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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Soluble Host Defense Lectins in Innate Immunity to Influenza Virus</title><author><name sortKey="Ng, Wy Ching" sort="Ng, Wy Ching" uniqKey="Ng W" first="Wy Ching" last="Ng">Wy Ching Ng</name><affiliation><nlm:aff id="I1">Department of Microbiology and Immunology, The University of Melbourne, Parkville, VIC 3010, Australia</nlm:aff></affiliation></author><author><name sortKey="Tate, Michelle D" sort="Tate, Michelle D" uniqKey="Tate M" first="Michelle D." last="Tate">Michelle D. Tate</name><affiliation><nlm:aff id="I1">Department of Microbiology and Immunology, The University of Melbourne, Parkville, VIC 3010, Australia</nlm:aff></affiliation><affiliation><nlm:aff id="I2">Centre for Innate Immunity and Infectious Disease, Monash Institute of Medical Research, Monash University, Clayton, VIC 3168, Australia</nlm:aff></affiliation></author><author><name sortKey="Brooks, Andrew G" sort="Brooks, Andrew G" uniqKey="Brooks A" first="Andrew G." last="Brooks">Andrew G. Brooks</name><affiliation><nlm:aff id="I1">Department of Microbiology and Immunology, The University of Melbourne, Parkville, VIC 3010, Australia</nlm:aff></affiliation></author><author><name sortKey="Reading, Patrick C" sort="Reading, Patrick C" uniqKey="Reading P" first="Patrick C." last="Reading">Patrick C. Reading</name><affiliation><nlm:aff id="I1">Department of Microbiology and Immunology, The University of Melbourne, Parkville, VIC 3010, Australia</nlm:aff></affiliation><affiliation><nlm:aff id="I3">WHO Collaborating Centre for Reference and Research on Influenza, Victorian Infectious Diseases Reference Laboratory, North Melbourne, VIC 3051, Australia</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22665991</idno><idno type="pmc">3362216</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3362216</idno><idno type="RBID">PMC:3362216</idno><idno type="doi">10.1155/2012/732191</idno><date when="2012">2012</date><idno type="wicri:Area/Pmc/Corpus">000D87</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000D87</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Soluble Host Defense Lectins in Innate Immunity to Influenza Virus</title><author><name sortKey="Ng, Wy Ching" sort="Ng, Wy Ching" uniqKey="Ng W" first="Wy Ching" last="Ng">Wy Ching Ng</name><affiliation><nlm:aff id="I1">Department of Microbiology and Immunology, The University of Melbourne, Parkville, VIC 3010, Australia</nlm:aff></affiliation></author><author><name sortKey="Tate, Michelle D" sort="Tate, Michelle D" uniqKey="Tate M" first="Michelle D." last="Tate">Michelle D. Tate</name><affiliation><nlm:aff id="I1">Department of Microbiology and Immunology, The University of Melbourne, Parkville, VIC 3010, Australia</nlm:aff></affiliation><affiliation><nlm:aff id="I2">Centre for Innate Immunity and Infectious Disease, Monash Institute of Medical Research, Monash University, Clayton, VIC 3168, Australia</nlm:aff></affiliation></author><author><name sortKey="Brooks, Andrew G" sort="Brooks, Andrew G" uniqKey="Brooks A" first="Andrew G." last="Brooks">Andrew G. Brooks</name><affiliation><nlm:aff id="I1">Department of Microbiology and Immunology, The University of Melbourne, Parkville, VIC 3010, Australia</nlm:aff></affiliation></author><author><name sortKey="Reading, Patrick C" sort="Reading, Patrick C" uniqKey="Reading P" first="Patrick C." last="Reading">Patrick C. Reading</name><affiliation><nlm:aff id="I1">Department of Microbiology and Immunology, The University of Melbourne, Parkville, VIC 3010, Australia</nlm:aff></affiliation><affiliation><nlm:aff id="I3">WHO Collaborating Centre for Reference and Research on Influenza, Victorian Infectious Diseases Reference Laboratory, North Melbourne, VIC 3051, Australia</nlm:aff></affiliation></author></analytic><series><title level="j">Journal of Biomedicine and Biotechnology</title><idno type="ISSN">1110-7243</idno><idno type="eISSN">1110-7251</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Host defenses against viral infections depend on a complex interplay of innate (nonspecific) and adaptive (specific) components. In the early stages of infection, innate mechanisms represent the main line of host defense, acting to limit the spread of virus in host tissues prior to the induction of the adaptive immune response. Serum and lung fluids contain a range of lectins capable of recognizing and destroying influenza A viruses (IAV). Herein, we review the mechanisms by which soluble endogenous lectins mediate anti-IAV activity, including their role in modulating IAV-induced inflammation and disease and their potential as prophylactic and/or therapeutic treatments during severe IAV-induced disease.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Barker, Wh" uniqKey="Barker W">WH Barker</name></author><author><name sortKey="Mullooly, Jp" uniqKey="Mullooly J">JP Mullooly</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wright, Pf" uniqKey="Wright P">PF Wright</name></author><author><name sortKey="Neumann, G" uniqKey="Neumann G">G Neumann</name></author><author><name sortKey="Kawaoka, Y" uniqKey="Kawaoka Y">Y Kawaoka</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Fouchier, Ram" uniqKey="Fouchier R">RAM Fouchier</name></author><author><name sortKey="Munster, V" uniqKey="Munster V">V Munster</name></author><author><name sortKey="Wallensten, A" uniqKey="Wallensten A">A Wallensten</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Murphy, Br" uniqKey="Murphy B">BR Murphy</name></author><author><name sortKey="Webster, Rg" uniqKey="Webster R">RG Webster</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Skehel, Jj" uniqKey="Skehel J">JJ Skehel</name></author><author><name sortKey="Wiley, Dc" uniqKey="Wiley D">DC Wiley</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Gong, J" uniqKey="Gong J">J Gong</name></author><author><name sortKey="Xu, W" uniqKey="Xu W">W Xu</name></author><author><name sortKey="Zhang, J" uniqKey="Zhang J">J Zhang</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Mitnaul, Lj" uniqKey="Mitnaul L">LJ Mitnaul</name></author><author><name sortKey="Matrosovich, Mn" uniqKey="Matrosovich M">MN Matrosovich</name></author><author><name sortKey="Castrucci, Mr" uniqKey="Castrucci M">MR Castrucci</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wagner, R" uniqKey="Wagner R">R Wagner</name></author><author><name sortKey="Matrosovich, M" uniqKey="Matrosovich M">M Matrosovich</name></author><author><name sortKey="Klenk, Hd" uniqKey="Klenk H">HD Klenk</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Basak, S" uniqKey="Basak S">S Basak</name></author><author><name sortKey="Pritchard, Dg" uniqKey="Pritchard D">DG Pritchard</name></author><author><name sortKey="Brown, As" uniqKey="Brown A">AS Brown</name></author><author><name sortKey="Compans, Rw" uniqKey="Compans R">RW Compans</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ward, Cw" uniqKey="Ward C">CW Ward</name></author><author><name sortKey="Dopheide, Ta" uniqKey="Dopheide T">TA Dopheide</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Imperiali, B" uniqKey="Imperiali B">B Imperiali</name></author><author><name sortKey="Hendrickson, Tl" uniqKey="Hendrickson T">TL Hendrickson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kornfeld, R" uniqKey="Kornfeld R">R Kornfeld</name></author><author><name sortKey="Kornfeld, S" uniqKey="Kornfeld S">S Kornfeld</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Basak, S" uniqKey="Basak S">S Basak</name></author><author><name sortKey="Tomana, M" uniqKey="Tomana M">M Tomana</name></author><author><name sortKey="Compans, Rw" uniqKey="Compans R">RW Compans</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Nakamura, K" uniqKey="Nakamura K">K Nakamura</name></author><author><name sortKey="Compans, Rw" uniqKey="Compans R">RW Compans</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Abe, Y" uniqKey="Abe Y">Y Abe</name></author><author><name sortKey="Takashita, E" uniqKey="Takashita E">E Takashita</name></author><author><name sortKey="Sugawara, K" uniqKey="Sugawara K">K Sugawara</name></author><author><name sortKey="Matsuzaki, Y" uniqKey="Matsuzaki Y">Y Matsuzaki</name></author><author><name sortKey="Muraki, Y" uniqKey="Muraki Y">Y Muraki</name></author><author><name sortKey="Hongo, S" uniqKey="Hongo S">S Hongo</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Skehel, Jj" uniqKey="Skehel J">JJ Skehel</name></author><author><name sortKey="Stevens, Dj" uniqKey="Stevens D">DJ Stevens</name></author><author><name sortKey="Daniels, Rs" uniqKey="Daniels R">RS Daniels</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wei, Cj" uniqKey="Wei C">CJ Wei</name></author><author><name sortKey="Boyington, Jc" uniqKey="Boyington J">JC Boyington</name></author><author><name sortKey="Dai, K" uniqKey="Dai K">K Dai</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sun, S" uniqKey="Sun S">S Sun</name></author><author><name sortKey="Wang, Q" uniqKey="Wang Q">Q Wang</name></author><author><name sortKey="Zhao, F" uniqKey="Zhao F">F Zhao</name></author><author><name sortKey="Chen, W" uniqKey="Chen W">W Chen</name></author><author><name sortKey="Li, Z" uniqKey="Li Z">Z Li</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zhang, M" uniqKey="Zhang M">M Zhang</name></author><author><name sortKey="Gaschen, B" uniqKey="Gaschen B">B Gaschen</name></author><author><name sortKey="Blay, W" uniqKey="Blay W">W Blay</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Drickamer, K" uniqKey="Drickamer K">K Drickamer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Drickamer, K" uniqKey="Drickamer K">K Drickamer</name></author><author><name sortKey="Taylor, Me" uniqKey="Taylor M">ME Taylor</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Drickamer, K" uniqKey="Drickamer K">K Drickamer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Veldhuizen, Eja" uniqKey="Veldhuizen E">EJA Veldhuizen</name></author><author><name sortKey="Van Eijk, M" uniqKey="Van Eijk M">M Van Eijk</name></author><author><name sortKey="Haagsman, Hp" uniqKey="Haagsman H">HP Haagsman</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Londrigan, Sl" uniqKey="Londrigan S">SL Londrigan</name></author><author><name sortKey="Turville, Sg" uniqKey="Turville S">SG Turville</name></author><author><name sortKey="Tate, Md" uniqKey="Tate M">MD Tate</name></author><author><name sortKey="Deng, Y M" uniqKey="Deng Y">Y-M Deng</name></author><author><name sortKey="Brooks, Ag" uniqKey="Brooks A">AG Brooks</name></author><author><name sortKey="Reading, Pc" uniqKey="Reading P">PC Reading</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Upham, Jp" uniqKey="Upham J">JP Upham</name></author><author><name sortKey="Pickett, D" uniqKey="Pickett D">D Pickett</name></author><author><name sortKey="Irimura, T" uniqKey="Irimura T">T Irimura</name></author><author><name sortKey="Anders, Em" uniqKey="Anders E">EM Anders</name></author><author><name sortKey="Reading, Pc" uniqKey="Reading P">PC Reading</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rabinovich, Ga" uniqKey="Rabinovich G">GA Rabinovich</name></author><author><name sortKey="Liu, Ft" uniqKey="Liu F">FT Liu</name></author><author><name sortKey="Hirashima, M" uniqKey="Hirashima M">M Hirashima</name></author><author><name sortKey="Anderson, A" uniqKey="Anderson A">A Anderson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Yang, Ry" uniqKey="Yang R">RY Yang</name></author><author><name sortKey="Rabinovich, Ga" uniqKey="Rabinovich G">GA Rabinovich</name></author><author><name sortKey="Liu, Ft" uniqKey="Liu F">FT Liu</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Yang, M L" uniqKey="Yang M">M-L Yang</name></author><author><name sortKey="Chen, Y H" uniqKey="Chen Y">Y-H Chen</name></author><author><name sortKey="Wang, S W" uniqKey="Wang S">S-W Wang</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Mantovani, A" uniqKey="Mantovani A">A Mantovani</name></author><author><name sortKey="Garlanda, C" uniqKey="Garlanda C">C Garlanda</name></author><author><name sortKey="Doni, A" uniqKey="Doni A">A Doni</name></author><author><name sortKey="Bottazzi, B" uniqKey="Bottazzi B">B Bottazzi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Inforzato, A" uniqKey="Inforzato A">A Inforzato</name></author><author><name sortKey="Bottazzi, B" uniqKey="Bottazzi B">B Bottazzi</name></author><author><name sortKey="Garlanda, C" uniqKey="Garlanda C">C Garlanda</name></author><author><name sortKey="Valentino, S" uniqKey="Valentino S">S Valentino</name></author><author><name sortKey="Mantovani, A" uniqKey="Mantovani A">A Mantovani</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hind, Crk" uniqKey="Hind C">CRK Hind</name></author><author><name sortKey="Collins, Pm" uniqKey="Collins P">PM Collins</name></author><author><name sortKey="Renn, D" uniqKey="Renn D">D Renn</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Andersen, O" uniqKey="Andersen O">O Andersen</name></author><author><name sortKey="Ravn, Kv" uniqKey="Ravn K">KV Ravn</name></author><author><name sortKey="S Rensen, Ij" uniqKey="S Rensen I">IJ Sørensen</name></author><author><name sortKey="Jonson, G" uniqKey="Jonson G">G Jonson</name></author><author><name sortKey="Holm Nielsen, E" uniqKey="Holm Nielsen E">E Holm Nielsen</name></author><author><name sortKey="Svehag, S E" uniqKey="Svehag S">S-E Svehag</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Horvath, A" uniqKey="Horvath A">A Horváth</name></author><author><name sortKey="Andersen, I" uniqKey="Andersen I">I Andersen</name></author><author><name sortKey="Junker, K" uniqKey="Junker K">K Junker</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Seaton, Ba" uniqKey="Seaton B">BA Seaton</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author><author><name sortKey="Mccormack, Fx" uniqKey="Mccormack F">FX McCormack</name></author><author><name sortKey="Head, Jf" uniqKey="Head J">JF Head</name></author><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="Mendelsohn, R" uniqKey="Mendelsohn R">R Mendelsohn</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Gupta, G" uniqKey="Gupta G">G Gupta</name></author><author><name sortKey="Surolia, A" uniqKey="Surolia A">A Surolia</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Van De Wetering, Jk" uniqKey="Van De Wetering J">JK Van De Wetering</name></author><author><name sortKey="Van Golde, Lmg" uniqKey="Van Golde L">LMG Van Golde</name></author><author><name sortKey="Batenburg, Jj" uniqKey="Batenburg J">JJ Batenburg</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Gottschalk, A" uniqKey="Gottschalk A">A Gottschalk</name></author><author><name sortKey="Belyavin, G" uniqKey="Belyavin G">G Belyavin</name></author><author><name sortKey="Biddle, F" uniqKey="Biddle F">F Biddle</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Anders, Em" uniqKey="Anders E">EM Anders</name></author><author><name sortKey="Hartley, Ca" uniqKey="Hartley C">CA Hartley</name></author><author><name sortKey="Jackson, Dc" uniqKey="Jackson D">DC Jackson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartley, Ca" uniqKey="Hartley C">CA Hartley</name></author><author><name sortKey="Jackson, Dc" uniqKey="Jackson D">DC Jackson</name></author><author><name sortKey="Anders, Em" uniqKey="Anders E">EM Anders</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hanaoka, K" uniqKey="Hanaoka K">K Hanaoka</name></author><author><name sortKey="Pritchett, Tj" uniqKey="Pritchett T">TJ Pritchett</name></author><author><name sortKey="Takasaki, S" uniqKey="Takasaki S">S Takasaki</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Pritchett, Tj" uniqKey="Pritchett T">TJ Pritchett</name></author><author><name sortKey="Paulson, Jc" uniqKey="Paulson J">JC Paulson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="Sastry, Kn" uniqKey="Sastry K">KN Sastry</name></author><author><name sortKey="Chang, D" uniqKey="Chang D">D Chang</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Reading, Pc" uniqKey="Reading P">PC Reading</name></author><author><name sortKey="Morey, Ls" uniqKey="Morey L">LS Morey</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author><author><name sortKey="Anders, Em" uniqKey="Anders E">EM Anders</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Benne, Ca" uniqKey="Benne C">CA Benne</name></author><author><name sortKey="Kraaijeveld, Ca" uniqKey="Kraaijeveld C">CA Kraaijeveld</name></author><author><name sortKey="Van Strijp, Jag" uniqKey="Van Strijp J">JAG Van Strijp</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Mikerov, An" uniqKey="Mikerov A">AN Mikerov</name></author><author><name sortKey="White, M" uniqKey="White M">M White</name></author><author><name sortKey="Hartshorn, K" uniqKey="Hartshorn K">K Hartshorn</name></author><author><name sortKey="Wang, G" uniqKey="Wang G">G Wang</name></author><author><name sortKey="Floros, J" uniqKey="Floros J">J Floros</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hawgood, S" uniqKey="Hawgood S">S Hawgood</name></author><author><name sortKey="Brown, C" uniqKey="Brown C">C Brown</name></author><author><name sortKey="Edmondson, J" uniqKey="Edmondson J">J Edmondson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Levine, Am" uniqKey="Levine A">AM LeVine</name></author><author><name sortKey="Whitsett, Ja" uniqKey="Whitsett J">JA Whitsett</name></author><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author><author><name sortKey="Korfhagen, Tr" uniqKey="Korfhagen T">TR Korfhagen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tate, Md" uniqKey="Tate M">MD Tate</name></author><author><name sortKey="Brooks, Ag" uniqKey="Brooks A">AG Brooks</name></author><author><name sortKey="Reading, Pc" uniqKey="Reading P">PC Reading</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Vigerust, Dj" uniqKey="Vigerust D">DJ Vigerust</name></author><author><name sortKey="Ulett, Kb" uniqKey="Ulett K">KB Ulett</name></author><author><name sortKey="Boyd, Kl" uniqKey="Boyd K">KL Boyd</name></author><author><name sortKey="Madsen, J" uniqKey="Madsen J">J Madsen</name></author><author><name sortKey="Hawgood, S" uniqKey="Hawgood S">S Hawgood</name></author><author><name sortKey="Mccullers, Ja" uniqKey="Mccullers J">JA McCullers</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Mogues, T" uniqKey="Mogues T">T Mogues</name></author><author><name sortKey="Ligtenberg, T" uniqKey="Ligtenberg T">T Ligtenberg</name></author><author><name sortKey="Crouch, E" uniqKey="Crouch E">E Crouch</name></author><author><name sortKey="Holmskov, U" uniqKey="Holmskov U">U Holmskov</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="Crouch, E" uniqKey="Crouch E">E Crouch</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Crouch, E" uniqKey="Crouch E">E Crouch</name></author><author><name sortKey="Persson, A" uniqKey="Persson A">A Persson</name></author><author><name sortKey="Chang, D" uniqKey="Chang D">D Chang</name></author><author><name sortKey="Heuser, J" uniqKey="Heuser J">J Heuser</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author><author><name sortKey="Smith, K" uniqKey="Smith K">K Smith</name></author><author><name sortKey="Mcdonald, B" uniqKey="Mcdonald B">B McDonald</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tecle, T" uniqKey="Tecle T">T Tecle</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Sorensen, G" uniqKey="Sorensen G">G Sorensen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Tecle, T" uniqKey="Tecle T">T Tecle</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="White, M" uniqKey="White M">M White</name></author><author><name sortKey="Kingma, P" uniqKey="Kingma P">P Kingma</name></author><author><name sortKey="Tecle, T" uniqKey="Tecle T">T Tecle</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="Webby, R" uniqKey="Webby R">R Webby</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Voelker, Dr" uniqKey="Voelker D">DR Voelker</name></author><author><name sortKey="Coburn, J" uniqKey="Coburn J">J Coburn</name></author><author><name sortKey="Zaner, K" uniqKey="Zaner K">K Zaner</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tecle, T" uniqKey="Tecle T">T Tecle</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="Reid, Kbm" uniqKey="Reid K">KBM Reid</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hirche, To" uniqKey="Hirche T">TO Hirche</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author><author><name sortKey="Espinola, M" uniqKey="Espinola M">M Espinola</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Tecle, T" uniqKey="Tecle T">T Tecle</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Leth Larsen, R" uniqKey="Leth Larsen R">R Leth-Larsen</name></author><author><name sortKey="Garred, P" uniqKey="Garred P">P Garred</name></author><author><name sortKey="Jensenius, H" uniqKey="Jensenius H">H Jensenius</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tate, Md" uniqKey="Tate M">MD Tate</name></author><author><name sortKey="Job, Er" uniqKey="Job E">ER Job</name></author><author><name sortKey="Brooks, Ag" uniqKey="Brooks A">AG Brooks</name></author><author><name sortKey="Reading, Pc" uniqKey="Reading P">PC Reading</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tate, Md" uniqKey="Tate M">MD Tate</name></author><author><name sortKey="Brooks, Ag" uniqKey="Brooks A">AG Brooks</name></author><author><name sortKey="Reading, Pc" uniqKey="Reading P">PC Reading</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ikegami, M" uniqKey="Ikegami M">M Ikegami</name></author><author><name sortKey="Na, Cl" uniqKey="Na C">CL Na</name></author><author><name sortKey="Korfhagen, Tr" uniqKey="Korfhagen T">TR Korfhagen</name></author><author><name sortKey="Whitsett, Ja" uniqKey="Whitsett J">JA