names>S.</given-names></name><name><surname>Goławski</surname><given-names>A.</given-names></name><name><surname>Chrzanowski</surname><given-names>G.</given-names></name><name><surname>Czerniewicz</surname><given-names>P.</given-names></name><name><surname>Sytykiewicz</surname><given-names>H.</given-names></name></person-group><article-title>Entomotoxic action of jackbean lectin (con a) in bird cherry-oat aphid through the effect on insect enzymes</article-title><source>J. Plant Interact.</source><year>2014</year><volume>9</volume><fpage>425</fpage><lpage>433</lpage><pub-id pub-id-type="doi">10.1080/17429145.2013.848947</pub-id></element-citation></ref><ref id="B131-ijms-18-01242"><label>131.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Bala</surname><given-names>A.</given-names></name><name><surname>Roy</surname><given-names>A.</given-names></name><name><surname>Behura</surname><given-names>N.</given-names></name><name><surname>Hess</surname><given-names>D.</given-names></name><name><surname>Das</surname><given-names>S.</given-names></name></person-group><article-title>Insight to the mode of action of allium sativum leaf agglutinin (asal) expressing in t3 rice lines on brown planthopper</article-title><source>Am. J. Plant Sci.</source><year>2013</year><volume>4</volume><fpage>400</fpage><lpage>407</lpage><pub-id pub-id-type="doi">10.4236/ajps.2013.42A052</pub-id></element-citation></ref><ref id="B132-ijms-18-01242"><label>132.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lagarda-Diaz</surname><given-names>I.</given-names></name><name><surname>Guzman-Partida</surname><given-names>A.M.</given-names></name><name><surname>Huerta-Ocampo</surname><given-names>J.A.</given-names></name><name><surname>Winzerling</surname><given-names>J.</given-names></name><name><surname>Vazquez-Moreno</surname><given-names>L.</given-names></name></person-group><article-title>Identification of membrane proteins of the midgut of Zabrotes subfasciatus larvae associated with the insecticidal mechanism of PF2 lectin</article-title><source>J. Asia-Pacif. Entomol.</source><year>2016</year><volume>19</volume><fpage>677</fpage><lpage>682</lpage><pub-id pub-id-type="doi">10.1016/j.aspen.2016.04.004</pub-id></element-citation></ref><ref id="B133-ijms-18-01242"><label>133.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lagarda-Diaz</surname><given-names>I.</given-names></name><name><surname>Robles-Burgeño</surname><given-names>M.R.</given-names></name><name><surname>Guzman-Partida</surname><given-names>A.M.</given-names></name><name><surname>Geiser</surname><given-names>D.</given-names></name><name><surname>Winzerling</surname><given-names>J.</given-names></name><name><surname>Vazquez-Moreno</surname><given-names>L.</given-names></name></person-group><article-title>Binding of PF2 lectin from <italic>Olneya tesota</italic> to gut proteins of Zabrotes subfasciatus larvae associated with the insecticidal mechanism</article-title><source>J. Agric. Food Chem.</source><year>2012</year><volume>60</volume><fpage>2398</fpage><lpage>2402</lpage><pub-id pub-id-type="doi">10.1021/jf2045872</pub-id><pub-id pub-id-type="pmid">22288827</pub-id></element-citation></ref><ref id="B134-ijms-18-01242"><label>134.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Upadhyay</surname><given-names>S.K.</given-names></name><name><surname>Singh</surname><given-names>P.K.</given-names></name></person-group><article-title>Receptors of garlic (Allium sativum) lectins and their role in insecticidal action</article-title><source>Protein J.</source><year>2012</year><volume>31</volume><fpage>439</fpage><lpage>446</lpage><pub-id pub-id-type="doi">10.1007/s10930-012-9423-8</pub-id><pub-id pub-id-type="pmid">22623282</pub-id></element-citation></ref><ref id="B135-ijms-18-01242"><label>135.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Shen</surname><given-names>L.</given-names></name><name><surname>Luo</surname><given-names>Z.</given-names></name><name><surname>Wu</surname><given-names>J.</given-names></name><name><surname>Qiu</surname><given-names>L.</given-names></name><name><surname>Luo</surname><given-names>M.</given-names></name><name><surname>Ke</surname><given-names>Q.