Legume Lectins: Proteins with Diverse Applications
Identifieur interne : 000637 ( Ncbi/Merge ); précédent : 000636; suivant : 000638Legume 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
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<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">000780</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000780</idno><idno type="wicri:Area/Pmc/Curation">000780</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000780</idno><idno type="wicri:Area/Pmc/Checkpoint">000196</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000196</idno><idno type="wicri:Area/Ncbi/Merge">000637</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. 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<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><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><affiliations><list></list><tree><noCountry><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><name sortKey="Lagarda Diaz, Irlanda" sort="Lagarda Diaz, Irlanda" uniqKey="Lagarda Diaz I" first="Irlanda" last="Lagarda-Diaz">Irlanda Lagarda-Diaz</name><name sortKey="Vazquez Moreno, Luz" sort="Vazquez Moreno, Luz" uniqKey="Vazquez Moreno L" first="Luz" last="Vazquez-Moreno">Luz Vazquez-Moreno</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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