Whitsett</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ikegami, M" uniqKey="Ikegami M">M Ikegami</name></author><author><name sortKey="Whitsett, Ja" uniqKey="Whitsett J">JA Whitsett</name></author><author><name sortKey="Jobe, A" uniqKey="Jobe A">A Jobe</name></author><author><name sortKey="Ross, G" uniqKey="Ross G">G Ross</name></author><author><name sortKey="Fisher, J" uniqKey="Fisher J">J Fisher</name></author><author><name sortKey="Korfhagen, T" uniqKey="Korfhagen T">T Korfhagen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Korfhagen, Tr" uniqKey="Korfhagen T">TR Korfhagen</name></author><author><name sortKey="Sheftelyevich, V" uniqKey="Sheftelyevich V">V Sheftelyevich</name></author><author><name sortKey="Burhans, Ms" uniqKey="Burhans M">MS Burhans</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kingma, Ps" uniqKey="Kingma P">PS Kingma</name></author><author><name sortKey="Zhang, L" uniqKey="Zhang L">L Zhang</name></author><author><name sortKey="Ikegami, M" uniqKey="Ikegami M">M Ikegami</name></author><author><name sortKey="Hartshorn, K" uniqKey="Hartshorn K">K Hartshorn</name></author><author><name sortKey="Mccormack, Fx" uniqKey="Mccormack F">FX McCormack</name></author><author><name sortKey="Whitsett, Ja" uniqKey="Whitsett J">JA Whitsett</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zhang, L" uniqKey="Zhang L">L Zhang</name></author><author><name sortKey="Ikegami, M" uniqKey="Ikegami M">M Ikegami</name></author><author><name sortKey="Korfhagen, Tr" uniqKey="Korfhagen T">TR Korfhagen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Reading, Pc" uniqKey="Reading P">PC Reading</name></author><author><name sortKey="Allison, J" uniqKey="Allison J">J Allison</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author><author><name sortKey="Margot Anders, E" uniqKey="Margot Anders E">E Margot Anders</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Takahashi, K" uniqKey="Takahashi K">K Takahashi</name></author><author><name sortKey="Ip, Wke" uniqKey="Ip W">WKE Ip</name></author><author><name sortKey="Michelow, Ic" uniqKey="Michelow I">IC Michelow</name></author><author><name sortKey="Ezekowitz, Rab" uniqKey="Ezekowitz R">RAB Ezekowitz</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Haurum, Js" uniqKey="Haurum J">JS Haurum</name></author><author><name sortKey="Thiel, S" uniqKey="Thiel S">S Thiel</name></author><author><name sortKey="Haagsman, Hp" uniqKey="Haagsman H">HP Haagsman</name></author><author><name sortKey="Laursen, Sb" uniqKey="Laursen S">SB Laursen</name></author><author><name sortKey="Larsen, B" uniqKey="Larsen B">B Larsen</name></author><author><name sortKey="Jensenius, Jc" uniqKey="Jensenius J">JC Jensenius</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Fujita, T" uniqKey="Fujita T">T Fujita</name></author><author><name sortKey="Matsushita, M" uniqKey="Matsushita M">M Matsushita</name></author><author><name sortKey="Endo, Y" uniqKey="Endo Y">Y Endo</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Takahashi, M" uniqKey="Takahashi M">M Takahashi</name></author><author><name sortKey="Mori, S" uniqKey="Mori S">S Mori</name></author><author><name sortKey="Shigeta, S" uniqKey="Shigeta S">S Shigeta</name></author><author><name sortKey="Fujita, T" uniqKey="Fujita T">T Fujita</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Krarup, A" uniqKey="Krarup A">A Krarup</name></author><author><name sortKey="Wallis, R" uniqKey="Wallis R">R Wallis</name></author><author><name sortKey="Presanis, Js" uniqKey="Presanis J">JS Presanis</name></author><author><name sortKey="Gal, P" uniqKey="Gal P">P Gál</name></author><author><name sortKey="Sim, Rb" uniqKey="Sim R">RB Sim</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Presanis, Js" uniqKey="Presanis J">JS Presanis</name></author><author><name sortKey="Hajela, K" uniqKey="Hajela K">K Hajela</name></author><author><name sortKey="Ambrus, G" uniqKey="Ambrus G">G Ambrus</name></author><author><name sortKey="Gal, P" uniqKey="Gal P">P Gál</name></author><author><name sortKey="Sim, Rb" uniqKey="Sim R">RB Sim</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sastry, R" uniqKey="Sastry R">R Sastry</name></author><author><name sortKey="Wang, Js" uniqKey="Wang J">JS Wang</name></author><author><name sortKey="Brown, Dc" uniqKey="Brown D">DC Brown</name></author><author><name sortKey="Ezekowitz, Ra" uniqKey="Ezekowitz R">RA Ezekowitz</name></author><author><name sortKey="Tauber, Ai" uniqKey="Tauber A">AI Tauber</name></author><author><name sortKey="Sastry, Kn" uniqKey="Sastry K">KN Sastry</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Takahashi, K" uniqKey="Takahashi K">K Takahashi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hansen, S" uniqKey="Hansen S">S Hansen</name></author><author><name sortKey="Thiel, S" uniqKey="Thiel S">S Thiel</name></author><author><name sortKey="Willis, A" uniqKey="Willis A">A Willis</name></author><author><name sortKey="Holmskov, U" uniqKey="Holmskov U">U Holmskov</name></author><author><name sortKey="Jensenius, Jc" uniqKey="Jensenius J">JC Jensenius</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Eisen, Dp" uniqKey="Eisen D">DP Eisen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Fidler, Kj" uniqKey="Fidler K">KJ Fidler</name></author><author><name sortKey="Hilliard, Tn" uniqKey="Hilliard T">TN Hilliard</name></author><author><name sortKey="Bush, A" uniqKey="Bush A">A Bush</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Chang, Wc" uniqKey="Chang W">WC Chang</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Moyo, P" uniqKey="Moyo P">P Moyo</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Shepherd, V" uniqKey="Shepherd V">V Shepherd</name></author><author><name sortKey="Reid, K" uniqKey="Reid K">K Reid</name></author><author><name sortKey="Jensenius, Jg" uniqKey="Jensenius J">JG Jensenius</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="Sastry, K" uniqKey="Sastry K">K Sastry</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Job, Er" uniqKey="Job E">ER Job</name></author><author><name sortKey="Deng, Ym" uniqKey="Deng Y">YM Deng</name></author><author><name sortKey="Tate, Md" uniqKey="Tate M">MD Tate</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kase, T" uniqKey="Kase T">T Kase</name></author><author><name sortKey="Suzuki, Y" uniqKey="Suzuki Y">Y Suzuki</name></author><author><name sortKey="Kawai, T" uniqKey="Kawai T">T Kawai</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Anders, Em" uniqKey="Anders E">EM Anders</name></author><author><name sortKey="Hartley, Ca" uniqKey="Hartley C">CA Hartley</name></author><author><name sortKey="Reading, Pc" uniqKey="Reading P">PC Reading</name></author><author><name sortKey="Ezekowitz, Rab" uniqKey="Ezekowitz R">RAB Ezekowitz</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Reading, Pc" uniqKey="Reading P">PC Reading</name></author><author><name sortKey="Hartley, Ca" uniqKey="Hartley C">CA Hartley</name></author><author><name sortKey="Ezekowitz, Rab" uniqKey="Ezekowitz R">RAB Ezekowitz</name></author><author><name sortKey="Anders, Em" uniqKey="Anders E">EM Anders</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Malhotra, R" uniqKey="Malhotra R">R Malhotra</name></author><author><name sortKey="Haurum, Js" uniqKey="Haurum J">JS Haurum</name></author><author><name sortKey="Thiel, S" uniqKey="Thiel S">S Thiel</name></author><author><name sortKey="Sim, Rb" uniqKey="Sim R">RB Sim</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tokunaga, H" uniqKey="Tokunaga H">H Tokunaga</name></author><author><name sortKey="Ushirogawa, H" uniqKey="Ushirogawa H">H Ushirogawa</name></author><author><name sortKey="Ohuchi, M" uniqKey="Ohuchi M">M Ohuchi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ling, Mt" uniqKey="Ling M">MT Ling</name></author><author><name sortKey="Tu, W" uniqKey="Tu W">W Tu</name></author><author><name sortKey="Han, Y" uniqKey="Han Y">Y Han</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ohtani, K" uniqKey="Ohtani K">K Ohtani</name></author><author><name sortKey="Suzuki, Y" uniqKey="Suzuki Y">Y Suzuki</name></author><author><name sortKey="Eda, S" uniqKey="Eda S">S Eda</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ohtani, K" uniqKey="Ohtani K">K Ohtani</name></author><author><name sortKey="Suzuki, Y" uniqKey="Suzuki Y">Y Suzuki</name></author><author><name sortKey="Eda, S" uniqKey="Eda S">S Eda</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hansen, S" uniqKey="Hansen S">S Hansen</name></author><author><name sortKey="Selman, L" uniqKey="Selman L">L Selman</name></author><author><name sortKey="Palaniyar, N" uniqKey="Palaniyar N">N Palaniyar</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Motomura, W" uniqKey="Motomura W">W Motomura</name></author><author><name sortKey="Yoshizaki, T" uniqKey="Yoshizaki T">T Yoshizaki</name></author><author><name sortKey="Ohtani, K" uniqKey="Ohtani K">K Ohtani</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Yoshizaki, T" uniqKey="Yoshizaki T">T Yoshizaki</name></author><author><name sortKey="Ohtani, K" uniqKey="Ohtani K">K Ohtani</name></author><author><name sortKey="Motomura, W" uniqKey="Motomura W">W Motomura</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bordet, J" uniqKey="Bordet J">J Bordet</name></author><author><name sortKey="Gay, Fp" uniqKey="Gay F">FP Gay</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lachmann, Pj" uniqKey="Lachmann P">PJ Lachmann</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lachmann, Pj" uniqKey="Lachmann P">PJ Lachmann</name></author><author><name sortKey="Muller Eberhard, Hj" uniqKey="Muller Eberhard H">HJ Müller-Eberhard</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hansen, S" uniqKey="Hansen S">S Hansen</name></author><author><name sortKey="Holmskov, U" uniqKey="Holmskov U">U Holmskov</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="Holmskov, U" uniqKey="Holmskov U">U Holmskov</name></author><author><name sortKey="Hansen, S" uniqKey="Hansen S">S Hansen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rothmann, Ab" uniqKey="Rothmann A">AB Rothmann</name></author><author><name sortKey="Mortensen, Hd" uniqKey="Mortensen H">HD Mortensen</name></author><author><name sortKey="Holmskov, U" uniqKey="Holmskov U">U Holmskov</name></author><author><name sortKey="Hojrup, P" uniqKey="Hojrup P">P Hojrup</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wakamiya, N" uniqKey="Wakamiya N">N Wakamiya</name></author><author><name sortKey="Okuno, Y" uniqKey="Okuno Y">Y Okuno</name></author><author><name sortKey="Sasao, F" uniqKey="Sasao F">F Sasao</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Eda, S" uniqKey="Eda S">S Eda</name></author><author><name sortKey="Suzuki, Y" uniqKey="Suzuki Y">Y Suzuki</name></author><author><name sortKey="Kase, T" uniqKey="Kase T">T Kase</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="Sastry, K" uniqKey="Sastry K">K Sastry</name></author><author><name sortKey="Brown, D" uniqKey="Brown D">D Brown</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kawai, T" uniqKey="Kawai T">T Kawai</name></author><author><name sortKey="Kase, T" uniqKey="Kase T">T Kase</name></author><author><name sortKey="Suzuki, Y" uniqKey="Suzuki Y">Y Suzuki</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Suzuki, Y" uniqKey="Suzuki Y">Y Suzuki</name></author><author><name sortKey="Eda, S" uniqKey="Eda S">S Eda</name></author><author><name sortKey="Kawai, T" uniqKey="Kawai T">T Kawai</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Eda, S" uniqKey="Eda S">S Eda</name></author><author><name sortKey="Suzuki, Y" uniqKey="Suzuki Y">Y Suzuki</name></author><author><name sortKey="Kawai, T" uniqKey="Kawai T">T Kawai</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Eda, S" uniqKey="Eda S">S Eda</name></author><author><name sortKey="Suzuki, Y" uniqKey="Suzuki Y">Y Suzuki</name></author><author><name sortKey="Kawai, T" uniqKey="Kawai T">T Kawai</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Holmskov, U" uniqKey="Holmskov U">U Holmskov</name></author><author><name sortKey="Teisner, B" uniqKey="Teisner B">B Teisner</name></author><author><name sortKey="Willis, Ac" uniqKey="Willis A">AC Willis</name></author><author><name sortKey="Reid, Kbm" uniqKey="Reid K">KBM Reid</name></author><author><name sortKey="Jensenius, Jc" uniqKey="Jensenius J">JC Jensenius</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Holmskov, U" uniqKey="Holmskov U">U Holmskov</name></author><author><name sortKey="Laursen, Sb" uniqKey="Laursen S">SB Laursen</name></author><author><name sortKey="Malhotra, R" uniqKey="Malhotra R">R Malhotra</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Crouch, E" uniqKey="Crouch E">E Crouch</name></author><author><name sortKey="Chang, D" uniqKey="Chang D">D Chang</name></author><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Smith, K" uniqKey="Smith K">K Smith</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Tecle, T" uniqKey="Tecle T">T Tecle</name></author><author><name sortKey="Sorensen, G" uniqKey="Sorensen G">G Sorensen</name></author><author><name sortKey="Holmskov, U" uniqKey="Holmskov U">U Holmskov</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Van Eijk, M" uniqKey="Van Eijk M">M Van Eijk</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Batenburg, Jj" uniqKey="Batenburg J">JJ Batenburg</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Van Eijk, M" uniqKey="Van Eijk M">M Van Eijk</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Crouch, Ec" uniqKey="Crouch E">EC Crouch</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hillaire, Mlb" uniqKey="Hillaire M">MLB Hillaire</name></author><author><name sortKey="Van Eijk, M" uniqKey="Van Eijk M">M van Eijk</name></author><author><name sortKey="Van Trierum, Se" uniqKey="Van Trierum S">SE van Trierum</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Brown, Ih" uniqKey="Brown I">IH Brown</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Laursen, Sb" uniqKey="Laursen S">SB Laursen</name></author><author><name sortKey="Dalgaard, Ts" uniqKey="Dalgaard T">TS Dalgaard</name></author><author><name sortKey="Thiel, S" uniqKey="Thiel S">S Thiel</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hogenkamp, A" uniqKey="Hogenkamp A">A Hogenkamp</name></author><author><name sortKey="Van Eijk, M" uniqKey="Van Eijk M">M Van Eijk</name></author><author><name sortKey="Van Dijk, A" uniqKey="Van Dijk A">A Van Dijk</name></author><author><name sortKey="Van Asten, Ajam" uniqKey="Van Asten A">AJAM Van Asten</name></author><author><name sortKey="Veldhuizen, Eja" uniqKey="Veldhuizen E">EJA Veldhuizen</name></author><author><name sortKey="Haagsman, Hp" uniqKey="Haagsman H">HP Haagsman</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hughes, Al" uniqKey="Hughes A">AL Hughes</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hogenkamp, A" uniqKey="Hogenkamp A">A Hogenkamp</name></author><author><name sortKey="Isohadouten, N" uniqKey="Isohadouten N">N Isohadouten</name></author><author><name sortKey="Reemers, Ssn" uniqKey="Reemers S">SSN Reemers</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Reading, Pc" uniqKey="Reading P">PC Reading</name></author><author><name sortKey="Bozza, S" uniqKey="Bozza S">S Bozza</name></author><author><name sortKey="Gilbertson, B" uniqKey="Gilbertson B">B Gilbertson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Igarashi, M" uniqKey="Igarashi M">M Igarashi</name></author><author><name sortKey="Ito, K" uniqKey="Ito K">K Ito</name></author><author><name sortKey="Yoshida, R" uniqKey="Yoshida R">R Yoshida</name></author><author><name sortKey="Tomabechi, D" uniqKey="Tomabechi D">D Tomabechi</name></author><author><name sortKey="Kida, H" uniqKey="Kida H">H Kida</name></author><author><name sortKey="Takada, A" uniqKey="Takada A">A Takada</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Qi, L" uniqKey="Qi L">L Qi</name></author><author><name sortKey="Kash, Jc" uniqKey="Kash J">JC Kash</name></author><author><name sortKey="Dugan, Vg" uniqKey="Dugan V">VG Dugan</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Eisen, Dp" uniqKey="Eisen D">DP Eisen</name></author><author><name sortKey="Marshall, C" uniqKey="Marshall C">C Marshall</name></author><author><name sortKey="Dean, Mm" uniqKey="Dean M">MM Dean</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Kongchanagul, A" uniqKey="Kongchanagul A">A Kongchanagul</name></author><author><name sortKey="Suptawiwat, O" uniqKey="Suptawiwat O">O Suptawiwat</name></author><author><name sortKey="Boonarkart, C" uniqKey="Boonarkart C">C Boonarkart</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cameron, Cm" uniqKey="Cameron C">CM Cameron</name></author><author><name sortKey="Cameron, Mj" uniqKey="Cameron M">MJ Cameron</name></author><author><name sortKey="Bermejo Martin, Jf" uniqKey="Bermejo Martin J">JF Bermejo-Martin</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cill Niz, C" uniqKey="Cill Niz C">C Cillóniz</name></author><author><name sortKey="Shinya, K" uniqKey="Shinya K">K Shinya</name></author><author><name sortKey="Peng, X" uniqKey="Peng X">X Peng</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Herbert, J" uniqKey="Herbert J">J Herbert</name></author><author><name sortKey="Hutchinson, Wl" uniqKey="Hutchinson W">WL Hutchinson</name></author><author><name sortKey="Carr, J" uniqKey="Carr J">J Carr</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Crouch, E" uniqKey="Crouch E">E Crouch</name></author><author><name sortKey="Chang, D" uniqKey="Chang D">D Chang</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Chang, Wc" uniqKey="Chang W">WC Chang</name></author><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Gardai, Sj" uniqKey="Gardai S">SJ Gardai</name></author><author><name sortKey="Xiao, Yq" uniqKey="Xiao Y">YQ Xiao</name></author><author><name sortKey="Dickinson, M" uniqKey="Dickinson M">M Dickinson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Crouch, E" uniqKey="Crouch E">E Crouch</name></author><author><name sortKey="Tu, Y" uniqKey="Tu Y">Y Tu</name></author><author><name sortKey="Briner, D" uniqKey="Briner D">D Briner</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Crouch, E" uniqKey="Crouch E">E Crouch</name></author><author><name sortKey="Hartshorn, K" uniqKey="Hartshorn K">K Hartshorn</name></author><author><name sortKey="Horlacher, T" uniqKey="Horlacher T">T Horlacher</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="White, Mr" uniqKey="White M">MR White</name></author><author><name sortKey="Boland, P" uniqKey="Boland P">P Boland</name></author><author><name sortKey="Tecle, T" uniqKey="Tecle T">T Tecle</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Crouch, E" uniqKey="Crouch E">E Crouch</name></author><author><name sortKey="Nikolaidis, N" uniqKey="Nikolaidis N">N Nikolaidis</name></author><author><name sortKey="Mccormack, Fx" uniqKey="Mccormack F">FX McCormack</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Van Eijk, M" uniqKey="Van Eijk M">M Van Eijk</name></author><author><name sortKey="Bruinsma, L" uniqKey="Bruinsma L">L Bruinsma</name></author><author><name sortKey="Hartshorn, Kl" uniqKey="Hartshorn K">KL Hartshorn</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lu, J" uniqKey="Lu J">J Lu</name></author><author><name sortKey="Willis, Ac" uniqKey="Willis A">AC Willis</name></author><author><name sortKey="Reid, Kbm" uniqKey="Reid K">KBM Reid</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hansen, S" uniqKey="Hansen S">S Hansen</name></author><author><name sortKey="Holm, D" uniqKey="Holm D">D Holm</name></author><author><name sortKey="Moeller, V" uniqKey="Moeller V">V Moeller</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lee, Rt" uniqKey="Lee R">RT Lee</name></author><author><name sortKey="Ichikawa, Y" uniqKey="Ichikawa Y">Y Ichikawa</name></author><author><name sortKey="Allen, Hj" uniqKey="Allen H">HJ Allen</name></author><author><name sortKey="Lee, Yc" uniqKey="Lee Y">YC Lee</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Reading, Pc" uniqKey="Reading P">PC Reading</name></author><author><name sortKey="Holmskov, U" uniqKey="Holmskov U">U Holmskov</name></author><author><name sortKey="Anders, Em" uniqKey="Anders E">EM Anders</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">J Biomed Biotechnol</journal-id><journal-id journal-id-type="iso-abbrev">J. Biomed. Biotechnol</journal-id><journal-id journal-id-type="publisher-id">JBB</journal-id><journal-title-group><journal-title>Journal of Biomedicine and Biotechnology</journal-title></journal-title-group><issn pub-type="ppub">1110-7243</issn><issn pub-type="epub">1110-7251</issn><publisher><publisher-name>Hindawi Publishing Corporation</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">22665991</article-id><article-id pub-id-type="pmc">3362216</article-id><article-id pub-id-type="doi">10.1155/2012/732191</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review Article</subject></subj-group></article-categories><title-group><article-title>Soluble Host Defense Lectins in Innate Immunity to Influenza Virus</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Ng</surname><given-names>Wy Ching</given-names></name><xref ref-type="aff" rid="I1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Tate</surname><given-names>Michelle D.</given-names></name><xref ref-type="aff" rid="I1"><sup>1</sup></xref><xref ref-type="aff" rid="I2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Brooks</surname><given-names>Andrew G.</given-names></name><xref ref-type="aff" rid="I1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Reading</surname><given-names>Patrick C.