</given-names></name><name><surname>Dong</surname><given-names>X.</given-names></name></person-group><article-title>Enhanced expression of α2, 3-linked sialic acids promotes gastric cancer cell metastasis and correlates with poor prognosis</article-title><source>Int. J. Oncol.</source><year>2017</year><volume>50</volume><fpage>1201</fpage><lpage>1210</lpage><pub-id pub-id-type="pmid">28259967</pub-id></element-citation></ref><ref id="B136-ijms-18-01242"><label>136.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Litynska</surname><given-names>A.</given-names></name><name><surname>Przybyuulo</surname><given-names>M.</given-names></name><name><surname>Pochec</surname><given-names>E.</given-names></name><name><surname>Hoja-uuLukowicz</surname><given-names>D.</given-names></name><name><surname>Ciouulczyk</surname><given-names>D.</given-names></name><name><surname>Laidler</surname><given-names>P.</given-names></name><name><surname>Gil</surname><given-names>D.</given-names></name></person-group><article-title>Comparison of the lectin-binding pattern in different human melanoma cell lines</article-title><source>Melanoma Res.</source><year>2001</year><volume>11</volume><fpage>205</fpage><lpage>212</lpage><pub-id pub-id-type="doi">10.1097/00008390-200106000-00001</pub-id><pub-id pub-id-type="pmid">11468508</pub-id></element-citation></ref><ref id="B137-ijms-18-01242"><label>137.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Korourian</surname><given-names>S.</given-names></name><name><surname>Siegel</surname><given-names>E.</given-names></name><name><surname>Kieber-Emmons</surname><given-names>T.</given-names></name><name><surname>Monzavi-Karbassi</surname><given-names>B.</given-names></name></person-group><article-title>Expression analysis of carbohydrate antigens in ductal carcinoma in situ of the breast by lectin histochemistry</article-title><source>BMC Cancer</source><year>2008</year><volume>8</volume><elocation-id>136</elocation-id><pub-id pub-id-type="doi">10.1186/1471-2407-8-136</pub-id><pub-id pub-id-type="pmid">18479514</pub-id></element-citation></ref><ref id="B138-ijms-18-01242"><label>138.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Blomme</surname><given-names>B.</given-names></name><name><surname>Van Steenkiste</surname><given-names>C.</given-names></name><name><surname>Callewaert</surname><given-names>N.</given-names></name><name><surname>Van Vlierberghe</surname><given-names>H.</given-names></name></person-group><article-title>Alteration of protein glycosylation in liver diseases</article-title><source>J. Hepatol.</source><year>2009</year><volume>50</volume><fpage>592</fpage><lpage>603</lpage><pub-id pub-id-type="doi">10.1016/j.jhep.2008.12.010</pub-id><pub-id pub-id-type="pmid">19157620</pub-id></element-citation></ref><ref id="B139-ijms-18-01242"><label>139.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Fu</surname><given-names>L.L.</given-names></name><name><surname>Zhou</surname><given-names>C.C.</given-names></name><name><surname>Yao</surname><given-names>S.</given-names></name><name><surname>Yu</surname><given-names>J.Y.</given-names></name><name><surname>Liu</surname><given-names>B.</given-names></name><name><surname>Bao</surname><given-names>J.K.</given-names></name></person-group><article-title>Plant lectins: Targeting programmed cell death pathways as antitumor agents</article-title><source>Int. J. Biochem. Cell Biol.</source><year>2011</year><volume>43</volume><fpage>1442</fpage><lpage>1449</lpage><pub-id pub-id-type="doi">10.1016/j.biocel.2011.07.004</pub-id><pub-id pub-id-type="pmid">21798364</pub-id></element-citation></ref><ref id="B140-ijms-18-01242"><label>140.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Stauder</surname><given-names>H.</given-names></name><name><surname>Kreuser</surname><given-names>E.-D.</given-names></name></person-group><article-title>Mistletoe extracts standardised in terms of mistletoe lectins (ml i) in oncology: Current state of clinical research</article-title><source>Oncol. Res. Treat.</source><year>2002</year><volume>25</volume><fpage>374</fpage><lpage>380</lpage><pub-id pub-id-type="doi">10.1159/000066058</pub-id></element-citation></ref><ref id="B141-ijms-18-01242"><label>141.