</given-names></name><xref ref-type="aff" rid="I1"><sup>1</sup></xref><xref ref-type="aff" rid="I3"><sup>3</sup></xref><xref ref-type="corresp" rid="cor1">*</xref></contrib></contrib-group><aff id="I1"><sup>1</sup>Department of Microbiology and Immunology, The University of Melbourne, Parkville, VIC 3010, Australia</aff><aff id="I2"><sup>2</sup>Centre for Innate Immunity and Infectious Disease, Monash Institute of Medical Research, Monash University, Clayton, VIC 3168, Australia</aff><aff id="I3"><sup>3</sup>WHO Collaborating Centre for Reference and Research on Influenza, Victorian Infectious Diseases Reference Laboratory, North Melbourne, VIC 3051, Australia</aff><author-notes><corresp id="cor1">*Patrick C. Reading: <email>preading@unimelb.edu.au</email></corresp><fn fn-type="other"><p>Academic Editor: Nobutaka Wakamiya</p></fn></author-notes><pub-date pub-type="ppub"><year>2012</year></pub-date><pub-date pub-type="epub"><day>16</day><month>5</month><year>2012</year></pub-date><volume>2012</volume><elocation-id>732191</elocation-id><history><date date-type="received"><day>20</day><month>12</month><year>2011</year></date><date date-type="accepted"><day>21</day><month>2</month><year>2012</year></date></history><permissions><copyright-statement>Copyright © 2012 Wy Ching Ng et al.</copyright-statement><copyright-year>2012</copyright-year><license license-type="open-access"><license-p>This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</license-p></license></permissions><abstract><p>Host defenses against viral infections depend on a complex interplay of innate (nonspecific) and adaptive (specific) components. In the early stages of infection, innate mechanisms represent the main line of host defense, acting to limit the spread of virus in host tissues prior to the induction of the adaptive immune response. Serum and lung fluids contain a range of lectins capable of recognizing and destroying influenza A viruses (IAV). Herein, we review the mechanisms by which soluble endogenous lectins mediate anti-IAV activity, including their role in modulating IAV-induced inflammation and disease and their potential as prophylactic and/or therapeutic treatments during severe IAV-induced disease.</p></abstract></article-meta></front><body><sec id="sec1"><title>1. General Features of Influenza Virus</title><p> Influenza virus causes a highly contagious, acute infection of the upper and lower respiratory tract that is responsible for millions of deaths annually, predominantly in the elderly and in those with underlying pulmonary and cardiac disease [<xref ref-type="bibr" rid="B1">1</xref>]. Influenza viruses belong to the family <italic>Orthomyxoviridae</italic>, which consists of type A, B, and C influenza viruses, Thogotovirus, and Isavirus. While all 3 types of influenza virus infect humans, only influenza A viruses (IAVs) have the capacity to induce both epidemics and pandemics. Type B influenza viruses are associated with yearly epidemics whereas type C viruses rarely cause severe disease [<xref ref-type="bibr" rid="B2">2</xref>].</p><p>IAV is an enveloped virus with a genome comprising 8 segments of single-stranded, negative sense RNA encoding at least 10 proteins, including hemagglutinin (HA) and neuraminidase (NA), which are expressed on the virion surface. HA and, to a lesser extent, NA represent major targets for recognition by neutralizing antibodies and IAVs are divided into subtypes based on serological and genetic differences in their HA and NA proteins and the genes that encode them. At present, at least 16 HA and 9 NA subtypes of IAV have been identified, all of which are found amongst aquatic birds [<xref ref-type="bibr" rid="B2">2</xref>, <xref ref-type="bibr" rid="B3">3</xref>]. In humans, only certain HA (H1, H2, and H3) and NA (N1 and N2) subtypes have been involved in epidemics and pandemics. Other subtypes of avian or equine origin (e.g., H5N1, H7N7, and H9N2) have infected humans but have not spread efficiently in the human population. These findings do, however, highlight the potential for mutation and/or genetic reassortment to facilitate entry and transmission of novel IAV in the human population.</p><p>Antigenic variation is the mechanism by which new subtypes or strains of IAV emerge in humans (reviewed in [<xref ref-type="bibr" rid="B4">4</xref>]). Antigenic shift is the most profound type of antigenic variation and results in the emergence of a virus that possesses novel HA and/or NA, to which the human population is immunologically naïve. Antigenic drift describes the gradual accumulation of point mutations in the genome of viruses that have been circulating in humans for an extended time. Mutations in viral RNA can lead to changes in the amino acid sequence of HA or NA and variants with changes in key antigenic epitopes will be selected as they can escape neutralization by preexisting antibodies. Antigenic variation via shift (which can result in pandemics) and drift (which can result in epidemics) ensures continued presence of IAV in the human population despite immunity arising from previous vaccination and/or infection.</p><sec sec-type="subsection" id="sec1.1"><title>1.1. Glycosylation of IAV Glycoproteins</title><p>The HA is a trimeric glycoprotein that mediates attachment of IAV to sialic acid (SA) on host cells as well as fusion of the viral and endosomal membranes during cell entry (reviewed in [<xref ref-type="bibr" rid="B5">5</xref>]). NA is a tetramer that enzymatically cleaves SA from glycoproteins, thereby facilitating release of progeny virions from the surface of infected cells and preventing self-aggregation of virus [<xref ref-type="bibr" rid="B6">6</xref>]. The “balance” between the receptor-binding and receptor-destroying activities of HA and NA, respectively, is a critical factor determining the efficiency of host cell infection by different IAV strains [<xref ref-type="bibr" rid="B7">7</xref>, <xref ref-type="bibr" rid="B8">8</xref>].</p><p>Glycosylation of HA and NA occurs in the endoplasmic reticulum (ER) and in the Golgi apparatus in a process similar to that of host cell glycoproteins. HA/NA can express a mixture of high mannose (branched structures terminating in mannose), complex (structures terminating in different combinations of galactose, <italic>N</italic>-acetyl-galactosamine (GalNAc), fucose, or SA), or hybrid-type oligosaccharides [<xref ref-type="bibr" rid="B9">9</xref>, <xref ref-type="bibr" rid="B10">10</xref>]. Biosynthesis of <italic>N</italic>-glycans begins in the rough endoplasmic reticulum (ER) with the transfer of a 14-sugar precursor (usually comprising 3 glucose, 9 mannose, and 2 N-acetyl-glucosamine (GlcNAc) molecules) from a polyisoprenol derivative to the nascent polypeptide chain. Transport of the glycoprotein is accompanied by trimming of terminal glucose and mannose residues in the ER and Golgi to generate high-mannose type glycans. Further processing, including the attachment of additional GlcNAc, fucose, galactose, and SA in the Golgi apparatus, results in the generation of complex and hybrid-type glycans. The oligosaccharides expressed on both HA and NA are exclusively <italic>N</italic>-linked glycans attached to the Asn residue of Asn-X-Ser/Thr, where X represents any amino acid except proline [<xref ref-type="bibr" rid="B11">11</xref>, <xref ref-type="bibr" rid="B12">12</xref>]. Complex oligosaccharides on IAV HA/NA are not sialylated and bear terminal galactose/GlcNAc/fucose due to removal of terminal SA by the viral NA [<xref ref-type="bibr" rid="B13">13</xref>].</p><p>Oligosaccharide diversity of HA/NA depends on the number and location of potential <italic>N</italic>-glycosylation sites in the viral genome as well as the size and composition of the attached glycans. Certain regions of HA have conserved glycosylation sites or must remain free of oligosaccharides for the formation, transport, and/or maintenance of functional HA. The combinations of high-mannose, complex, and hybrid type glycans present on IAV glycoproteins are also determined by the particular biosynthetic and trimming enzymes provided by the host cell in which the virus was grown [<xref ref-type="bibr" rid="B14">14</xref>]. Acquisition of glycosylation sites on HA through antigenic drift has been proposed to mask or modify antigenic sites, thereby preventing recognition by neutralizing antibodies elicited to previous virus strains [<xref ref-type="bibr" rid="B15">15</xref>–<xref ref-type="bibr" rid="B17">17</xref>]. Consequently, pandemic IAV strains derived from zoonotic reservoirs generally have fewer potential <italic>N</italic>-linked glycosylation sites on the head of HA compared to seasonal IAV strains that have circulated in the human population for many years [<xref ref-type="bibr" rid="B17">17</xref>–<xref ref-type="bibr" rid="B19">19</xref>]. In addition to increased numbers, positional conversion of glycosylation sites (i.e., acquisition of a new glycosylation site accompanied by loss of an existing site) represents an additional mechanism proposed to favour evasion of antibody-mediated immunity and therefore persistence of IAV in humans [<xref ref-type="bibr" rid="B18">18</xref>]. The presence of potential <italic>N</italic>-linked glycosylation sites in the amino acid sequence of HA does not always correspond to the presence of attached glycans and some sites may not be glycosylated efficiently. To date, the detailed structure of the glycans carried at particular glycosylation sites has not been well established for most strains of IAV.</p></sec></sec><sec id="sec2"><title>2. General Features of Animal Lectins</title><p>Lectins are nonenzymatic proteins that bind selectively to specific carbohydrate structures. Over the last 20 years, numerous lectins have been isolated and characterized from mammals, birds, and other animals. Unlike plant lectins, which are often grouped into families based on taxonomy, animal lectins often exhibit structural similarities even when derived from diverse phyla. Therefore, animal lectins are generally classified on the basis of an evolutionarily conserved carbohydrate recognition domain (CRD) [<xref ref-type="bibr" rid="B20">20</xref>] and on this basis they can be grouped into families, including C-type, S-type (or galectins), P-type (or Man-6-P lectins), Ig-type (or Siglecs), R-type, and F-type lectins (reviewed in [<xref ref-type="bibr" rid="B21">21</xref>]). Other lectins do not contain these CRDs but have evolved equivalent carbohydrate-binding characteristics, including pentraxins and glycosaminoglycan-binding proteins. C-type and S-type lectins, as well as pentraxins, have been reported to display lectin-mediated anti-IAV activity <italic>in vitro</italic> and/or <italic>in vivo</italic> and will be discussed further in this review.</p><sec sec-type="subsection" id="sec2.1"><title>2.1. C-Type Lectins</title><p>C-type lectins are a family of animal proteins that display Ca<sup>2+</sup>-dependent (C-type) carbohydrate-binding activity and mediate a range of biological processes including endocytosis, cell-to-cell adhesion, turnover of serum glycoproteins, and pathogen recognition. The C-type lectin CRD contains conserved residue motifs that are characteristic of the domain and are responsible for Ca<sup>2+</sup>-dependent binding activity [<xref ref-type="bibr" rid="B20">20</xref>, <xref ref-type="bibr" rid="B22">22</xref>]. In general terms, C-type lectins bind either derivatives of mannose (Man-type ligands) or galactose (Gal-type ligands) [<xref ref-type="bibr" rid="B22">22</xref>, <xref ref-type="bibr" rid="B23">23</xref>] and may be further subdivided into endocytic lectins and collectins on the basis of structural similarities. Endocytic C-type lectins include type I (e.g., macrophage mannose receptor (MMR)) and type II (e.g., macrophage galactose-type lectin (MGL) and DC-specific ICAM-3 grabbing non-integrin (DC-SIGN)) transmembrane proteins and these have been implicated as attachment and entry receptors for IAV infection [<xref ref-type="bibr" rid="B24">24</xref>, <xref ref-type="bibr" rid="B25">25</xref>]. The collectins, so called because of their collagenous domains, are soluble C-type lectins that have been implicated as a major component of innate host defense against IAV infection (<xref ref-type="fig" rid="fig1">Figure 1</xref>). The mechanisms by which collectins mediate anti-IAV activity, their role in innate host defense, and their potential as therapeutic agents to ameliorate IAV-induced disease will be discussed further in this paper.</p></sec><sec sec-type="subsection" id="sec2.2"><title>2.2. S-Type Lectins</title><p>S-type lectins, also known as galectins, do not require divalent cations for ligand binding, display specificity for <italic>β</italic>-galactosyl-containing glycoconjugates, and mediate a diverse range of biological functions (<xref ref-type="fig" rid="fig1">Figure 1</xref>; reviewed in [<xref ref-type="bibr" rid="B26">26</xref>]). They are widely distributed among animal tissues and may be located both inside (in the cytoplasm and/or nucleus) and outside cells (on the cell surface and/or within extracellular spaces). To date, 15 galectins have been identified, all of which contain a conserved CRD (reviewed in [<xref ref-type="bibr" rid="B27">27</xref>]). Galectin-1, -3, -8, and -9 are found in human airways, the primary site of IAV infection. Recently, galectin-1 was implicated as an effector in innate host defense during IAV infection [<xref ref-type="bibr" rid="B28">28</xref>].</p></sec><sec sec-type="subsection" id="sec2.3"><title>2.3. Pentraxins</title><p>Like collectins, the pentraxins are a family of lectin-like proteins highly conserved during evolution and characterized by a multimeric (usually pentameric) structure. The classic short pentraxins, C-reactive protein (CRP) and serum amyloid P-component (SAP), are produced by the liver in response to inflammatory signals and are the main acute phase reactants in human and mouse, respectively [<xref ref-type="bibr" rid="B29">29</xref>]. Moreover, they share a structural organization that comprises 5 or 10 identical units arranged in a pentameric radial symmetry (<xref ref-type="fig" rid="fig1">Figure 1</xref>). PTX3, the prototype of the long pentraxins, shares similarities with short pentraxins but contains an unrelated N-terminal domain, is produced by different cell types, and binds to a different spectrum of ligands [<xref ref-type="bibr" rid="B30">30</xref>]. Pentraxins display lectin-like properties, including binding to carbohydrates and related structures in a Ca<sup>2+</sup>-dependent manner. SAP was originally isolated based on its ability to bind to the 4,6-cyclin pyruvate acetal group of <italic>β</italic>-D-galactose [<xref ref-type="bibr" rid="B31">31</xref>] and has also been implicated in lectin-mediated interactions with IAV [<xref ref-type="bibr" rid="B32">32</xref>, <xref ref-type="bibr" rid="B33">33</xref>].</p></sec></sec><sec id="sec3"><title>3. Collectins in Innate Host Defense against Influenza Virus Infection</title><p>Collectins are present in serum and mucosal secretions and recognize particular patterns of carbohydrates expressed on the surface of bacteria, fungi, protozoa, and viruses. To date, nine distinct collectins have been identified: surfactant protein (SP)-A, SP-D, mannose-binding lectin (MBL), collectin placenta 1 (CL-P1), collectin liver 1 (CL-L1), and collectin kidney 1 (CL-K1 or collectin-11) as well as the bovine-specific collectins CL-43, CL-46, and conglutinin. The basic structural unit of collectins is a trimer of 3 associated polypeptides. Each polypeptide consists of a short N-terminal domain, a triple helical collagen domain of variable length, a neck region, and a CRD (<xref ref-type="fig" rid="fig1">Figure 1</xref>). The neck region induces polypeptide trimerization, which is further stabilized by the collagen domain. Trimers can associate to form higher-order multimeric complexes through disulfide-stabilized interactions at the N-terminus, thereby increasing binding avidity for microbes and other ligands [<xref ref-type="bibr" rid="B34">34</xref>]. MBL and SP-A are commonly composed of six associated trimers (octadecamers or 18-mers), which resemble a bouquet of flowers. In contrast, SP-D, conglutinin, and CL-46 are assembled into dodecamers (12-mers) of four or more trimeric subunits and form a cruciform-like structure. With the exception of CL-P1, all collectins described to date show ligand-binding preference for Man-type sugars over Gal-type sugars [<xref ref-type="bibr" rid="B23">23</xref>] (see <xref ref-type="table" rid="tab1">Table 1</xref>). Several reviews provide detailed description of the structural and functional features of the collectins [<xref ref-type="bibr" rid="B23">23</xref>, <xref ref-type="bibr" rid="B34">34</xref>–<xref ref-type="bibr" rid="B36">36</xref>]. In the current paper, we will focus on the relevance of collectins to immunity during IAV infection.</p><p>Nonspecific inhibitors of IAV, first described in the 1940s, have been classified as <italic>α</italic>, <italic>β</italic>, or <italic>γ</italic> inhibitors based on their chemical composition and properties (reviewed in [<xref ref-type="bibr" rid="B37">37</xref>]). The first evidence of the anti-IAV activities of collectins was provided by Anders et al. who demonstrated that <italic>β</italic> inhibitors in bovine and mouse serum were Ca<sup>2+</sup>-dependent mannose-binding lectins that bound to glycans on the globular head of IAV HA, thereby blocking the ability of the HA to bind to sialylated cell-surface receptors [<xref ref-type="bibr" rid="B38">38</xref>]. Subsequent studies identified conglutinin and MBL as the major <italic>β</italic> inhibitors in bovine and mouse serum, respectively [<xref ref-type="bibr" rid="B39">39</xref>]. In contrast to the lectin-mediated actions of <italic>β</italic> inhibitors, <italic>γ</italic> inhibitors are sialylated glycoproteins that act independently of Ca<sup>2+</sup> by competing with sialylated cell-surface receptors for binding to HA [<xref ref-type="bibr" rid="B40">40</xref>, <xref ref-type="bibr" rid="B41">41</xref>]. Today, collectins are known to mediate a range of anti-IAV activities including (but not limited to) inhibition of IAV HA and NA, neutralization of virus infectivity, virus aggregation, increased IAV uptake by neutrophils, and opsonization of virus to enhance neutrophil respiratory burst responses to IAV (see <xref ref-type="table" rid="tab2">Table 2</xref>). As discussed in this review, there is growing evidence defining the role of particular collectins in anti-IAV immunity and researchers are now exploring their potential as therapeutic agents for the treatment of IAV-associated disease.</p><sec sec-type="subsection" id="sec3.1"><title>3.1. SP-D</title><p>SP-D and SP-A are constitutively present in lung fluids of the respiratory tract, the major site of IAV infection. SP-D acts as a classical <italic>β</italic> inhibitor and its CRDs bind to mannose-rich glycans expressed on IAV HA and NA [<xref ref-type="bibr" rid="B42">42</xref>–<xref ref-type="bibr" rid="B44">44</xref>]. In contrast, SP-A inhibits IAV in a Ca<sup>2+</sup>-independent manner by binding of viral HA to a sialylated glycan expressed within the SP-A CRD, thereby blocking the ability of HA to interact with cellular receptors [<xref ref-type="bibr" rid="B45">45</xref>]. Findings that (i) removal of the SP-A glycan completely abrogated anti-IAV activity and (ii) SP-A was effective against the poorly glycosylated A/PR/8/34 (PR8, H1N1) strain of IAV [<xref ref-type="bibr" rid="B46">46</xref>] are consistent with SP-A acting as a <italic>γ</italic> inhibitor rather than a <italic>β</italic>-type lectin inhibitor. Thus, SP-A and SP-D bind to similar regions on the HA molecule but do so via distinct mechanisms. For the purposes of this paper we will focus on lectin-mediated recognition of IAV by SP-D.</p><p>Human influenza is primarily an infection of the upper respiratory tract but can spread to the lower airways resulting in viral pneumonia and/or predispose to secondary bacterial infection. SP-D, present in nasal washings and bronchoalveolar fluids (BALF) from naïve mice, is upregulated following IAV infection and appears to be the major IAV inhibitor in the airways of mice [<xref ref-type="bibr" rid="B44">44</xref>, <xref ref-type="bibr" rid="B47">47</xref>–<xref ref-type="bibr" rid="B50">50</xref>]. Moreover, SP-D has been shown to contribute to anti-IAV activity in BAL from healthy human volunteers [<xref ref-type="bibr" rid="B42">42</xref>, <xref ref-type="bibr" rid="B51">51</xref>] and to enhance aggregation and neutrophil uptake of pathogens commonly associated with secondary bacterial pneumonia such as <italic>Streptococcus pneumoniae</italic> and <italic>Staphlococcus aureus</italic> [<xref ref-type="bibr" rid="B52">52</xref>].