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Jiang</surname><given-names>Q.L.</given-names></name><name><surname>Zhang</surname><given-names>S.</given-names></name><name><surname>Tian</surname><given-names>M.</given-names></name><name><surname>Zhang</surname><given-names>S.Y.</given-names></name><name><surname>Xie</surname><given-names>T.</given-names></name><name><surname>Chen</surname><given-names>D.Y.</given-names></name><name><surname>Chen</surname><given-names>Y.J.</given-names></name><name><surname>He</surname><given-names>J.</given-names></name><name><surname>Liu</surname><given-names>J.</given-names></name><name><surname>Ouyang</surname><given-names>L.</given-names></name></person-group><article-title>Plant lectins, from ancient sugar-binding proteins to emerging anti-cancer drugs in apoptosis and autophagy</article-title><source>Cell Prolif.</source><year>2015</year><volume>48</volume><fpage>17</fpage><lpage>28</lpage><pub-id pub-id-type="doi">10.1111/cpr.12155</pub-id><pub-id pub-id-type="pmid">25488051</pub-id></element-citation></ref><ref id="B142-ijms-18-01242"><label>142.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hajela</surname><given-names>K.</given-names></name><name><surname>Kojima</surname><given-names>M.</given-names></name><name><surname>Ambrus</surname><given-names>G.</given-names></name><name><surname>Wong</surname><given-names>K.H.</given-names></name><name><surname>Moffatt</surname><given-names>B.E.</given-names></name><name><surname>Ferluga</surname><given-names>J.</given-names></name><name><surname>Hajela</surname><given-names>S.</given-names></name><name><surname>Gál</surname><given-names>P.</given-names></name><name><surname>Sim</surname><given-names>R.B.</given-names></name></person-group><article-title>The biological functions of MBL-associated serine proteases (MASPs)</article-title><source>Immunobiology</source><year>2002</year><volume>205</volume><fpage>467</fpage><lpage>475</lpage><pub-id pub-id-type="doi">10.1078/0171-2985-00147</pub-id><pub-id pub-id-type="pmid">12396008</pub-id></element-citation></ref><ref id="B143-ijms-18-01242"><label>143.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Panda</surname><given-names>P.K.</given-names></name><name><surname>Mukhopadhyay</surname><given-names>S.</given-names></name><name><surname>Behera</surname><given-names>B.</given-names></name><name><surname>Bhol</surname><given-names>C.S.</given-names></name><name><surname>Dey</surname><given-names>S.</given-names></name><name><surname>Das</surname><given-names>D.N.</given-names></name><name><surname>Sinha</surname><given-names>N.</given-names></name><name><surname>Bissoyi</surname><given-names>A.</given-names></name><name><surname>Pramanik</surname><given-names>K.</given-names></name><name><surname>Maiti</surname><given-names>T.K.</given-names></name></person-group><article-title>Antitumor effect of soybean lectin mediated through reactive oxygen species-dependent pathway</article-title><source>Life Sci.</source><year>2014</year><volume>111</volume><fpage>27</fpage><lpage>35</lpage><pub-id pub-id-type="doi">10.1016/j.lfs.2014.07.004</pub-id><pub-id pub-id-type="pmid">25064824</pub-id></element-citation></ref><ref id="B144-ijms-18-01242"><label>144.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kim</surname><given-names>M.</given-names></name><name><surname>Rao</surname><given-names>M.</given-names></name><name><surname>Tweardy</surname><given-names>D.</given-names></name><name><surname>Prakash</surname><given-names>M.</given-names></name><name><surname>Galili</surname><given-names>U.</given-names></name><name><surname>Gorelik</surname><given-names>E.</given-names></name></person-group><article-title>Lectin-induced apoptosis of tumour cells</article-title><source>Glycobiology</source><year>1993</year><volume>3</volume><fpage>447</fpage><lpage>453</lpage><pub-id pub-id-type="doi">10.1093/glycob/3.5.447</pub-id><pub-id pub-id-type="pmid">8286857</pub-id></element-citation></ref><ref id="B145-ijms-18-01242"><label>145.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Chang</surname><given-names>C.P.</given-names></name><name><surname>Lei</surname><given-names>H.Y.