</p><p>SP-D preparations from different species show varying proportions of dodecamers (four homotrimeric subunits), multimers of dodecamers, and/or single trimeric subunits [<xref ref-type="bibr" rid="B53">53</xref>, <xref ref-type="bibr" rid="B54">54</xref>]. The degree of oligomerization is an important factor modulating anti-IAV activity and dodecamers and multimers exhibit greater antiviral activities than trimers [<xref ref-type="bibr" rid="B55">55</xref>–<xref ref-type="bibr" rid="B57">57</xref>]. In general terms, SP-D binds to Man-type oligosaccharides (see <xref ref-type="table" rid="tab1">Table 1</xref>) although the CRD from human, mouse, and rat SP-D showed distinct preferences for particular saccharide ligands [<xref ref-type="bibr" rid="B54">54</xref>]. SP-D binds to glycans on the IAV envelope glycoproteins to mediate hemagglutination inhibition (HI), inhibition of NA activity, virus aggregation, and neutralization of virus infectivity [<xref ref-type="bibr" rid="B42">42</xref>, <xref ref-type="bibr" rid="B44">44</xref>, <xref ref-type="bibr" rid="B58">58</xref>–<xref ref-type="bibr" rid="B60">60</xref>] (<xref ref-type="table" rid="tab2">Table 2</xref>). Binding of SP-D also promotes uptake of IAV by neutrophils and protects neutrophils against IAV-induced neutrophil dysfunction [<xref ref-type="bibr" rid="B42">42</xref>, <xref ref-type="bibr" rid="B61">61</xref>]. However, neutrophil proteases can cleave SP-D and chronic neutrophilic inflammation in the airways may result in degradation of SP-D and account for the increased risk of IAV infection associated with heavy smoking or cystic fibrosis [<xref ref-type="bibr" rid="B62">62</xref>, <xref ref-type="bibr" rid="B63">63</xref>]. There are several polymorphisms in the coding sequence of human SP-D, including one at the codon corresponding to amino acid residue 11 (Met<sup>11</sup>Thr). Moreover, the Thr/Thr11 variant assembles as trimers rather than higher-order multimeric species [<xref ref-type="bibr" rid="B64">64</xref>] and these display reduced anti-IAV activity <italic>in vitro </italic>[<xref ref-type="bibr" rid="B56">56</xref>, <xref ref-type="bibr" rid="B64">64</xref>].</p><p>SP-D binds directly to oligosaccharides expressed on either IAV HA or NA [<xref ref-type="bibr" rid="B44">44</xref>, <xref ref-type="bibr" rid="B59">59</xref>], yet the susceptibility of different IAV strains to SP-D correlates with the degree of glycosylation of HA. Seasonal “drift” strains of H3N2 IAV with increased glycosylation on the globular head of HA were more susceptible to neutralization by SP-D and showed reduced virulence in mice [<xref ref-type="bibr" rid="B44">44</xref>]. Furthermore, Hartshorn et al. used hemagglutination inhibition (HI) assays to implicate specific sites on the HA of H3N2 and H1N1 subtype IAV as targets for recognition by recombinant human (Rh) SP-D [<xref ref-type="bibr" rid="B58">58</xref>]. Recently, site-directed mutagenesis and reverse genetics were utilized to define the contribution of specific glycans on H3N2 [<xref ref-type="bibr" rid="B50">50</xref>, <xref ref-type="bibr" rid="B65">65</xref>] and H1N1 [<xref ref-type="bibr" rid="B66">66</xref>] IAV in determining sensitivity to SP-D and to virulence in mice. Collectively, these studies indicated that both the number and the position of potential glycosylation sites on the globular head of the HA modulate the avidity of SP-D binding and therefore the potency of antiviral activity against different IAV.</p><p>SP-D-deficient mice (SP-D<sup>−/−</sup>) display aberrant pulmonary surfactant homeostasis, including progressive pulmonary inflammation, emphysema, macrophage activation, and surfactant phospholipid accumulation [<xref ref-type="bibr" rid="B67">67</xref>–<xref ref-type="bibr" rid="B69">69</xref>] and correction of alveolar homeostasis required the collagenous domain of SP-D [<xref ref-type="bibr" rid="B70">70</xref>, <xref ref-type="bibr" rid="B71">71</xref>]. Following infection with highly glycosylated IAV, SP-D<sup>−/−</sup> mice show increased virus replication, airway inflammation, and disease [<xref ref-type="bibr" rid="B47">47</xref>, <xref ref-type="bibr" rid="B48">48</xref>, <xref ref-type="bibr" rid="B50">50</xref>] (summarized in <xref ref-type="table" rid="tab3">Table 3</xref>) and these effects could be corrected by overexpression of wild type or mutant SP-D proteins in the airways [<xref ref-type="bibr" rid="B70">70</xref>]. Mannan, a complex polymer of mannose residues, efficiently blocks the anti-IAV activities of SP-D <italic>in vitro</italic> and intranasal treatment of wild-type mice with mannan prior to and during infection with a highly glycosylated H3N2 IAV strain resulted in enhanced viral replication, pulmonary inflammation, and death [<xref ref-type="bibr" rid="B49">49</xref>]. Studies in a mouse model have also suggested that compromise of SP-D-mediated defenses by elevated glucose levels might be an important factor contributing to the increased disease severity of IAV-induced disease in diabetic mice [<xref ref-type="bibr" rid="B72">72</xref>].</p></sec><sec sec-type="subsection" id="sec3.2"><title>3.2. MBL</title><p> MBL binds to oligosaccharides with characteristic chemical and spatial features that are expressed on the surface of a wide range of pathogens, including bacteria, fungi, and viruses (reviewed in [<xref ref-type="bibr" rid="B73">73</xref>]). In general terms, MBL recognizes Man-type sugars and Haurum et al. reported that MBL binding to mannan was inhibited by monosaccharides such as GlcNAc, mannose, L-fucose, and <italic>N</italic>-acetyl-mannosamine but not by galactose or GalNAc [<xref ref-type="bibr" rid="B74">74</xref>] (<xref ref-type="table" rid="tab1">Table 1</xref>). Following binding to pathogens, MBL can activate the lectin complement pathway via MBL-associated serine proteases (MASPs), resulting in complement-mediated lysis and/or opsonophagocytosis [<xref ref-type="bibr" rid="B75">75</xref>, <xref ref-type="bibr" rid="B76">76</xref>]. Binding of MBL-MASP complexes to appropriate ligands also activates coagulation via thrombin-like activity [<xref ref-type="bibr" rid="B77">77</xref>, <xref ref-type="bibr" rid="B78">78</xref>]. MBL is unique among the collectins in its ability to activate complement and coagulation. </p><p>Although humans express a single MBL gene, two homologous forms of MBL, termed MBL-A and MBL-C, have been identified in rodents [<xref ref-type="bibr" rid="B79">79</xref>, <xref ref-type="bibr" rid="B80">80</xref>]. These two forms of rodent MBL are 50% homologous, display distinct but overlapping ligand-binding specificity, and bind to MASPs to activate complement [<xref ref-type="bibr" rid="B81">81</xref>]. Multiple structural and promoter polymorphisms in the human <italic>MBL2</italic> gene can result in low levels and/or dysfunctional MBL. Moreover, MBL deficiency has been associated with predisposition to numerous infectious diseases, including respiratory infections (reviewed in [<xref ref-type="bibr" rid="B82">82</xref>]).</p><p>SP-A and SP-D are constitutively expressed in the lungs whereas MBL is predominantly a serum protein. MBL is rarely detected in BALF from healthy humans or mice, although significant levels have been detected during airway inflammation [<xref ref-type="bibr" rid="B83">83</xref>], including that associated with IAV infection of mice [<xref ref-type="bibr" rid="B44">44</xref>]. Recently, affinity purification and western blot confirmed the presence of MBL in BALF from healthy mice, albeit at levels that were below detection by ELISA [<xref ref-type="bibr" rid="B84">84</xref>].</p><p>MBL has been reported to mediate a range of anti-IAV activities <italic>in vitro</italic>, including inhibition of virus-induced hemagglutination [<xref ref-type="bibr" rid="B85">85</xref>, <xref ref-type="bibr" rid="B86">86</xref>], blocking of NA enzymatic activity [<xref ref-type="bibr" rid="B60">60</xref>, <xref ref-type="bibr" rid="B87">87</xref>], opsonization for enhanced neutrophil reactivity to IAV [<xref ref-type="bibr" rid="B85">85</xref>, <xref ref-type="bibr" rid="B86">86</xref>], and neutralization of virus infectivity [<xref ref-type="bibr" rid="B84">84</xref>, <xref ref-type="bibr" rid="B86">86</xref>–<xref ref-type="bibr" rid="B88">88</xref>] (<xref ref-type="table" rid="tab2">Table 2</xref>). These activities are complement-independent and shared by other mammalian collectins such as SP-D and conglutinin. In addition, MBL-mediated activation of complement can induce irreversible inactivation of IAV [<xref ref-type="bibr" rid="B89">89</xref>] and promote lysis of IAV-infected cells [<xref ref-type="bibr" rid="B90">90</xref>]. Chang et al. recently reported that recombinant human MBL (RhMBL) and murine MBL-A/-C could neutralize IAV infectivity but that preferential activation of the lectin complement pathway and thrombin-like activity by MBL-A and MBL-C, respectively, was associated with enhanced MBL-mediated neutralization [<xref ref-type="bibr" rid="B84">84</xref>].</p><p>Lectin blot analysis indicates that MBL can bind to both HA and NA glycoproteins [<xref ref-type="bibr" rid="B44">44</xref>, <xref ref-type="bibr" rid="B88">88</xref>, <xref ref-type="bibr" rid="B91">91</xref>], yet as for SP-D, the degree of glycosylation on the head of IAV HA is the critical factor determining sensitivity to MBL. Seasonal H1N1 IAVs expressing 3-4 potential glycosylation sites on the head of HA were more sensitive to neutralization by RhMBL compared to poorly glycosylated strains such as PR8 (H1N1) or A/California/04/09 (Cal/09, A(H1N1) 2009 pdm) [<xref ref-type="bibr" rid="B87">87</xref>]. Similarly, H3N2 IAVs carrying 4-5 potential glycosylation sites on the head of HA were highly sensitive to MBL in mouse serum [<xref ref-type="bibr" rid="B44">44</xref>]. Current evidence suggests that inhibition of NA activity also results from steric hindrance of the active site of NA by SP-D/MBL bound to mannose-rich glycans on the viral HA [<xref ref-type="bibr" rid="B44">44</xref>, <xref ref-type="bibr" rid="B60">60</xref>, <xref ref-type="bibr" rid="B87">87</xref>].</p><p>The role of MBL <italic>in vivo</italic> during IAV infections remains controversial. Chang et al. reported MBL-deficient mice to be more susceptible to A/Philippines/82 (Phil/82, H3N2), a highly glycosylated IAV strain that is readily neutralized by MBL [<xref ref-type="bibr" rid="B84">84</xref>] (<xref ref-type="table" rid="tab3">Table 3</xref>). MBL showed some binding to A(H1N1) 2009 pdm, yet these viruses were resistant to MBL-mediated neutralization [<xref ref-type="bibr" rid="B87">87</xref>, <xref ref-type="bibr" rid="B92">92</xref>] and MBL-null mice infected with A(H1N1) 2009 pdm (or H9N2/G1) IAV showed reduced disease severity and airway inflammation [<xref ref-type="bibr" rid="B93">93</xref>] (<xref ref-type="table" rid="tab3">Table 3</xref>), arguing that MBL may be a risk factor during certain IAV infections. Thus, high avidity interaction between MBL and IAV may result in protective antiviral responses whereas low avidity binding may be insufficient to mediate anti-IAV function, resulting in detrimental MBL-induced pro-inflammatory responses and severe disease.</p></sec><sec sec-type="subsection" id="sec3.3"><title>3.3. Other Collectins</title><p>In addition to “classical collectins” such as SP-D and MBL, much less is known regarding the general structure and function of “novel collectins” such as CL-L1, CL-P1, and CL-K1 (collectin 11) and there are limited data regarding their role in anti-IAV immunity. CL-L1, predominantly produced by the liver, is a cytosolic protein with weak lectin function [<xref ref-type="bibr" rid="B94">94</xref>] suggesting a different biological function to that of the classical collectins. CL-P1, a membrane-associated collectin, is expressed on vascular endothelial cells and recognizes oxidized low-density lipoprotein as well as bacteria and yeasts [<xref ref-type="bibr" rid="B95">95</xref>]. To date, no interactions between IAV and CL-L1 or CL-P1 have been reported. Collectin 11, a MASP-associated plasma lectin, was recently shown to inhibit IAV-induced hemagglutination and to neutralize virus infectivity [<xref ref-type="bibr" rid="B96">96</xref>]. Moreover, collectin 11 is expressed in airway bronchioles [<xref ref-type="bibr" rid="B97">97</xref>] and as a circulating plasma protein [<xref ref-type="bibr" rid="B96">96</xref>, <xref ref-type="bibr" rid="B98">98</xref>] and may therefore represent an innate barrier to IAV infection and/or transude from the plasma to inflamed airways in a manner analogous to that reported for MBL [<xref ref-type="bibr" rid="B44">44</xref>, <xref ref-type="bibr" rid="B83">83</xref>].</p></sec><sec sec-type="subsection" id="sec3.4"><title>3.4. Bovine, Porcine, and Avian Collectins</title><sec sec-type="subsubsection" id="sec3.4.1"><title>3.4.1. Bovine Collectins</title><p> Conglutinin was the first described lectin of animal origin and was originally discovered by its ability to agglutinate (conglutinate) erythrocytes coated with antibody and complement [<xref ref-type="bibr" rid="B99">99</xref>]. It is distinct from other collectins as it binds iC3b, a component of the complement pathway [<xref ref-type="bibr" rid="B100">100</xref>, <xref ref-type="bibr" rid="B101">101</xref>]. While most collectins have been identified in multiple species, conglutinin, CL-43, and CL-46 appear to be restricted to the species <italic>Bovidae</italic> and characterization of their respective genes indicates that they are descendants of an ancestral SP-D gene [<xref ref-type="bibr" rid="B102">102</xref>]. Conglutinin and CL-46 form dodecameric structures similar to those of SP-D whereas CL-43 occurs naturally as trimers [<xref ref-type="bibr" rid="B102">102</xref>–<xref ref-type="bibr" rid="B104">104</xref>]. The evolutionary pressures that have resulted in the presence of additional collectins in <italic>Bovidae </italic>are not known. Hartshorn et al. proposed that the combined anti-IAV activities of conglutinin, CL-43, and CL-46 might explain why cattle do not represent a natural reservoir for IAV infection, despite living in close proximity to other natural hosts of IAV, such as birds, pigs, horses, and humans [<xref ref-type="bibr" rid="B103">103</xref>].</p><p>Conglutinin acts as a <italic>β</italic> inhibitor of IAV, binding to oligosaccharides on the tip of the HA spike in a Ca<sup>2+</sup>-dependent manner [<xref ref-type="bibr" rid="B39">39</xref>, <xref ref-type="bibr" rid="B105">105</xref>] to inhibit virus-induced hemagglutination, aggregation, and neutralization of virus infectivity [<xref ref-type="bibr" rid="B39">39</xref>, <xref ref-type="bibr" rid="B105">105</xref>–<xref ref-type="bibr" rid="B109">109</xref>] (<xref ref-type="table" rid="tab2">Table 2</xref>). Opsonization with conglutinin also enhanced neutrophil respiratory burst responses after exposure to IAV [<xref ref-type="bibr" rid="B107">107</xref>]. Lectin blot studies have demonstrated that MBL and SP-D bind to both HA and NA, yet conglutinin binds only to HA [<xref ref-type="bibr" rid="B88">88</xref>, <xref ref-type="bibr" rid="B106">106</xref>, <xref ref-type="bibr" rid="B110">110</xref>, <xref ref-type="bibr" rid="B111">111</xref>], and this has been proposed as one factor contributing to its relatively poor ability to inhibit viral spreading to adjacent cells [<xref ref-type="bibr" rid="B108">108</xref>]. Of the different IAV strains and subtypes tested, most H1N1 and H3N2 subtypes were susceptible to conglutinin with the exception of the poorly glycosylated PR8 (H1N1) strain [<xref ref-type="bibr" rid="B39">39</xref>, <xref ref-type="bibr" rid="B105">105</xref>, <xref ref-type="bibr" rid="B107">107</xref>]. Mutants of H3N2 or H1N1 IAV lacking a single glycosylation site from the tip of the HA spike (Asn<sub>165</sub>-H3 numbering or Asn<sub>104</sub>-H1 numbering, respectively) were also markedly resistant to conglutinin [<xref ref-type="bibr" rid="B38">38</xref>, <xref ref-type="bibr" rid="B39">39</xref>].</p><p>CL-43, like conglutinin, is a potent inhibitor of IAV; however this lectin exhibits distinct monosaccharide binding properties [<xref ref-type="bibr" rid="B112">112</xref>] (see <xref ref-type="table" rid="tab1">Table 1</xref>) and forms trimers but not other high-order multimers [<xref ref-type="bibr" rid="B113">113</xref>]. The potency of various SP-D preparations in mediating HI and virus neutralization has been strongly associated with its degree of multimerization [<xref ref-type="bibr" rid="B85">85</xref>, <xref ref-type="bibr" rid="B114">114</xref>], yet trimers of CL-43 mediated HI and neutralizing activity against IAV to levels equivalent to those of fully multimerized SP-D and were markedly more potent than trimeric SP-D preparations [<xref ref-type="bibr" rid="B103">103</xref>]. Collectin-induced aggregation of IAV has also been strongly associated with the ability of SP-D, MBL, or conglutinin preparations to enhance neutrophil respiratory burst responses and to increase neutrophil uptake of IAV [<xref ref-type="bibr" rid="B61">61</xref>, <xref ref-type="bibr" rid="B85">85</xref>]. CL-43 did not induce viral aggregation and did not enhance IAV-induced generation of H<sub>2</sub>O<sub>2</sub>; however neutrophil uptake of IAV was increased [<xref ref-type="bibr" rid="B103">103</xref>] (<xref ref-type="table" rid="tab2">Table 2</xref>), most likely via mechanisms distinct to those of other collectins. Recently, trimers composed of the neck and CRD (NCRD) of CL-46 were also shown to neutralize IAV infectivity, inhibit virus-induced hemagglutination, induce aggregation of IAV, and to increase neutrophil uptake of IAV [<xref ref-type="bibr" rid="B115">115</xref>, <xref ref-type="bibr" rid="B116">116</xref>].</p></sec><sec sec-type="subsubsection" id="sec3.4.2"><title>3.4.2. Porcine SP-D</title><p> Porcine (p)SP-D is unique amongst the mammalian SP-Ds described to date in that it contains a sialic acid-rich <italic>N</italic>-glycan in its CRD [<xref ref-type="bibr" rid="B117">117</xref>, <xref ref-type="bibr" rid="B118">118</xref>]. Human and porcine SP-A also express sialylated N-glycans in their respective CRDs and mediate Ca<sup>2+</sup>-independent anti-IAV activity that was abrogated by the removal of this glycan [<xref ref-type="bibr" rid="B45">45</xref>, <xref ref-type="bibr" rid="B118">118</xref>]. In contrast, pSP-D displayed dual mechanisms of anti-IAV activity by mediating (i) Ca<sup>2+</sup>-dependent binding of the pSP-D CRD to oligosaccharides of IAV HA, and (ii) binding of IAV HA to sialic acid expressed by pSP-D. Initial binding of pSP-D to mannose-rich glycans on HA appears to be critical and secondary interactions between IAV HA and sialylated glycans on pSP-D do not take place in the absence of lectin-mediated binding [<xref ref-type="bibr" rid="B117">117</xref>, <xref ref-type="bibr" rid="B118">118</xref>]. The sialylated glycan expressed on pSP-D was shown to enhance virus aggregation and neutralization as well as neutrophil responses to IAV [<xref ref-type="bibr" rid="B118">118</xref>]. Accordingly, pSP-D isolated from porcine BAL and recombinant pSP-D displayed more potent anti-IAV activity compared to human or rat SP-D and were active against a broader spectrum of IAV strains [<xref ref-type="bibr" rid="B118">118</xref>, <xref ref-type="bibr" rid="B119">119</xref>]. Together these data suggest that pulmonary innate defenses may be particularly efficient against IAV in pigs and represent an important barrier limiting disease severity. IAV strains show limited antigenic variation in swine compared to humans [<xref ref-type="bibr" rid="B120">120</xref>], and this may reflect the shorter lifespan of farmed animals. Moreover, restriction of IAV infection by porcine innate defenses might also limit the induction of antibody-mediated adaptive immune responses in pigs that are required to drive antigenic drift.</p></sec><sec sec-type="subsubsection" id="sec3.4.3"><title>3.4.3. Chicken Collectins</title><p> Avian species, including domestic poultry, represent an important natural reservoir for IAV infection. Ducks, chickens, and turkeys may all be farmed in close proximity to humans and other IAV reservoirs including pigs and horses, thereby increasing the potential for interspecies transmission. It is well established that mammalian collectins mediate anti-IAV activity. In chickens, 5 collectins have been described to date, namely, MBL [<xref ref-type="bibr" rid="B121">121</xref>], SP-A (cSP-A), and chicken collectins 1, 2, and 3 (cCL-1, -2 and -3) which resemble the mammalian proteins CL-L1, collectin 11, and CL-P1, respectively [<xref ref-type="bibr" rid="B122">122</xref>]. In addition, chicken lung lectin (cLL) was identified as a C-type lectin but not as a collectin due to its lack of a collagenous domain [<xref ref-type="bibr" rid="B122">122</xref>]. Phylogenetic analyses suggest that the homologue of mammalian SP-D has been deleted in chickens and that a bird-specific duplication of the SP-A gene may have given rise to cLL [<xref ref-type="bibr" rid="B123">123</xref>]. cLL inhibited the hemagglutination activity of Phil/82 (H3N2; highly glycosylated HA) and PR8 (H1N1; poorly glycosylated HA) to similar levels but did not neutralize either virus strain [<xref ref-type="bibr" rid="B124">124</xref>]. At present the mechanisms underlying cLL-IAV interactions are not fully understood and further studies are required to determine the role of avian collectins in anti-IAV immunity.</p></sec></sec></sec><sec id="sec4"><title>4. Other Mammalian Lectins with Anti-Influenza Activity</title><p>Galectins are S-type animal lectins characterized by a conserved CRD that recognizes galactose-containing oligosaccharides. Recently, lectin-mediated binding of galectin-1 to IAV was shown to inhibit IAV-induced hemagglutination and to reduce virus production in MDCK cells [<xref ref-type="bibr" rid="B28">28</xref>]. Galectin-1 bound to a range of IAV subtypes (H1N1, H2N2, H3N2, H5N2, and H6N1) with micromolar <italic>K</italic><sub><italic>d</italic></sub> values suggesting broad antiviral activity and binding was inhibited by lactose, but not by mannose (<xref ref-type="table" rid="tab1">Table 1</xref>). Importantly, galectin-1 was upregulated in the lungs of IAV-infected mice and mice lacking endogenous galectin-1 showed reduced survival compared to wild-type mice [<xref ref-type="bibr" rid="B28">28</xref>]. Together, these data are the first to demonstrate the importance of galectins in anti-IAV immunity.</p><p>The short pentraxin SAP has been reported to act as a <italic>β</italic> inhibitor against IAV, binding in a Ca<sup>2+</sup>-dependent manner to glycans on the viral HA to mediate HI and neutralize virus infectivity [<xref ref-type="bibr" rid="B32">32</xref>, <xref ref-type="bibr" rid="B33">33</xref>] (<xref ref-type="table" rid="tab2">Table 2</xref>).<italic> In vitro</italic>, human SAP inhibited a range of type A (H1N1, H2N2, and H3N2) and type B viruses and antiviral activity was blocked by the inclusion of mannose, consistent with recognition of Man-type glycans on the IAV. PTX3 also mediates anti-IAV activity; however this appears to be mediated by binding of the IAV HA to SA residues expressed on PTX3 [<xref ref-type="bibr" rid="B125">125</xref>] in a manner analogous to that described for SP-A. As lectin-mediated recognition of IAV by PTX3 does not appear to contribute to its anti-IAV activity, it will not be discussed further in this paper.</p></sec><sec id="sec5"><title>5. Pandemic IAV and Lectin-Mediated Defenses</title><p>When pandemic IAVs first emerge, they generally carry little glycosylation on the head of HA but acquire additional glycosylation sites as they continue to circulate in the human population. In 1968, H3N2 IAV associated with “Hong Kong flu” carried 2 potential glycosylation sites on the HA head whereas recent H3N2 viruses carry 6 to 7 sites [<xref ref-type="bibr" rid="B50">50</xref>, <xref ref-type="bibr" rid="B58">58</xref>]. Pandemic H1N1 strains associated with the 1918 “Spanish flu” had only 1 potential glycosylation site (Asn<sub>104</sub>) on the globular head of HA but by the 1950s had acquired a total of 4 to 5 sites [<xref ref-type="bibr" rid="B17">17</xref>, <xref ref-type="bibr" rid="B18">18</xref>, <xref ref-type="bibr" rid="B126">126</xref>]. Asn<sub>104</sub> was also the only site expressed on the head of HA of A(H1N1) 2009 pdm viruses associated with the 2009 “Swine flu” pandemic [<xref ref-type="bibr" rid="B17">17</xref>, <xref ref-type="bibr" rid="B87">87</xref>, <xref ref-type="bibr" rid="B126">126</xref>] and few variants with altered HA glycosylation have been detected to date [<xref ref-type="bibr" rid="B18">18</xref>]. In the future it is likely that A(H1N1) pdm viruses will develop resistance to the current vaccine, perhaps through the evolution of mutants with altered HA glycosylation patterns that favour resistance to preexisting neutralizing antibodies.</p><p>The degree of glycosylation on the globular head of HA is a critical factor in determining sensitivity of different IAV strains to the antiviral activities of collectins. Consequently, pandemic IAVs tend to be resistant to collectins when compared to seasonal IAV strains. For example, human SP-D and MBL inhibited IAV-induced hemagglutinating activity, blocked the enzymatic activity of NA, and neutralized the infectivity of seasonal H1N1, but not pandemic A(H1N1) 2009 pdm IAV [<xref ref-type="bibr" rid="B87">87</xref>]. Chimeric viruses expressing the HA of 1918 (H1), 1957 (H2), 1968 (H3), and 2009 (H1) pandemic IAV in the context of a seasonal H1N1 IAV were poorly recognized by RhSP-D <italic>in vitro </italic>and were associated with enhanced lower respiratory tract pathology in IAV-infected mice [<xref ref-type="bibr" rid="B127">127</xref>], consistent with the notion that sensitivity to SP-D might limit the ability of IAV to invade the lower airways and induce severe disease. In the mouse model, weak interactions between MBL and A(H1N1) 2009 pdm viruses have also been implicated in the induction of MBL-induced proinflammatory responses, suggesting that MBL might be a risk factor associated with severe disease during pandemic IAV infections [<xref ref-type="bibr" rid="B93">93</xref>]. However, no association was observed between phenotypic MBL deficiency and predisposition to A(H1N1) 2009 pdm in exposed health care workers [<xref ref-type="bibr" rid="B128">128</xref>].</p><p>Highly pathogenic avian influenza (HPAI) H5N1 IAV infections have been associated with very severe disease and fatality in humans and are still considered to be a potentially serious pandemic threat [<xref ref-type="bibr" rid="B129">129</xref>]. Microarray analysis and quantitative RT-PCR showed SP-D expression to be reduced in lungs from two fatal cases of H5N1 IAV infection when compared to healthy patients or patients with acute respiratory distress syndrome [<xref ref-type="bibr" rid="B130">130</xref>], although other studies noted no major changes in SP-D expression in the airways of H5N1-infected ferrets [<xref ref-type="bibr" rid="B131">131</xref>] or macaques [<xref ref-type="bibr" rid="B132">132</xref>]. In addition, 2 human H5N1 strains that were less glycosylated than recent seasonal H1N1 and H3N2 strains were also resistant to SP-D<italic> in vitro</italic> [<xref ref-type="bibr" rid="B58">58</xref>], consistent with the notion that SP-D-mediated defenses may be ineffective against H5N1 strains. Future studies will determine the susceptibility of a range of different avian IAV to SP-D as well as the potential of animal lectins as prophylactic and/or therapeutic treatments during severe H5N1-induced disease. As noted previously, lectins are expressed in the respiratory and digestive systems of chickens. As these are the major sites of IAV replication and dissemination, understanding their role in avian host defense is particularly important as they may act to control disease and limit viral transmission.</p></sec><sec id="sec6"><title>6. Therapeutic Potential of Recombinant Animal Lectins during IAV Infection</title><p>Understanding mechanisms by which mammalian lectins mediate antiviral activity against IAV is an important first step towards development of novel lectin-based therapeutic and prophylactic agents. Treatment of lectin-deficient mice with purified recombinant lectins can reverse the enhanced susceptibility associated with IAV infection. For example, intraperitoneal injection of RhMBL or intratracheal administration of RhSP-D reduced titres of Phil/82 in the lungs of MBL null mice [<xref ref-type="bibr" rid="B84">84</xref>] or SP-D null mice [<xref ref-type="bibr" rid="B48">48</xref>], respectively, to levels equivalent to those of wild-type animals. Yang et al. demonstrated that intranasal treatment of IAV-infected C57BL/6 mice with recombinant galectin-1 enhanced survival, reduced viral load, and attenuated lung inflammation and injury [<xref ref-type="bibr" rid="B28">28</xref>]. In addition, intranasal treatment of BALB/c mice with human SAP 1 hr prior to infection with A/Japan/57 (Jap/57, H2N2) reduced disease severity [<xref ref-type="bibr" rid="B33">33</xref>] although Herbert et al. reported that intraperitoneal injection of C57BL/6 mice with human SAP had no effect on disease outcome [<xref ref-type="bibr" rid="B133">133</xref>]. The particular route of lectin administration will be one factor modulating the effectiveness of exogenous animal lectins in ameliorating IAV-associated disease. Moreover, IAV strains show major differences in susceptibility to animal lectins [<xref ref-type="bibr" rid="B44">44</xref>, <xref ref-type="bibr" rid="B50">50</xref>, <xref ref-type="bibr" rid="B58">58</xref>], highlighting the importance of assessing therapeutic and/or prophylactic potential against a range of seasonal and pandemic IAV strains.</p><sec sec-type="subsection" id="sec6.1"><title>6.1. Recombinant Chimeric Lectins (RCLs)</title><p>RCLs represent a tailored approach exploiting particular anti-IAV properties of different pattern recognition molecules. For example, chimeric lectins comprising the collagenous domain of SP-D in conjunction with the neck and CRD of MBL displayed more potent anti-IAV activities compared to either SP-D or MBL alone [<xref ref-type="bibr" rid="B114">114</xref>, <xref ref-type="bibr" rid="B134">134</xref>]. Similarly, expression of the conglutinin neck and CRD domains in conjunction with the collagenous domain of SP-D resulted in increased anti-IAV activity [<xref ref-type="bibr" rid="B43">43</xref>]. An RCL bearing the CRD of MBL and the collagenous domains of L-ficolin (an additional innate pattern recognition receptor) showed enhanced activation of the lectin complement pathway and anti-IAV activity as well as reduced thrombin-like and FXa-like coagulation enzyme activities compared to RhMBL alone [<xref ref-type="bibr" rid="B135">135</xref>], representing further refinement towards potent therapeutics against IAV which might display reduced side effects in a clinical setting.</p></sec><sec sec-type="subsection" id="sec6.2"><title>6.2. Recombinant Truncated Lectins</title><p>Recombinant truncated NCRD trimers of SP-D represent an appealing therapeutic option as they can be produced in large quantities and lack the collagen domain associated with potential pro-inflammatory effects of SP-D [<xref ref-type="bibr" rid="B136">136</xref>]. However, NCRDs of human or rodent SP-D bound effectively to various SP-D ligands but displayed only weak inhibitory activity against IAV <italic>in vitro</italic> [<xref ref-type="bibr" rid="B54">54</xref>–<xref ref-type="bibr" rid="B56">56</xref>, <xref ref-type="bibr" rid="B137">137</xref>]. Subsequent studies demonstrated that cross-linking of NCRDs and/or mutagenesis of specific CRD residues represent complimentary strategies that enhanced anti-IAV activity of SP-D NCRDs [<xref ref-type="bibr" rid="B138">138</xref>, <xref ref-type="bibr" rid="B139">139</xref>]. The lectin domains of serum collectin NCRDs (e.g., MBL, conglutinin, CL-43, or CL-46) show intrinsically greater anti-IAV activity compared to the NCRDs of SP-D [<xref ref-type="bibr" rid="B43">43</xref>, <xref ref-type="bibr" rid="B103">103</xref>, <xref ref-type="bibr" rid="B134">134</xref>]. For example, CL-43 NCRDs were more potent than SP-D NCRDs and CL-43 showed a distinctive three amino acid insertion (RAK) in the flanking region of the carbohydrate binding site that was absent in SP-D. Insertion of 3 amino acids (RAK or AAA) into the SP-D NCRD enhanced anti-IAV activity relative to the wild-type SP-D NCRD [<xref ref-type="bibr" rid="B115">115</xref>, <xref ref-type="bibr" rid="B137">137</xref>].</p><p>Alignment of serum collectins with SP-D has also revealed nonconservative substitutions at amino acid positions 325 and 343 which are highly exposed on opposing ridges of the carbohydrate-binding groove [<xref ref-type="bibr" rid="B140">140</xref>]. Recent studies have substituted these residues (alone or in combination) into the SP-D NCRD in an attempt to enhance ligand binding and anti-IAV activity [<xref ref-type="bibr" rid="B54">54</xref>, <xref ref-type="bibr" rid="B116">116</xref>, <xref ref-type="bibr" rid="B138">138</xref>, <xref ref-type="bibr" rid="B140">140</xref>]. Crouch et al. recently demonstrated that a mutant of the human SP-D NCRD that contained 2 amino acid substitutions (D325A + R343V) displayed enhanced anti-IAV activity <italic>in vitro</italic> compared to mutants which expressed either substitution alone [<xref ref-type="bibr" rid="B140">140</xref>]. Moreover, intratracheal coadministration of D325A + R343V NCRD reduced morbidity and increased viral clearance in mice infected with a reassortant of A/WSN/33 bearing a glycosylated HA, demonstrating the potential of exogenous recombinant NCRD preparations to enhance antiviral activity and reduce disease severity <italic>in vivo</italic>.</p></sec><sec sec-type="subsection" id="sec6.3"><title>6.3. Recombinant Lectins with Modified N-Glycans</title><p>pSP-D is unique in that it is the only SP-D species known to carry a sialylated sugar in its CRD domain [<xref ref-type="bibr" rid="B117">117</xref>]. Simultaneous binding of the CRD to glycans on HA/NA of IAV as well as HA-mediated recognition of terminal SA on the <italic>N</italic>-glycan expressed by the pSP-D CRD enhances antiviral activity and broadens the range of virus strains inhibited by pSP-D [<xref ref-type="bibr" rid="B118">118</xref>]. Recently, van Eijk et al. produced functionally active recombinant pSP-D (RpSP-D) and attempted to enhance the anti-IAV properties of recombinant hSP-D (RhSP-D) by introducing <italic>N</italic>-linked glycans into its CRD [<xref ref-type="bibr" rid="B141">141</xref>]. RpSP-D displayed more potent anti-IAV activity than RhSP-D but introduction of an SA-rich glycan at the same location as in the CRD of pSP-D did not enhance the anti-IAV activity of RhSP-D. Moreover, introduction of glycans at other sites within the CRD of RhSP-D interfered with protein secretion and/or lectin function. Therefore, further studies are required to determine the most effective manner in which glycan modification within the CRD can be utilized to augment lectin-mediated recognition and anti-IAV activities of RhSP-D.</p></sec></sec><sec id="sec7"><title>7. Conclusions</title><p>It is clear that endogenous lectins are important contributors to pulmonary defense against IAV via direct recognition of free virus (and virus-infected cells) as well as modulating airway inflammation and disease. While classical collectins such as MBL and SP-D have been studied in detail, much less is known regarding antiviral activities of other collectins such as CL-L1, CL-K1 (collectin 11) and avian lectins, or the role that they might play <italic>in vivo</italic>. Recent findings that chickens lack SP-D but contain an additional lectin (cLL) [<xref ref-type="bibr" rid="B123">123</xref>] and that pig SP-D contains unique structural features, including an extra glycosylation site in its CRD [<xref ref-type="bibr" rid="B118">118</xref>], highlight the importance of understanding species differences and particular biochemical features that can modulate the anti-IAV activity of endogenous lectins. This in turn will inform the development of highly effective novel lectin constructs that may be used effectively to prevent and/or treat influenza infections in humans. Finally, understanding the role of endogenous lectins in natural reservoirs (including humans, pigs and avian species) and animal models (e.g., ferrets and mice) of IAV infection will aid in our understanding of factors that may limit interspecies transmission of IAV and/or modulate disease severity.</p></sec></body><back><ack><title>Authors' Contribution</title><p>W. C. Ng, M. D. Tate, A. G. Brooks, and P. C. Reading all contributed to the planning, writing and preparation of this paper.</p></ack><ack><title>Acknowledgments</title><p>This work was supported by Project Grant 1032079 from the National Health & Medical Research Council (NHMRC) of Australia. W. C. Ng is a recipient of an NHMRC Biomedical (Dora Lush) Postgraduate Research Scholarship. The Melbourne WHO Collaborating Centre for Reference and Research on Influenza is supported by the Australian Government Department of Health and Ageing.</p></ack><ref-list><ref id="B1"><label>1</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Barker</surname><given-names>WH</given-names></name><name><surname>Mullooly</surname><given-names>JP</given-names></name></person-group><article-title>Pneumonia and influenza deaths during epidemics. Implications for prevention</article-title><source><italic>Archives of Internal Medicine</italic></source><year>1982</year><volume>142</volume><issue>1</issue><fpage>85</fpage><lpage>89</lpage><pub-id pub-id-type="pmid">7053739</pub-id></element-citation></ref><ref id="B2"><label>2</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Wright</surname><given-names>PF</given-names></name><name><surname>Neumann</surname><given-names>G</given-names></name><name><surname>Kawaoka</surname><given-names>Y</given-names></name></person-group><article-title>Orthomyxoviruses</article-title><source><italic>Fields Virology</italic></source><year>2007</year><volume>2</volume><edition>5th edition</edition><publisher-loc>Philadelphia, Pa, USA</publisher-loc><publisher-name>Lippincott Williams & Wilkins</publisher-name></element-citation></ref><ref id="B3"><label>3</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Fouchier</surname><given-names>RAM</given-names></name><name><surname>Munster</surname><given-names>V</given-names></name><name><surname>Wallensten</surname><given-names>A</given-names></name><etal></etal></person-group><article-title>Characterization of a novel influenza A virus hemagglutinin subtype (H16) obtained from black-headed gulls</article-title><source><italic>Journal of Virology</italic></source><year>2005</year><volume>79</volume><issue>5</issue><fpage>2814</fpage><lpage>2822</lpage><pub-id pub-id-type="pmid">15709000</pub-id></element-citation></ref><ref id="B4"><label>4</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Murphy</surname><given-names>BR</given-names></name><name><surname>Webster</surname><given-names>RG</given-names></name></person-group><article-title>Orthomyxoviruses</article-title><source><italic>Fields Virology</italic></source><year>1996</year><publisher-loc>Philadelphia, Pa, USA</publisher-loc><publisher-name>Lippincott-Raven</publisher-name></element-citation></ref><ref id="B5"><label>5</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Skehel</surname><given-names>JJ</given-names></name><name><surname>Wiley</surname><given-names>DC</given-names></name></person-group><article-title>Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin</article-title><source><italic>Annual Review of Biochemistry</italic></source><year>2000</year><volume>69</volume><fpage>531</fpage><lpage>569</lpage></element-citation></ref><ref id="B6"><label>6</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Gong</surname><given-names>J</given-names></name><name><surname>Xu</surname><given-names>W</given-names></name><name><surname>Zhang</surname><given-names>J</given-names></name></person-group><article-title>Structure and functions of influenza virus neuraminidase</article-title><source><italic>Current Medicinal Chemistry</italic></source><year>2007</year><volume>14</volume><issue>1</issue><fpage>113</fpage><lpage>122</lpage><pub-id pub-id-type="pmid">17266572</pub-id></element-citation></ref><ref id="B7"><label>7</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Mitnaul</surname><given-names>LJ</given-names></name><name><surname>Matrosovich</surname><given-names>MN</given-names></name><name><surname>Castrucci</surname><given-names>MR</given-names></name><etal></etal></person-group><article-title>Balanced hemagglutinin and neuraminidase activities are critical for efficient replication of influenza A virus</article-title><source><italic>Journal of Virology</italic></source><year>2000</year><volume>74</volume><issue>13</issue><fpage>6015</fpage><lpage>6020</lpage><pub-id pub-id-type="pmid">10846083</pub-id></element-citation></ref><ref id="B8"><label>8</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Wagner</surname><given-names>R</given-names></name><name><surname>Matrosovich</surname><given-names>M</given-names></name><name><surname>Klenk</surname><given-names>HD</given-names></name></person-group><article-title>Functional balance between haemagglutinin and neuraminidase in influenza virus infections</article-title><source><italic>Reviews in Medical Virology</italic></source><year>2002</year><volume>12</volume><issue>3</issue><fpage>159</fpage><lpage>166</lpage><pub-id pub-id-type="pmid">11987141</pub-id></element-citation></ref><ref id="B9"><label>9</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Basak</surname><given-names>S</given-names></name><name><surname>Pritchard</surname><given-names>DG</given-names></name><name><surname>Brown</surname><given-names>AS</given-names></name><name><surname>Compans</surname><given-names>RW</given-names></name></person-group><article-title>Glycosylation sites of influenza viral glycoproteins: characterization of tryptic glycopeptides from the A/USSR(H1N1) hemagglutinin glycoprotein</article-title><source><italic>Journal of Virology</italic></source><year>1981</year><volume>37</volume><issue>2</issue><fpage>549</fpage><lpage>558</lpage><pub-id pub-id-type="pmid">7218432</pub-id></element-citation></ref><ref id="B10"><label>10</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ward</surname><given-names>CW</given-names></name><name><surname>Dopheide</surname><given-names>TA</given-names></name></person-group><article-title>Amino acid sequence and oligosaccharide distribution of the haemagglutinin from an early Hong Kong influenza virus variant A/Aichi/2/68 (X-31)</article-title><source><italic>Biochemical Journal</italic></source><year>1981</year><volume>193</volume><issue>3</issue><fpage>953</fpage><lpage>962</lpage><pub-id pub-id-type="pmid">7305969</pub-id></element-citation></ref><ref id="B11"><label>11</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Imperiali</surname><given-names>B</given-names></name><name><surname>Hendrickson</surname><given-names>TL</given-names></name></person-group><article-title>Asparagine-linked glycosylation: specificity and function of oligosaccharyl transferase</article-title><source><italic>Bioorganic and Medicinal Chemistry</italic></source><year>1995</year><volume>3</volume><issue>12</issue><fpage>1565</fpage><lpage>1578</lpage><pub-id pub-id-type="pmid">8770382</pub-id></element-citation></ref><ref id="B12"><label>12</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kornfeld</surname><given-names>R</given-names></name><name><surname>Kornfeld</surname><given-names>S</given-names></name></person-group><article-title>Assembly of asparagine-linked oligosaccharides</article-title><source><italic>Annual Review of Biochemistry</italic></source><year>1985</year><volume>54</volume><fpage>631</fpage><lpage>664</lpage></element-citation></ref><ref