</given-names></name></person-group><article-title>Autophagy induction in t cell-independent acute hepatitis induced by concanavalin a in scid/nod mice</article-title><source>Int. J. Immunopathol. Pharmacol.</source><year>2008</year><volume>21</volume><fpage>817</fpage><lpage>826</lpage><pub-id pub-id-type="doi">10.1177/039463200802100406</pub-id><pub-id pub-id-type="pmid">19144267</pub-id></element-citation></ref></ref-list></back><floats-group><fig id="ijms-18-01242-f001" orientation="portrait" position="float"><label>Figure 1</label><caption><p>Overall structure of legume lectins. (<bold>A</bold>) tetramer with carbohydrate recognition domains (red); (<bold>B</bold>) amplified image of monomer with β-sheets (yellow), α-turns (purple), metal binding sites (area with green and gray spheres) and carbohydrate recognition domain (area occupied by the grey and red molecule). Image modified from Protein Data Bank (accession code 1GZ9).</p></caption><graphic xlink:href="ijms-18-01242-g001"></graphic></fig><fig id="ijms-18-01242-f002" orientation="portrait" position="float"><label>Figure 2</label><caption><p>Insecticidal action mechanism for lectins.</p></caption><graphic xlink:href="ijms-18-01242-g002"></graphic></fig><table-wrap id="ijms-18-01242-t001" orientation="portrait" position="float"><object-id pub-id-type="pii">ijms-18-01242-t001_Table 1</object-id><label>Table 1</label><caption><p>Antimicrobial effect of legume lectins.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Lectin</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Carbohydrate/Glycoprotein Receptor</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Type of Microorganism</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Mechanism of Action</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Reference</th></tr></thead><tbody><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">From Leguminosae, tribe: <italic>Vicieae</italic><break></break><italic>Diocleae</italic><break></break><italic>Phaseoleae</italic><break></break><italic>Erithrinea</italic><break></break><italic>Glycineae</italic><break></break><italic>Sophoreae</italic><break></break><italic>Galegeae</italic><break></break><italic>Genisteae</italic><break></break><italic>Loteae</italic><break></break><italic>Acacieae</italic></td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Components of the cell Wall: Muramic acid, <italic>N</italic>-acetylmuramic acid, <italic>N</italic>-acetylglucosamine, Muramyl-dipeptides, glucosaminyl-muyamyl-dipeptide, lipopolysacharides</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Bacteria</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Form a channel or pore on cell membrane and the cell dies as a result of the out flowing of cellular contents. Bacterial aggregation and inhibition bacterial cell division</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B79-ijms-18-01242" ref-type="bibr">79</xref>,<xref rid="B83-ijms-18-01242" ref-type="bibr">83</xref>,<xref rid="B87-ijms-18-01242" ref-type="bibr">87</xref>,<xref rid="B89-ijms-18-01242" ref-type="bibr">89</xref>,<xref rid="B90-ijms-18-01242" ref-type="bibr">90</xref>,<xref rid="B91-ijms-18-01242" ref-type="bibr">91</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1"><italic>Astragalus mongholicus</italic> agglutinin <break></break><italic>P. vulgaris agglutinin</italic><break></break><italic>P. coccineus</italic> agglutinin <break></break>Soy bean agglutinin <break></break>Peanut agglutinin</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Components of fungal cell wall: Chitin, sialic acid</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Fungi</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Binding to hyphae, swollen hyphal, vacuolization of the cell content, and enhanced susceptibility to cell wall lysis of the hyphal induced by osmotic shock, producing more susceptibility to other stress conditions. This condition produces poor absorption of nutrients, interference spore germination and rupture of the cell wall.