id="B13"><label>13</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Basak</surname><given-names>S</given-names></name><name><surname>Tomana</surname><given-names>M</given-names></name><name><surname>Compans</surname><given-names>RW</given-names></name></person-group><article-title>Sialic acid is incorporated into influenza hemagglutinin glycoproteins in the absence of viral neuraminidase</article-title><source><italic>Virus Research</italic></source><year>1985</year><volume>2</volume><issue>1</issue><fpage>61</fpage><lpage>68</lpage><pub-id pub-id-type="pmid">3984493</pub-id></element-citation></ref><ref id="B14"><label>14</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Nakamura</surname><given-names>K</given-names></name><name><surname>Compans</surname><given-names>RW</given-names></name></person-group><article-title>Host cell- and virus strain-dependent differences in oligosaccharides of hemagglutinin glycoproteins of influenza A viruses</article-title><source><italic>Virology</italic></source><year>1979</year><volume>95</volume><issue>1</issue><fpage>8</fpage><lpage>23</lpage><pub-id pub-id-type="pmid">442545</pub-id></element-citation></ref><ref id="B15"><label>15</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Abe</surname><given-names>Y</given-names></name><name><surname>Takashita</surname><given-names>E</given-names></name><name><surname>Sugawara</surname><given-names>K</given-names></name><name><surname>Matsuzaki</surname><given-names>Y</given-names></name><name><surname>Muraki</surname><given-names>Y</given-names></name><name><surname>Hongo</surname><given-names>S</given-names></name></person-group><article-title>Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin</article-title><source><italic>Journal of Virology</italic></source><year>2004</year><volume>78</volume><issue>18</issue><fpage>9605</fpage><lpage>9611</lpage><pub-id pub-id-type="pmid">15331693</pub-id></element-citation></ref><ref id="B16"><label>16</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Skehel</surname><given-names>JJ</given-names></name><name><surname>Stevens</surname><given-names>DJ</given-names></name><name><surname>Daniels</surname><given-names>RS</given-names></name></person-group><article-title>A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody</article-title><source><italic>Proceedings of the National Academy of Sciences of the United States of America</italic></source><year>1984</year><volume>81</volume><issue>6</issue><fpage>1779</fpage><lpage>1783</lpage><pub-id pub-id-type="pmid">6584912</pub-id></element-citation></ref><ref id="B17"><label>17</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Wei</surname><given-names>CJ</given-names></name><name><surname>Boyington</surname><given-names>JC</given-names></name><name><surname>Dai</surname><given-names>K</given-names></name><etal></etal></person-group><article-title>Cross-neutralization of 1918 and 2009 influenza viruses: role of glycans in viral evolution and vaccine design</article-title><source><italic>Science Translational Medicine</italic></source><year>2010</year><volume>2</volume><issue>24</issue><fpage>p. 24ra21</fpage></element-citation></ref><ref id="B18"><label>18</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sun</surname><given-names>S</given-names></name><name><surname>Wang</surname><given-names>Q</given-names></name><name><surname>Zhao</surname><given-names>F</given-names></name><name><surname>Chen</surname><given-names>W</given-names></name><name><surname>Li</surname><given-names>Z</given-names></name></person-group><article-title>Glycosylation site alteration in the evolution of influenza a (H1N1) viruses</article-title><source><italic>PLoS One</italic></source><year>2011</year><volume>6</volume><issue>7</issue><comment>Article ID e22844.</comment></element-citation></ref><ref id="B19"><label>19</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Zhang</surname><given-names>M</given-names></name><name><surname>Gaschen</surname><given-names>B</given-names></name><name><surname>Blay</surname><given-names>W</given-names></name><etal></etal></person-group><article-title>Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin</article-title><source><italic>Glycobiology</italic></source><year>2004</year><volume>14</volume><issue>12</issue><fpage>1229</fpage><lpage>1246</lpage><pub-id pub-id-type="pmid">15175256</pub-id></element-citation></ref><ref id="B20"><label>20</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Drickamer</surname><given-names>K</given-names></name></person-group><article-title>Two distinct classes of carbohydrate-recognition domains in animal lectins</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>1988</year><volume>263</volume><issue>20</issue><fpage>9557</fpage><lpage>9560</lpage><pub-id pub-id-type="pmid">3290208</pub-id></element-citation></ref><ref id="B21"><label>21</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Drickamer</surname><given-names>K</given-names></name><name><surname>Taylor</surname><given-names>ME</given-names></name></person-group><article-title>Biology of animal lectins</article-title><source><italic>Annual Review of Cell Biology</italic></source><year>1993</year><volume>9</volume><fpage>237</fpage><lpage>264</lpage></element-citation></ref><ref id="B22"><label>22</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Drickamer</surname><given-names>K</given-names></name></person-group><article-title>C-type lectin-like domains</article-title><source><italic>Current Opinion in Structural Biology</italic></source><year>1999</year><volume>9</volume><issue>5</issue><fpage>585</fpage><lpage>590</lpage><pub-id pub-id-type="pmid">10508765</pub-id></element-citation></ref><ref id="B23"><label>23</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Veldhuizen</surname><given-names>EJA</given-names></name><name><surname>Van Eijk</surname><given-names>M</given-names></name><name><surname>Haagsman</surname><given-names>HP</given-names></name></person-group><article-title>The carbohydrate recognition domain of collectins</article-title><source><italic>FEBS Journal</italic></source><year>2011</year><volume>278</volume><issue>20</issue><fpage>3930</fpage><lpage>3941</lpage><pub-id pub-id-type="pmid">21651725</pub-id></element-citation></ref><ref id="B24"><label>24</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Londrigan</surname><given-names>SL</given-names></name><name><surname>Turville</surname><given-names>SG</given-names></name><name><surname>Tate</surname><given-names>MD</given-names></name><name><surname>Deng</surname><given-names>Y-M</given-names></name><name><surname>Brooks</surname><given-names>AG</given-names></name><name><surname>Reading</surname><given-names>PC</given-names></name></person-group><article-title>N-linked glycosylation facilitates sialic acid-independent attachment and entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN</article-title><source><italic>Journal of Virology</italic></source><year>2011</year><volume>85</volume><issue>6</issue><fpage>2990</fpage><lpage>3000</lpage><pub-id pub-id-type="pmid">21191006</pub-id></element-citation></ref><ref id="B25"><label>25</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Upham</surname><given-names>JP</given-names></name><name><surname>Pickett</surname><given-names>D</given-names></name><name><surname>Irimura</surname><given-names>T</given-names></name><name><surname>Anders</surname><given-names>EM</given-names></name><name><surname>Reading</surname><given-names>PC</given-names></name></person-group><article-title>Macrophage receptors for influenza a virus: role of the macrophage galactose-type lectin and mannose receptor in viral entry</article-title><source><italic>Journal of Virology</italic></source><year>2010</year><volume>84</volume><issue>8</issue><fpage>3730</fpage><lpage>3737</lpage><pub-id pub-id-type="pmid">20106926</pub-id></element-citation></ref><ref id="B26"><label>26</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Rabinovich</surname><given-names>GA</given-names></name><name><surname>Liu</surname><given-names>FT</given-names></name><name><surname>Hirashima</surname><given-names>M</given-names></name><name><surname>Anderson</surname><given-names>A</given-names></name></person-group><article-title>An emerging role for galectins in tuning the immune response: lessons from experimental models of inflammatory disease, autoimmunity and cancer</article-title><source><italic>Scandinavian Journal of Immunology</italic></source><year>2007</year><volume>66</volume><issue>2-3</issue><fpage>143</fpage><lpage>158</lpage><pub-id pub-id-type="pmid">17635792</pub-id></element-citation></ref><ref id="B27"><label>27</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Yang</surname><given-names>RY</given-names></name><name><surname>Rabinovich</surname><given-names>GA</given-names></name><name><surname>Liu</surname><given-names>FT</given-names></name></person-group><article-title>Galectins: structure, function and therapeutic potential</article-title><source><italic>Expert Reviews in Molecular Medicine</italic></source><year>2008</year><volume>10</volume><issue>17, article e17</issue></element-citation></ref><ref id="B28"><label>28</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Yang</surname><given-names>M-L</given-names></name><name><surname>Chen</surname><given-names>Y-H</given-names></name><name><surname>Wang</surname><given-names>S-W</given-names></name><etal></etal></person-group><article-title>Galectin-1 binds to influenza virus and ameliorates influenza virus pathogenesis</article-title><source><italic>Journal of Virology</italic></source><year>2011</year><volume>85</volume><issue>19</issue><fpage>10010</fpage><lpage>10020</lpage><pub-id pub-id-type="pmid">21795357</pub-id></element-citation></ref><ref id="B29"><label>29</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Mantovani</surname><given-names>A</given-names></name><name><surname>Garlanda</surname><given-names>C</given-names></name><name><surname>Doni</surname><given-names>A</given-names></name><name><surname>Bottazzi</surname><given-names>B</given-names></name></person-group><article-title>Pentraxins in innate immunity: from C-reactive protein to the long pentraxin PTX3</article-title><source><italic>Journal of Clinical Immunology</italic></source><year>2008</year><volume>28</volume><issue>1</issue><fpage>1</fpage><lpage>13</lpage><pub-id pub-id-type="pmid">17828584</pub-id></element-citation></ref><ref id="B30"><label>30</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Inforzato</surname><given-names>A</given-names></name><name><surname>Bottazzi</surname><given-names>B</given-names></name><name><surname>Garlanda</surname><given-names>C</given-names></name><name><surname>Valentino</surname><given-names>S</given-names></name><name><surname>Mantovani</surname><given-names>A</given-names></name></person-group><article-title>Pentraxins in humoral innate immunity</article-title><source><italic>Advances in Experimental Medicine and Biology</italic></source><year>2012</year><volume>946</volume><fpage>1</fpage><lpage>20</lpage><pub-id pub-id-type="pmid">21948359</pub-id></element-citation></ref><ref id="B31"><label>31</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hind</surname><given-names>CRK</given-names></name><name><surname>Collins</surname><given-names>PM</given-names></name><name><surname>Renn</surname><given-names>D</given-names></name></person-group><article-title>Binding specificity of serum amyloid P component for the pyruvate acetal of galactose</article-title><source><italic>Journal of Experimental Medicine</italic></source><year>1984</year><volume>159</volume><issue>4</issue><fpage>1058</fpage><lpage>1069</lpage><pub-id pub-id-type="pmid">6707579</pub-id></element-citation></ref><ref id="B32"><label>32</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Andersen</surname><given-names>O</given-names></name><name><surname>Ravn</surname><given-names>KV</given-names></name><name><surname>Sørensen</surname><given-names>IJ</given-names></name><name><surname>Jonson</surname><given-names>G</given-names></name><name><surname>Holm Nielsen</surname><given-names>E</given-names></name><name><surname>Svehag</surname><given-names>S-E</given-names></name></person-group><article-title>Serum amyloid P component binds to influenza A virus haemagglutinin and inhibits the virus infection in vitro</article-title><source><italic>Scandinavian Journal of Immunology</italic></source><year>1997</year><volume>46</volume><issue>4</issue><fpage>331</fpage><lpage>337</lpage><pub-id pub-id-type="pmid">9350282</pub-id></element-citation></ref><ref id="B33"><label>33</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Horváth</surname><given-names>A</given-names></name><name><surname>Andersen</surname><given-names>I</given-names></name><name><surname>Junker</surname><given-names>K</given-names></name><etal></etal></person-group><article-title>Serum amyloid P component inhibits influenza A virus infections: in vitro and in vivo studies</article-title><source><italic>Antiviral Research</italic></source><year>2001</year><volume>52</volume><issue>1</issue><fpage>43</fpage><lpage>53</lpage><pub-id pub-id-type="pmid">11530187</pub-id></element-citation></ref><ref id="B34"><label>34</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Seaton</surname><given-names>BA</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name><name><surname>McCormack</surname><given-names>FX</given-names></name><name><surname>Head</surname><given-names>JF</given-names></name><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>Mendelsohn</surname><given-names>R</given-names></name></person-group><article-title>Structural determinants of pattern recognition by lung collectins</article-title><source><italic>Innate Immunity</italic></source><year>2010</year><volume>16</volume><issue>3</issue><fpage>143</fpage><lpage>150</lpage><pub-id pub-id-type="pmid">20423923</pub-id></element-citation></ref><ref id="B35"><label>35</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Gupta</surname><given-names>G</given-names></name><name><surname>Surolia</surname><given-names>A</given-names></name></person-group><article-title>Collectins: sentinels of innate immunity</article-title><source><italic>BioEssays</italic></source><year>2007</year><volume>29</volume><issue>5</issue><fpage>452</fpage><lpage>464</lpage><pub-id pub-id-type="pmid">17450595</pub-id></element-citation></ref><ref id="B36"><label>36</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Van De Wetering</surname><given-names>JK</given-names></name><name><surname>Van Golde</surname><given-names>LMG</given-names></name><name><surname>Batenburg</surname><given-names>JJ</given-names></name></person-group><article-title>Collectins: players of the innate immune system</article-title><source><italic>European Journal of Biochemistry</italic></source><year>2004</year><volume>271</volume><issue>7</issue><fpage>1229</fpage><lpage>1249</lpage><pub-id pub-id-type="pmid">15030473</pub-id></element-citation></ref><ref id="B37"><label>37</label><element-citation publication-type="book"><person-group person-group-type="author"><name><surname>Gottschalk</surname><given-names>A</given-names></name><name><surname>Belyavin</surname><given-names>G</given-names></name><name><surname>Biddle</surname><given-names>F</given-names></name></person-group><article-title>Glycoproteins as influenza virus haemagglutinin inhibitors and as cellular virus receptors</article-title><source><italic>Glycoproteins Their Composition, Structure and Function</italic></source><year>1972</year><publisher-loc>New York, NY, USA</publisher-loc><publisher-name>Elsevier</publisher-name></element-citation></ref><ref id="B38"><label>38</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Anders</surname><given-names>EM</given-names></name><name><surname>Hartley</surname><given-names>CA</given-names></name><name><surname>Jackson</surname><given-names>DC</given-names></name></person-group><article-title>Bovine and mouse serum <italic>β</italic> inhibitors of influenza A viruses are mannose-binding lectins</article-title><source><italic>Proceedings of the National Academy of Sciences of the United States of America</italic></source><year>1990</year><volume>87</volume><issue>12</issue><fpage>4485</fpage><lpage>4489</lpage><pub-id pub-id-type="pmid">2162043</pub-id></element-citation></ref><ref id="B39"><label>39</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartley</surname><given-names>CA</given-names></name><name><surname>Jackson</surname><given-names>DC</given-names></name><name><surname>Anders</surname><given-names>EM</given-names></name></person-group><article-title>Two distinct serum mannose-binding lectins function as <italic>β</italic> inhibitors of influenza virus: identification of bovine serum <italic>β</italic> inhibitor as conglutinin</article-title><source><italic>Journal of Virology</italic></source><year>1992</year><volume>66</volume><issue>7</issue><fpage>4358</fpage><lpage>4363</lpage><pub-id pub-id-type="pmid">1602549</pub-id></element-citation></ref><ref id="B40"><label>40</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hanaoka</surname><given-names>K</given-names></name><name><surname>Pritchett</surname><given-names>TJ</given-names></name><name><surname>Takasaki</surname><given-names>S</given-names></name><etal></etal></person-group><article-title>4-O-Acetyl-N-acetylneuraminic acid in the N-linked carbohydrate structures of equine and guinea pig <italic>α</italic>2-macroglobulins, potent inhibitors of influenza virus infection</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>1989</year><volume>264</volume><issue>17</issue><fpage>9842</fpage><lpage>9849</lpage><pub-id pub-id-type="pmid">2470764</pub-id></element-citation></ref><ref id="B41"><label>41</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Pritchett</surname><given-names>TJ</given-names></name><name><surname>Paulson</surname><given-names>JC</given-names></name></person-group><article-title>Basis for the potent inhibition of influenza virus infection by equine and guinea pig <italic>α</italic>2-macroglobulin</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>1989</year><volume>264</volume><issue>17</issue><fpage>9850</fpage><lpage>9858</lpage><pub-id pub-id-type="pmid">2470765</pub-id></element-citation></ref><ref id="B42"><label>42</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><etal></etal></person-group><article-title>Evidence for a protective role of pulmonary surfactant protein D (SP-D) against influenza A viruses</article-title><source><italic>Journal of Clinical Investigation</italic></source><year>1994</year><volume>94</volume><issue>1</issue><fpage>311</fpage><lpage>319</lpage><pub-id pub-id-type="pmid">8040272</pub-id></element-citation></ref><ref id="B43"><label>43</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>Sastry</surname><given-names>KN</given-names></name><name><surname>Chang</surname><given-names>D</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name></person-group><article-title>Enhanced anti-influenza activity of a surfactant protein D and serum conglutinin fusion protein</article-title><source><italic>American Journal of Physiology</italic></source><year>2000</year><volume>278</volume><issue>1</issue><fpage>L90</fpage><lpage>L98</lpage><pub-id pub-id-type="pmid">10645895</pub-id></element-citation></ref><ref id="B44"><label>44</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Reading</surname><given-names>PC</given-names></name><name><surname>Morey</surname><given-names>LS</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name><name><surname>Anders</surname><given-names>EM</given-names></name></person-group><article-title>Collectin-mediated antiviral host defense of the lung: evidence from influenza virus infection of mice</article-title><source><italic>Journal of Virology</italic></source><year>1997</year><volume>71</volume><issue>11</issue><fpage>8204</fpage><lpage>8212</lpage><pub-id pub-id-type="pmid">9343171</pub-id></element-citation></ref><ref id="B45"><label>45</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Benne</surname><given-names>CA</given-names></name><name><surname>Kraaijeveld</surname><given-names>CA</given-names></name><name><surname>Van Strijp</surname><given-names>JAG</given-names></name><etal></etal></person-group><article-title>Interactions of surfactant protein A with influenza A viruses: binding and neutralization</article-title><source><italic>Journal of Infectious Diseases</italic></source><year>1995</year><volume>171</volume><issue>2</issue><fpage>335</fpage><lpage>341</lpage><pub-id pub-id-type="pmid">7844369</pub-id></element-citation></ref><ref id="B46"><label>46</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Mikerov</surname><given-names>AN</given-names></name><name><surname>White</surname><given-names>M</given-names></name><name><surname>Hartshorn</surname><given-names>K</given-names></name><name><surname>Wang</surname><given-names>G</given-names></name><name><surname>Floros</surname><given-names>J</given-names></name></person-group><article-title>Inhibition of hemagglutination activity of influenza a viruses by SP-A1 and SP-A2 variants expressed in CHO cells</article-title><source><italic>Medical Microbiology and Immunology</italic></source><year>2008</year><volume>197</volume><issue>1</issue><fpage>9</fpage><lpage>12</lpage><pub-id pub-id-type="pmid">17520282</pub-id></element-citation></ref><ref id="B47"><label>47</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hawgood</surname><given-names>S</given-names></name><name><surname>Brown</surname><given-names>C</given-names></name><name><surname>Edmondson</surname><given-names>J</given-names></name><etal></etal></person-group><article-title>Pulmonary