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B79-ijms-18-01242" ref-type="bibr">79</xref>,<xref rid="B83-ijms-18-01242" ref-type="bibr">83</xref>,<xref rid="B91-ijms-18-01242" ref-type="bibr">91</xref>,<xref rid="B92-ijms-18-01242" ref-type="bibr">92</xref>,<xref rid="B93-ijms-18-01242" ref-type="bibr">93</xref>,<xref rid="B94-ijms-18-01242" ref-type="bibr">94</xref>,<xref rid="B95-ijms-18-01242" ref-type="bibr">95</xref>,<xref rid="B96-ijms-18-01242" ref-type="bibr">96</xref>,<xref rid="B97-ijms-18-01242" ref-type="bibr">97</xref>,<xref rid="B98-ijms-18-01242" ref-type="bibr">98</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Concanavalin A <break></break><italic>Psophocarpus tetragonolubus</italic> agglutinin <break></break><italic>Lens culinaris</italic> agglutinin <break></break><italic>Vicia faba</italic> agglutinin <break></break><italic>Pisum sativum</italic> agglutinin Erythroagglutinin</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Components of viral envelope: Glycoproteins Gp120/Gp41, sialic acid</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Virus</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Bind to the glycosylated envelope protein and block cellular entry (interfere with replication cycle)</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B98-ijms-18-01242" ref-type="bibr">98</xref>,<xref rid="B99-ijms-18-01242" ref-type="bibr">99</xref>,<xref rid="B100-ijms-18-01242" ref-type="bibr">100</xref>,<xref rid="B101-ijms-18-01242" ref-type="bibr">101</xref>,<xref rid="B102-ijms-18-01242" ref-type="bibr">102</xref>,<xref rid="B103-ijms-18-01242" ref-type="bibr">103</xref>,<xref rid="B104-ijms-18-01242" ref-type="bibr">104</xref>,<xref rid="B105-ijms-18-01242" ref-type="bibr">105</xref>]</td></tr></tbody></table></table-wrap><table-wrap id="ijms-18-01242-t002" orientation="portrait" position="float"><object-id pub-id-type="pii">ijms-18-01242-t002_Table 2</object-id><label>Table 2</label><caption><p>Receptors of plant lectins of different insects.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="center" valign="top" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Lectin</th><th align="center" valign="top" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Receptor</th><th align="center" valign="top" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Insect</th><th align="center" valign="top" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Reference</th></tr></thead><tbody><tr><td align="center" valign="top" rowspan="1" colspan="1"><italic>Allium sativum</italic> L. bulbs (ASAI and ASAII)</td><td align="center" valign="top" rowspan="1" colspan="1">Aminopeptidase N Sucrase</td><td align="center" valign="top" rowspan="1" colspan="1"><italic>Acyrthosiphon pisum</italic></td><td align="center" valign="top" rowspan="1" colspan="1">[<xref rid="B126-ijms-18-01242" ref-type="bibr">126</xref>]</td></tr><tr><td align="center" valign="top" rowspan="1" colspan="1"><italic>Galantus nivalis</italic> lectin</td><td align="center" valign="top" rowspan="1" colspan="1">Ferritin</td><td align="center" valign="top" rowspan="1" colspan="1"><italic>Nilaparvata lunges Spodoptera littoralis</italic></td><td align="center" valign="top" rowspan="1" colspan="1">[<xref rid="B127-ijms-18-01242" ref-type="bibr">127</xref>]<break></break>[<xref rid="B128-ijms-18-01242" ref-type="bibr">128</xref>]</td></tr><tr><td align="center" valign="top" rowspan="1" colspan="1"><italic>Myracrodruon urundeuva</italic> leaf lectin (MuLL)</td><td align="center" valign="top" rowspan="1" colspan="1">Trypsin α-amylase</td><td align="center" valign="top" rowspan="1" colspan="1"><italic>Aedes aegypti</italic></td><td align="center" valign="top" rowspan="1" colspan="1">[<xref rid="B129-ijms-18-01242" ref-type="bibr">129</xref>]</td></tr><tr><td align="center" valign="top" rowspan="1" colspan="1"><italic>Bauhinia monandra</italic> leaf lectin (BmoLL)</td><td align="center" valign="top" rowspan="1" colspan="1">α-amylase</td><td align="center" valign="top" rowspan="1" colspan="1"><italic>Callosobruchus maculatus</italic></td><td align="center" valign="top" rowspan="1" colspan="1">[<xref rid="B117-ijms-18-01242" ref-type="bibr">117</xref>]</td></tr><tr><td align="center" valign="top" rowspan="1" colspan="1">Concanavalin A</td><td align="center" valign="top" rowspan="1" colspan="1">β-glucosidases <break></break>cathepsin L</td><td align="center" valign="top" rowspan="1" colspan="1"><italic>Rhopalosiphum padi L.