collectins modulate strain-specific influenza A virus infection and host responses</article-title><source><italic>Journal of Virology</italic></source><year>2004</year><volume>78</volume><issue>16</issue><fpage>8565</fpage><lpage>8572</lpage><pub-id pub-id-type="pmid">15280465</pub-id></element-citation></ref><ref id="B48"><label>48</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>LeVine</surname><given-names>AM</given-names></name><name><surname>Whitsett</surname><given-names>JA</given-names></name><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name><name><surname>Korfhagen</surname><given-names>TR</given-names></name></person-group><article-title>Surfactant protein D enhances clearance of influenza A virus from the lung in vivo</article-title><source><italic>Journal of Immunology</italic></source><year>2001</year><volume>167</volume><issue>10</issue><fpage>5868</fpage><lpage>5873</lpage></element-citation></ref><ref id="B49"><label>49</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tate</surname><given-names>MD</given-names></name><name><surname>Brooks</surname><given-names>AG</given-names></name><name><surname>Reading</surname><given-names>PC</given-names></name></person-group><article-title>Inhibition of lectin-mediated innate host defences in vivo modulates disease severity during influenza virus infection</article-title><source><italic>Immunology and Cell Biology</italic></source><year>2011</year><volume>89</volume><issue>3</issue><fpage>482</fpage><lpage>491</lpage><pub-id pub-id-type="pmid">20938455</pub-id></element-citation></ref><ref id="B50"><label>50</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Vigerust</surname><given-names>DJ</given-names></name><name><surname>Ulett</surname><given-names>KB</given-names></name><name><surname>Boyd</surname><given-names>KL</given-names></name><name><surname>Madsen</surname><given-names>J</given-names></name><name><surname>Hawgood</surname><given-names>S</given-names></name><name><surname>McCullers</surname><given-names>JA</given-names></name></person-group><article-title>N-linked glycosylation attenuates H3N2 influenza viruses</article-title><source><italic>Journal of Virology</italic></source><year>2007</year><volume>81</volume><issue>16</issue><fpage>8593</fpage><lpage>8600</lpage><pub-id pub-id-type="pmid">17553891</pub-id></element-citation></ref><ref id="B51"><label>51</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Mogues</surname><given-names>T</given-names></name><name><surname>Ligtenberg</surname><given-names>T</given-names></name><name><surname>Crouch</surname><given-names>E</given-names></name><name><surname>Holmskov</surname><given-names>U</given-names></name></person-group><article-title>Lung and salivary scavenger receptor glycoprotein-340 contribute to the host defense against influenza A viruses</article-title><source><italic>American Journal of Physiology</italic></source><year>2003</year><volume>285</volume><issue>5</issue><fpage>L1066</fpage><lpage>L1076</lpage><pub-id pub-id-type="pmid">12871854</pub-id></element-citation></ref><ref id="B52"><label>52</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>Crouch</surname><given-names>E</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><etal></etal></person-group><article-title>Pulmonary surfactant proteins A and D enhance neutrophil uptake of bacteria</article-title><source><italic>American Journal of Physiology</italic></source><year>1998</year><volume>274</volume><issue>6</issue><fpage>L958</fpage><lpage>L969</lpage><pub-id pub-id-type="pmid">9609735</pub-id></element-citation></ref><ref id="B53"><label>53</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Crouch</surname><given-names>E</given-names></name><name><surname>Persson</surname><given-names>A</given-names></name><name><surname>Chang</surname><given-names>D</given-names></name><name><surname>Heuser</surname><given-names>J</given-names></name></person-group><article-title>Molecular structure of pulmonary surfactant protein D (SP-D)</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>1994</year><volume>269</volume><issue>25</issue><fpage>17311</fpage><lpage>17319</lpage><pub-id pub-id-type="pmid">8006040</pub-id></element-citation></ref><ref id="B54"><label>54</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Crouch</surname><given-names>EC</given-names></name><name><surname>Smith</surname><given-names>K</given-names></name><name><surname>McDonald</surname><given-names>B</given-names></name><etal></etal></person-group><article-title>Species differences in the carbohydrate binding preferences of surfactant protein D</article-title><source><italic>American Journal of Respiratory Cell and Molecular Biology</italic></source><year>2006</year><volume>35</volume><issue>1</issue><fpage>84</fpage><lpage>94</lpage><pub-id pub-id-type="pmid">16514117</pub-id></element-citation></ref><ref id="B55"><label>55</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tecle</surname><given-names>T</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Sorensen</surname><given-names>G</given-names></name><etal></etal></person-group><article-title>Critical role for cross-linking of trimeric lectin domains of surfactant protein D in antiviral activity against influenza A virus</article-title><source><italic>Biochemical Journal</italic></source><year>2008</year><volume>412</volume><issue>2</issue><fpage>323</fpage><lpage>329</lpage><pub-id pub-id-type="pmid">18302538</pub-id></element-citation></ref><ref id="B56"><label>56</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Tecle</surname><given-names>T</given-names></name><etal></etal></person-group><article-title>Reduced influenza viral neutralizing activity of natural human trimers of surfactant protein D</article-title><source><italic>Respiratory Research</italic></source><year>2007</year><volume>8, article 9</volume></element-citation></ref><ref id="B57"><label>57</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>White</surname><given-names>M</given-names></name><name><surname>Kingma</surname><given-names>P</given-names></name><name><surname>Tecle</surname><given-names>T</given-names></name><etal></etal></person-group><article-title>Multimerization of surfactant protein D, but not its collagen domain, is required for antiviral and opsonic activities related to influenza virus</article-title><source><italic>Journal of Immunology</italic></source><year>2008</year><volume>181</volume><issue>11</issue><fpage>7936</fpage><lpage>7943</lpage></element-citation></ref><ref id="B58"><label>58</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>Webby</surname><given-names>R</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><etal></etal></person-group><article-title>Role of viral hemagglutinin glycosylation in anti-influenza activities of recombinant surfactant protein D</article-title><source><italic>Respiratory research</italic></source><year>2008</year><volume>9, article 65</volume></element-citation></ref><ref id="B59"><label>59</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Voelker</surname><given-names>DR</given-names></name><name><surname>Coburn</surname><given-names>J</given-names></name><name><surname>Zaner</surname><given-names>K</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name></person-group><article-title>Mechanism of binding of surfactant protein D to influenza A viruses: importance of binding to haemagglutinin to antiviral activity</article-title><source><italic>Biochemical Journal</italic></source><year>2000</year><volume>351</volume><issue>2</issue><fpage>449</fpage><lpage>458</lpage><pub-id pub-id-type="pmid">11023831</pub-id></element-citation></ref><ref id="B60"><label>60</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tecle</surname><given-names>T</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name><name><surname>Hartshorn</surname><given-names>KL</given-names></name></person-group><article-title>Inhibition of influenza viral neuraminidase activity by collectins</article-title><source><italic>Archives of Virology</italic></source><year>2007</year><volume>152</volume><issue>9</issue><fpage>1731</fpage><lpage>1742</lpage><pub-id pub-id-type="pmid">17514488</pub-id></element-citation></ref><ref id="B61"><label>61</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>Reid</surname><given-names>KBM</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><etal></etal></person-group><article-title>Neutrophil deactivation by influenza A viruses: mechanisms of protection after viral opsonization with collectins and hemagglutination-inhibiting antibodies</article-title><source><italic>Blood</italic></source><year>1996</year><volume>87</volume><issue>8</issue><fpage>3450</fpage><lpage>3461</lpage><pub-id pub-id-type="pmid">8605364</pub-id></element-citation></ref><ref id="B62"><label>62</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hirche</surname><given-names>TO</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name><name><surname>Espinola</surname><given-names>M</given-names></name><etal></etal></person-group><article-title>Neutrophil serine proteinases inactivate surfactant protein D by cleaving within a conserved subregion of the carbohydrate recognition domain</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>2004</year><volume>279</volume><issue>26</issue><fpage>27688</fpage><lpage>27698</lpage><pub-id pub-id-type="pmid">15078883</pub-id></element-citation></ref><ref id="B63"><label>63</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Tecle</surname><given-names>T</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name><name><surname>Hartshorn</surname><given-names>KL</given-names></name></person-group><article-title>Impact of neutrophils on antiviral activity of human bronchoalveolar lavage fluid</article-title><source><italic>American Journal of Physiology</italic></source><year>2007</year><volume>293</volume><issue>5</issue><fpage>L1293</fpage><lpage>L1299</lpage><pub-id pub-id-type="pmid">17720872</pub-id></element-citation></ref><ref id="B64"><label>64</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Leth-Larsen</surname><given-names>R</given-names></name><name><surname>Garred</surname><given-names>P</given-names></name><name><surname>Jensenius</surname><given-names>H</given-names></name><etal></etal></person-group><article-title>A common polymorphism in the SFTPD gene influences assembly, function, and concentration of surfactant protein D</article-title><source><italic>Journal of Immunology</italic></source><year>2005</year><volume>174</volume><issue>3</issue><fpage>1532</fpage><lpage>1538</lpage></element-citation></ref><ref id="B65"><label>65</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tate</surname><given-names>MD</given-names></name><name><surname>Job</surname><given-names>ER</given-names></name><name><surname>Brooks</surname><given-names>AG</given-names></name><name><surname>Reading</surname><given-names>PC</given-names></name></person-group><article-title>Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 influenza viruses to innate proteins in airway secretions and virulence in mice</article-title><source><italic>Virology</italic></source><year>2011</year><volume>413</volume><issue>1</issue><fpage>84</fpage><lpage>92</lpage><pub-id pub-id-type="pmid">21353279</pub-id></element-citation></ref><ref id="B66"><label>66</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tate</surname><given-names>MD</given-names></name><name><surname>Brooks</surname><given-names>AG</given-names></name><name><surname>Reading</surname><given-names>PC</given-names></name></person-group><article-title>Specific sites of N-linked glycosylation on the hemagglutinin of H1N1 subtype influenza A virus determine sensitivity to inhibitors of the innate immune system and virulence in mice</article-title><source><italic>Journal of Immunology</italic></source><year>2011</year><volume>187</volume><issue>4</issue><fpage>1884</fpage><lpage>1894</lpage></element-citation></ref><ref id="B67"><label>67</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ikegami</surname><given-names>M</given-names></name><name><surname>Na</surname><given-names>CL</given-names></name><name><surname>Korfhagen</surname><given-names>TR</given-names></name><name><surname>Whitsett</surname><given-names>JA</given-names></name></person-group><article-title>Surfactant protein D influences surfactant ultrastructure and uptake by alveolar type II cells</article-title><source><italic>American Journal of Physiology</italic></source><year>2005</year><volume>288</volume><issue>3</issue><fpage>L552</fpage><lpage>L561</lpage><pub-id pub-id-type="pmid">15579631</pub-id></element-citation></ref><ref id="B68"><label>68</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ikegami</surname><given-names>M</given-names></name><name><surname>Whitsett</surname><given-names>JA</given-names></name><name><surname>Jobe</surname><given-names>A</given-names></name><name><surname>Ross</surname><given-names>G</given-names></name><name><surname>Fisher</surname><given-names>J</given-names></name><name><surname>Korfhagen</surname><given-names>T</given-names></name></person-group><article-title>Surfactant metabolism in SP-D gene-targeted mice</article-title><source><italic>American Journal of Physiology</italic></source><year>2000</year><volume>279</volume><issue>3</issue><fpage>L468</fpage><lpage>L476</lpage><pub-id pub-id-type="pmid">10956621</pub-id></element-citation></ref><ref id="B69"><label>69</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Korfhagen</surname><given-names>TR</given-names></name><name><surname>Sheftelyevich</surname><given-names>V</given-names></name><name><surname>Burhans</surname><given-names>MS</given-names></name><etal></etal></person-group><article-title>Surfactant protein-D regulates surfactant phospholipid homeostasis in vivo</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>1998</year><volume>273</volume><issue>43</issue><fpage>28438</fpage><lpage>28443</lpage><pub-id pub-id-type="pmid">9774472</pub-id></element-citation></ref><ref id="B70"><label>70</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kingma</surname><given-names>PS</given-names></name><name><surname>Zhang</surname><given-names>L</given-names></name><name><surname>Ikegami</surname><given-names>M</given-names></name><name><surname>Hartshorn</surname><given-names>K</given-names></name><name><surname>McCormack</surname><given-names>FX</given-names></name><name><surname>Whitsett</surname><given-names>JA</given-names></name></person-group><article-title>Correction of pulmonary abnormalities in <italic>Sftpd-/-</italic> mice requires the collagenous domain of surfactant protein D</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>2006</year><volume>281</volume><issue>34</issue><fpage>24496</fpage><lpage>24505</lpage><pub-id pub-id-type="pmid">16787926</pub-id></element-citation></ref><ref id="B71"><label>71</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Zhang</surname><given-names>L</given-names></name><name><surname>Ikegami</surname><given-names>M</given-names></name><name><surname>Korfhagen</surname><given-names>TR</given-names></name><etal></etal></person-group><article-title>Neither SP-A nor NH2-terminal domains of SP-A can substitute for SP-D in regulation of alveolar homeostasis</article-title><source><italic>American Journal of Physiology</italic></source><year>2006</year><volume>291</volume><issue>2</issue><fpage>L181</fpage><lpage>L190</lpage><pub-id pub-id-type="pmid">16500946</pub-id></element-citation></ref><ref id="B72"><label>72</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Reading</surname><given-names>PC</given-names></name><name><surname>Allison</surname><given-names>J</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name><name><surname>Margot Anders</surname><given-names>E</given-names></name></person-group><article-title>Increased susceptibility of diabetic mice to influenza virus infection: compromise of collectin-mediated host defense of the lung by glucose?</article-title><source><italic>Journal of Virology</italic></source><year>1998</year><volume>72</volume><issue>8</issue><fpage>6884</fpage><lpage>6887</lpage><pub-id pub-id-type="pmid">9658139</pub-id></element-citation></ref><ref id="B73"><label>73</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Takahashi</surname><given-names>K</given-names></name><name><surname>Ip</surname><given-names>WKE</given-names></name><name><surname>Michelow</surname><given-names>IC</given-names></name><name><surname>Ezekowitz</surname><given-names>RAB</given-names></name></person-group><article-title>The mannose-binding lectin: a prototypic pattern recognition molecule</article-title><source><italic>Current Opinion in Immunology</italic></source><year>2006</year><volume>18</volume><issue>1</issue><fpage>16</fpage><lpage>23</lpage><pub-id pub-id-type="pmid">16368230</pub-id></element-citation></ref><ref id="B74"><label>74</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Haurum</surname><given-names>JS</given-names></name><name><surname>Thiel</surname><given-names>S</given-names></name><name><surname>Haagsman</surname><given-names>HP</given-names></name><name><surname>Laursen</surname><given-names>SB</given-names></name><name><surname>Larsen</surname><given-names>B</given-names></name><name><surname>Jensenius</surname><given-names>JC</given-names></name></person-group><article-title>Studies on the carbohydrate-binding characteristics of human pulmonary surfactant-associated protein A and comparison with two other collectins: Mannan-binding protein and conglutinin</article-title><source><italic>Biochemical Journal</italic></source><year>1993</year><volume>293</volume><issue>3</issue><fpage>873</fpage><lpage>878</lpage><pub-id pub-id-type="pmid">8352755</pub-id></element-citation></ref><ref id="B75"><label>75</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Fujita</surname><given-names>T</given-names></name><name><surname>Matsushita</surname><given-names>M</given-names></name><name><surname>Endo</surname><given-names>Y</given-names></name></person-group><article-title>The lectin-complement pathway—its role in innate immunity and evolution</article-title><source><italic>Immunological Reviews</italic></source><year>2004</year><volume>198</volume><fpage>185</fpage><lpage>202</lpage><pub-id pub-id-type="pmid">15199963</pub-id></element-citation></ref><ref id="B76"><label>76</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Takahashi</surname><given-names>M</given-names></name><name><surname>Mori</surname><given-names>S</given-names></name><name><surname>Shigeta</surname><given-names>S</given-names></name><name><surname>Fujita</surname><given-names>T</given-names></name></person-group><article-title>Role of MBL-associated serine protease (MASP) on activation of the lectin complement pathway</article-title><source><italic>Advances in Experimental Medicine and Biology</italic></source><year>2007</year><volume>598</volume><fpage>93</fpage><lpage>104</lpage><pub-id pub-id-type="pmid">17892207</pub-id></element-citation></ref><ref id="B77"><label>77</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Krarup</surname><given-names>A</given-names></name><name><surname>Wallis</surname><given-names>R</given-names></name><name><surname>Presanis</surname><given-names>JS</given-names></name><name><surname>Gál</surname><given-names>P</given-names></name><name><surname>Sim</surname><given-names>RB</given-names></name></person-group><article-title>Simultaneous activation of complement and coagulation by MBL-associated serine protease 2</article-title><source><italic>PLoS One</italic></source><year>2007</year><volume>2</volume><issue>7, article no. e623</issue></element-citation></ref><ref id="B78"><label>78</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Presanis</surname><given-names>JS</given-names></name><name><surname>Hajela</surname><given-names>K</given-names></name><name><surname>Ambrus</surname><given-names>G</given-names></name><name><surname>Gál</surname><given-names>P</given-names></name><name><surname>Sim</surname><given-names>RB</given-names></name></person-group><article-title>Differential substrate and inhibitor profiles for human MASP-1 and MASP-2</article-title><source><italic>Molecular Immunology</italic></source><year>2004</year><volume>40</volume><issue>13</issue><fpage>921</fpage><lpage>929</lpage><pub-id pub-id-type="pmid">14725788</pub-id></element-citation></ref><ref id="B79"><label>79</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sastry</surname><given-names>R</given-names></name><name><surname>Wang</surname><given-names>JS</given-names></name><name><surname>Brown</surname><given-names>DC</given-names></name><name><surname>Ezekowitz</surname><given-names>RA</given-names></name><name><surname>Tauber</surname><given-names>AI</given-names></name><name><surname>Sastry</surname><given-names>KN</given-names></name></person-group><article-title>Characterization of murine mannose-binding protein genes Mbl1 and Mbl2 reveals features common to other collectin genes</article-title><source><italic>Mammalian Genome</italic></source><year>1995</year><volume>6</volume><issue>2</issue><fpage>103</fpage><lpage>110</lpage><pub-id pub-id-type="pmid">7766991</pub-id></element-citation></ref><ref id="B80"><label>80</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Takahashi</surname><given-names>K</given-names></name></person-group><article-title>Lessons learned from murine models of mannose-binding lectin deficiency</article-title><source><italic>Biochemical Society Transactions</italic></source><year>2008</year><volume>36</volume><issue>6</issue><fpage>1487</fpage><lpage>1490</lpage><pub-id