</italic></td><td align="center" valign="top" rowspan="1" colspan="1">[<xref rid="B130-ijms-18-01242" ref-type="bibr">130</xref>]</td></tr><tr><td align="center" valign="top" rowspan="1" colspan="1"><italic>Allium sativum</italic> Leaf<break></break>Agglutinin (ASAL)</td><td align="center" valign="top" rowspan="1" colspan="1"> (Nicotinamide adenine dinucleotide reduced) quinone oxidoreductase</td><td align="center" valign="top" rowspan="1" colspan="1"><italic>Brown planthopper</italic></td><td align="center" valign="top" rowspan="1" colspan="1">[<xref rid="B131-ijms-18-01242" ref-type="bibr">131</xref>]</td></tr><tr><td align="center" valign="top" rowspan="1" colspan="1"><italic>Colocasia esculenta</italic> tuber agglutinin (CEA)</td><td align="center" valign="top" rowspan="1" colspan="1">Vacuolar ATP synthase<break></break>ATP synthase<break></break>Heat shock protein 70 clathrin heavy chain</td><td align="center" valign="top" rowspan="1" colspan="1"><italic>Lipaphis erysimi</italic></td><td align="center" valign="top" rowspan="1" colspan="1">[<xref rid="B122-ijms-18-01242" ref-type="bibr">122</xref>]</td></tr><tr><td align="center" valign="top" rowspan="1" colspan="1"></td><td align="center" valign="top" rowspan="1" colspan="1">Sarcoplasmic endoplasmic reticulum typ Ca<sup>2+</sup>ATPase</td><td align="center" valign="top" rowspan="1" colspan="1"><italic>Bemisia tabaci</italic></td><td align="center" valign="top" rowspan="1" colspan="1">[<xref rid="B122-ijms-18-01242" ref-type="bibr">122</xref>]</td></tr><tr><td align="center" valign="top" rowspan="1" colspan="1">PF2 lectin</td><td align="center" valign="top" rowspan="1" colspan="1">α-amylase<break></break>V-type proton ATPase<break></break>Arginine kinase <break></break>Prohibitin <break></break>Polyubiquitin <break></break>Actin<break></break>ATP-dependent RNA helicase <break></break>ATP synthase subunit alpha<break></break>Mitochondrial-processing peptidase <break></break>α-tubulin <break></break>Odorant receptor <break></break>Cytochrome c oxidase</td><td align="center" valign="top" rowspan="1" colspan="1"><italic>Zabrotes subfasciatus</italic></td><td align="center" valign="top" rowspan="1" colspan="1">[<xref rid="B132-ijms-18-01242" ref-type="bibr">132</xref>]<break></break><break></break><break></break><break></break><break></break><break></break><break></break><break></break><break></break>[<xref rid="B133-ijms-18-01242" ref-type="bibr">133</xref>]</td></tr><tr><td align="center" valign="top" rowspan="1" colspan="1"><italic>Allium sativum</italic> lectin</td><td align="center" valign="top" rowspan="1" colspan="1">Aminopeptidase <break></break>Cadherin-N <break></break>Polycalin <break></break>Alkaline phosphatase <break></break>Cytochrome P450</td><td align="center" valign="top" rowspan="1" colspan="1"><italic>Helicoverpa</italic><break></break><italic>Armigera</italic></td><td align="center" valign="top" rowspan="1" colspan="1">[<xref rid="B134-ijms-18-01242" ref-type="bibr">134</xref>]</td></tr><tr><td align="center" valign="top" style="border-bottom:solid thin" rowspan="1" colspan="1"></td><td align="center" valign="top" style="border-bottom:solid thin" rowspan="1" colspan="1">Alanyl <break></break>Aminopeptidase N<break></break>Sucrase</td><td align="center" valign="top" style="border-bottom:solid thin" rowspan="1" colspan="1"><italic>Acyrthosiphon</italic><break></break><italic>Pisum</italic></td><td align="center" valign="top" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B134-ijms-18-01242" ref-type="bibr">134</xref>]</td></tr></tbody></table></table-wrap></floats-group></pmc></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/CovidV2/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000B05 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 000B05 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Sante
|area= CovidV2
|flux= Pmc
|étape= Corpus
|type= RBID
|clé= PMC:5486065
|texte= Legume Lectins: Proteins with Diverse Applications
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/RBID.i -Sk "pubmed:28604616" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a CovidV2
| This area was generated with Dilib version V0.6.33. |  |