pub-id-type="pmid">19021581</pub-id></element-citation></ref><ref id="B81"><label>81</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hansen</surname><given-names>S</given-names></name><name><surname>Thiel</surname><given-names>S</given-names></name><name><surname>Willis</surname><given-names>A</given-names></name><name><surname>Holmskov</surname><given-names>U</given-names></name><name><surname>Jensenius</surname><given-names>JC</given-names></name></person-group><article-title>Purification and characterization of two mannan-binding lectins from mouse serum</article-title><source><italic>Journal of Immunology</italic></source><year>2000</year><volume>164</volume><issue>5</issue><fpage>2610</fpage><lpage>2618</lpage></element-citation></ref><ref id="B82"><label>82</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Eisen</surname><given-names>DP</given-names></name></person-group><article-title>Mannose-binding lectin deficiency and respiratory tract infection</article-title><source><italic>Journal of Innate Immunity</italic></source><year>2010</year><volume>2</volume><issue>2</issue><fpage>114</fpage><lpage>122</lpage><pub-id pub-id-type="pmid">20375630</pub-id></element-citation></ref><ref id="B83"><label>83</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Fidler</surname><given-names>KJ</given-names></name><name><surname>Hilliard</surname><given-names>TN</given-names></name><name><surname>Bush</surname><given-names>A</given-names></name><etal></etal></person-group><article-title>Mannose-binding lectin is present in the infected airway: a possible pulmonary defence mechanism</article-title><source><italic>Thorax</italic></source><year>2009</year><volume>64</volume><issue>2</issue><fpage>150</fpage><lpage>155</lpage><pub-id pub-id-type="pmid">18988662</pub-id></element-citation></ref><ref id="B84"><label>84</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Chang</surname><given-names>WC</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Moyo</surname><given-names>P</given-names></name><etal></etal></person-group><article-title>Lack of the pattern recognition molecule mannose-binding lectin increases susceptibility to influenza A virus infection</article-title><source><italic>BMC Immunology</italic></source><year>2010</year><volume>11, article 64</volume></element-citation></ref><ref id="B85"><label>85</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Shepherd</surname><given-names>V</given-names></name><name><surname>Reid</surname><given-names>K</given-names></name><name><surname>Jensenius</surname><given-names>JG</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name></person-group><article-title>Mechanisms of anti-influenza activity of surfactant proteins A and D: comparison with serum collectins</article-title><source><italic>American Journal of Physiology</italic></source><year>1997</year><volume>273</volume><issue>6</issue><fpage>L1156</fpage><lpage>L1166</lpage><pub-id pub-id-type="pmid">9435570</pub-id></element-citation></ref><ref id="B86"><label>86</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>Sastry</surname><given-names>K</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><etal></etal></person-group><article-title>Human mannose-binding protein functions as an opsonin for influenza A viruses</article-title><source><italic>Journal of Clinical Investigation</italic></source><year>1993</year><volume>91</volume><issue>4</issue><fpage>1414</fpage><lpage>1420</lpage><pub-id pub-id-type="pmid">7682571</pub-id></element-citation></ref><ref id="B87"><label>87</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Job</surname><given-names>ER</given-names></name><name><surname>Deng</surname><given-names>YM</given-names></name><name><surname>Tate</surname><given-names>MD</given-names></name><etal></etal></person-group><article-title>Pandemic H1N1 influenza a viruses are resistant to the antiviral activities of innate immune proteins of the collectin and pentraxin superfamilies</article-title><source><italic>Journal of Immunology</italic></source><year>2010</year><volume>185</volume><issue>7</issue><fpage>4284</fpage><lpage>4291</lpage></element-citation></ref><ref id="B88"><label>88</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kase</surname><given-names>T</given-names></name><name><surname>Suzuki</surname><given-names>Y</given-names></name><name><surname>Kawai</surname><given-names>T</given-names></name><etal></etal></person-group><article-title>Human mannan-binding lectin inhibits the infection of influenza a virus without complement</article-title><source><italic>Immunology</italic></source><year>1999</year><volume>97</volume><issue>3</issue><fpage>385</fpage><lpage>392</lpage><pub-id pub-id-type="pmid">10447758</pub-id></element-citation></ref><ref id="B89"><label>89</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Anders</surname><given-names>EM</given-names></name><name><surname>Hartley</surname><given-names>CA</given-names></name><name><surname>Reading</surname><given-names>PC</given-names></name><name><surname>Ezekowitz</surname><given-names>RAB</given-names></name></person-group><article-title>Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin</article-title><source><italic>Journal of General Virology</italic></source><year>1994</year><volume>75</volume><issue>3</issue><fpage>615</fpage><lpage>622</lpage><pub-id pub-id-type="pmid">8126457</pub-id></element-citation></ref><ref id="B90"><label>90</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Reading</surname><given-names>PC</given-names></name><name><surname>Hartley</surname><given-names>CA</given-names></name><name><surname>Ezekowitz</surname><given-names>RAB</given-names></name><name><surname>Anders</surname><given-names>EM</given-names></name></person-group><article-title>A serum mannose-binding lectin mediates complement dependent lysis of influenza virus-infected cells</article-title><source><italic>Biochemical and Biophysical Research Communications</italic></source><year>1995</year><volume>217</volume><issue>3</issue><fpage>1128</fpage><lpage>1136</lpage><pub-id pub-id-type="pmid">8554567</pub-id></element-citation></ref><ref id="B91"><label>91</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Malhotra</surname><given-names>R</given-names></name><name><surname>Haurum</surname><given-names>JS</given-names></name><name><surname>Thiel</surname><given-names>S</given-names></name><name><surname>Sim</surname><given-names>RB</given-names></name></person-group><article-title>Binding of human collectins (SP-A and MBP) to influenza virus</article-title><source><italic>Biochemical Journal</italic></source><year>1994</year><volume>304</volume><issue>2</issue><fpage>455</fpage><lpage>461</lpage><pub-id pub-id-type="pmid">7998980</pub-id></element-citation></ref><ref id="B92"><label>92</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Tokunaga</surname><given-names>H</given-names></name><name><surname>Ushirogawa</surname><given-names>H</given-names></name><name><surname>Ohuchi</surname><given-names>M</given-names></name></person-group><article-title>The pandemic (H1N1) 2009 influenza virus is resistant to mannose-binding lectin</article-title><source><italic>Virology Journal</italic></source><year>2011</year><volume>8, article 50</volume></element-citation></ref><ref id="B93"><label>93</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ling</surname><given-names>MT</given-names></name><name><surname>Tu</surname><given-names>W</given-names></name><name><surname>Han</surname><given-names>Y</given-names></name><etal></etal></person-group><article-title>Mannose-binding lectin contributes to deleterious inflammatory response in pandemic H1N1 and avian H9N2 infection</article-title><source><italic>Journal of Infectious Diseases</italic></source><year>2012</year><volume>205</volume><issue>1</issue><fpage>44</fpage><lpage>53</lpage><pub-id pub-id-type="pmid">22080095</pub-id></element-citation></ref><ref id="B94"><label>94</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ohtani</surname><given-names>K</given-names></name><name><surname>Suzuki</surname><given-names>Y</given-names></name><name><surname>Eda</surname><given-names>S</given-names></name><etal></etal></person-group><article-title>Molecular cloning of a novel human collectin from liver (CL-L1)</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>1999</year><volume>274</volume><issue>19</issue><fpage>13681</fpage><lpage>13689</lpage><pub-id pub-id-type="pmid">10224141</pub-id></element-citation></ref><ref id="B95"><label>95</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ohtani</surname><given-names>K</given-names></name><name><surname>Suzuki</surname><given-names>Y</given-names></name><name><surname>Eda</surname><given-names>S</given-names></name><etal></etal></person-group><article-title>The membrane-type Collectin CL-P1 is a scavenger receptor on vascular endothelial cells</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>2001</year><volume>276</volume><issue>47</issue><fpage>44222</fpage><lpage>44228</lpage><pub-id pub-id-type="pmid">11564734</pub-id></element-citation></ref><ref id="B96"><label>96</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hansen</surname><given-names>S</given-names></name><name><surname>Selman</surname><given-names>L</given-names></name><name><surname>Palaniyar</surname><given-names>N</given-names></name><etal></etal></person-group><article-title>Collectin 11 (CL-11, CL-K1) is a MASP-1/3-associated plasma collectin with microbial-binding activity</article-title><source><italic>Journal of Immunology</italic></source><year>2010</year><volume>185</volume><issue>10</issue><fpage>6096</fpage><lpage>6104</lpage></element-citation></ref><ref id="B97"><label>97</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Motomura</surname><given-names>W</given-names></name><name><surname>Yoshizaki</surname><given-names>T</given-names></name><name><surname>Ohtani</surname><given-names>K</given-names></name><etal></etal></person-group><article-title>Immunolocalization of a novel collectin CL-K1 in murine tissues</article-title><source><italic>Journal of Histochemistry and Cytochemistry</italic></source><year>2008</year><volume>56</volume><issue>3</issue><fpage>243</fpage><lpage>252</lpage><pub-id pub-id-type="pmid">18040075</pub-id></element-citation></ref><ref id="B98"><label>98</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Yoshizaki</surname><given-names>T</given-names></name><name><surname>Ohtani</surname><given-names>K</given-names></name><name><surname>Motomura</surname><given-names>W</given-names></name><etal></etal></person-group><article-title>Comparison of human blood concentrations of collectin kidney 1 and mannan-binding lectin</article-title><source><italic>Journal of Biochemistry</italic></source><year>2012</year><volume>151</volume><issue>1</issue><fpage>57</fpage><lpage>64</lpage><pub-id pub-id-type="pmid">21893516</pub-id></element-citation></ref><ref id="B99"><label>99</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Bordet</surname><given-names>J</given-names></name><name><surname>Gay</surname><given-names>FP</given-names></name></person-group><article-title>Sur les relations des sensibilisatrices avec l'alexine</article-title><source><italic>Annales de l'Institut Pasteur</italic></source><year>1906</year><volume>20</volume><fpage>467</fpage><lpage>498</lpage></element-citation></ref><ref id="B100"><label>100</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lachmann</surname><given-names>PJ</given-names></name></person-group><article-title>Conglutinin and Immunoconglutinins</article-title><source><italic>Advances in Immunology</italic></source><year>1967</year><volume>6</volume><fpage>479</fpage><lpage>527</lpage><pub-id pub-id-type="pmid">4860249</pub-id></element-citation></ref><ref id="B101"><label>101</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lachmann</surname><given-names>PJ</given-names></name><name><surname>Müller-Eberhard</surname><given-names>HJ</given-names></name></person-group><article-title>The demonstration in human serum of “conglutinogen-activating factor” and its effect on the third component of complement</article-title><source><italic>Journal of Immunology</italic></source><year>1968</year><volume>100</volume><issue>4</issue><fpage>691</fpage><lpage>698</lpage></element-citation></ref><ref id="B102"><label>102</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hansen</surname><given-names>S</given-names></name><name><surname>Holmskov</surname><given-names>U</given-names></name></person-group><article-title>Lung surfactant protein D (SP-D) and the molecular diverted descendants: conglutinin, CL-43 and CL-46</article-title><source><italic>Immunobiology</italic></source><year>2002</year><volume>205</volume><issue>4-5</issue><fpage>498</fpage><lpage>517</lpage><pub-id pub-id-type="pmid">12396011</pub-id></element-citation></ref><ref id="B103"><label>103</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>Holmskov</surname><given-names>U</given-names></name><name><surname>Hansen</surname><given-names>S</given-names></name><etal></etal></person-group><article-title>Distinctive anti-influenza properties of recombinant collectin 43</article-title><source><italic>Biochemical Journal</italic></source><year>2002</year><volume>366</volume><issue>1</issue><fpage>87</fpage><lpage>96</lpage><pub-id pub-id-type="pmid">11971759</pub-id></element-citation></ref><ref id="B104"><label>104</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Rothmann</surname><given-names>AB</given-names></name><name><surname>Mortensen</surname><given-names>HD</given-names></name><name><surname>Holmskov</surname><given-names>U</given-names></name><name><surname>Hojrup</surname><given-names>P</given-names></name></person-group><article-title>Structural characterization of bovine collectin-43</article-title><source><italic>European Journal of Biochemistry</italic></source><year>1997</year><volume>243</volume><issue>3</issue><fpage>630</fpage><lpage>635</lpage><pub-id pub-id-type="pmid">9057825</pub-id></element-citation></ref><ref id="B105"><label>105</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Wakamiya</surname><given-names>N</given-names></name><name><surname>Okuno</surname><given-names>Y</given-names></name><name><surname>Sasao</surname><given-names>F</given-names></name><etal></etal></person-group><article-title>Isolation and characterization of conglutinin as an influenza A virus inhibitor</article-title><source><italic>Biochemical and Biophysical Research Communications</italic></source><year>1992</year><volume>187</volume><issue>3</issue><fpage>1270</fpage><lpage>1278</lpage><pub-id pub-id-type="pmid">1417803</pub-id></element-citation></ref><ref id="B106"><label>106</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Eda</surname><given-names>S</given-names></name><name><surname>Suzuki</surname><given-names>Y</given-names></name><name><surname>Kase</surname><given-names>T</given-names></name><etal></etal></person-group><article-title>Recombinant bovine conglutinin, lacking the N-terminal and collagenous domains, has less conglutination activity but is able to inhibit haemagglutination by influenza A virus</article-title><source><italic>Biochemical Journal</italic></source><year>1996</year><volume>316</volume><issue>1</issue><fpage>43</fpage><lpage>48</lpage><pub-id pub-id-type="pmid">8645231</pub-id></element-citation></ref><ref id="B107"><label>107</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>Sastry</surname><given-names>K</given-names></name><name><surname>Brown</surname><given-names>D</given-names></name><etal></etal></person-group><article-title>Conglutinin acts as an opsonin for influenza A viruses</article-title><source><italic>Journal of Immunology</italic></source><year>1993</year><volume>151</volume><issue>11</issue><fpage>6265</fpage><lpage>6273</lpage></element-citation></ref><ref id="B108"><label>108</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kawai</surname><given-names>T</given-names></name><name><surname>Kase</surname><given-names>T</given-names></name><name><surname>Suzuki</surname><given-names>Y</given-names></name><etal></etal></person-group><article-title>Anti-influenza A virus activities of mannan-binding lectins and bovine conglutinin</article-title><source><italic>Journal of Veterinary Medical Science</italic></source><year>2007</year><volume>69</volume><issue>2</issue><fpage>221</fpage><lpage>224</lpage><pub-id pub-id-type="pmid">17339771</pub-id></element-citation></ref><ref id="B109"><label>109</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Suzuki</surname><given-names>Y</given-names></name><name><surname>Eda</surname><given-names>S</given-names></name><name><surname>Kawai</surname><given-names>T</given-names></name><etal></etal></person-group><article-title>Characterization of recombinant bovine conglutinin expressed in a mammalian cell</article-title><source><italic>Biochemical and Biophysical Research Communications</italic></source><year>1997</year><volume>238</volume><issue>3</issue><fpage>856</fpage><lpage>860</lpage><pub-id pub-id-type="pmid">9325181</pub-id></element-citation></ref><ref id="B110"><label>110</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Eda</surname><given-names>S</given-names></name><name><surname>Suzuki</surname><given-names>Y</given-names></name><name><surname>Kawai</surname><given-names>T</given-names></name><etal></etal></person-group><article-title>Structure of a truncated human surfactant protein D is less effective in agglutinating bacteria than the native structure and fails to inhibit haemagglutination by influenza A virus</article-title><source><italic>Biochemical Journal</italic></source><year>1997</year><volume>323</volume><issue>2</issue><fpage>393</fpage><lpage>399</lpage><pub-id pub-id-type="pmid">9163329</pub-id></element-citation></ref><ref id="B111"><label>111</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Eda</surname><given-names>S</given-names></name><name><surname>Suzuki</surname><given-names>Y</given-names></name><name><surname>Kawai</surname><given-names>T</given-names></name><etal></etal></person-group><article-title>Characterization of Truncated Human Mannan-Binding Protein (MBP) Expressed in Escherichia coli</article-title><source><italic>Bioscience, Biotechnology and Biochemistry</italic></source><year>1998</year><volume>62</volume><issue>7</issue><fpage>1326</fpage><lpage>1331</lpage></element-citation></ref><ref id="B112"><label>112</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Holmskov</surname><given-names>U</given-names></name><name><surname>Teisner</surname><given-names>B</given-names></name><name><surname>Willis</surname><given-names>AC</given-names></name><name><surname>Reid</surname><given-names>KBM</given-names></name><name><surname>Jensenius</surname><given-names>JC</given-names></name></person-group><article-title>Purification and characterization of a bovine serum lectin (CL-43) with structural homology to conglutinin and SP-D and carbohydrate specificity similar to mannan-binding protein</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>1993</year><volume>268</volume><issue>14</issue><fpage>10120</fpage><lpage>10125</lpage><pub-id pub-id-type="pmid">8486682</pub-id></element-citation></ref><ref id="B113"><label>113</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Holmskov</surname><given-names>U</given-names></name><name><surname>Laursen</surname><given-names>SB</given-names></name><name><surname>Malhotra</surname><given-names>R</given-names></name><etal></etal></person-group><article-title>Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins</article-title><source><italic>Biochemical Journal</italic></source><year>1995</year><volume>305</volume><issue>3</issue><fpage>889</fpage><lpage>896</lpage><pub-id pub-id-type="pmid">7848290</pub-id></element-citation></ref><ref id="B114"><label>114</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Crouch</surname><given-names>E</given-names></name><name><surname>Chang</surname><given-names>D</given-names></name><name><surname>Hartshorn</surname><given-names>KL</given-names></name></person-group><article-title>Increased antiviral and opsonic activity of a highly multimerized collectin chimera</article-title><source><italic>Biochemical and Biophysical Research Communications</italic></source><year>2001</year><volume>286</volume><issue>1</issue><fpage>206</fpage><lpage>213</lpage><pub-id pub-id-type="pmid">11485330</pub-id></element-citation></ref><ref id="B115"><label>115</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Smith</surname><given-names>K</given-names></name><etal></etal></person-group><article-title>Increasing antiviral activity of surfactant protein D trimers by introducing residues from bovine serum collectins: dissociation of mannan-binding and antiviral activity</article-title><source><italic>Scandinavian Journal of Immunology</italic></source><year>2010</year><volume>72</volume><issue>1</issue><fpage>22</fpage><lpage>30</lpage><pub-id pub-id-type="pmid">20591072</pub-id></element-citation></ref><ref id="B116"><label>116</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Tecle</surname><given-names>T</given-names></name><name><surname>Sorensen</surname><given-names>G</given-names></name><name><surname>Holmskov</surname><given-names>U</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name></person-group><article-title>Viral aggregating and opsonizing activity in collectin trimers</article-title><source><italic>American Journal of Physiology</italic></source><year>2010</year><volume>298</volume><issue>1</issue><fpage>L79</fpage><lpage>L88</lpage><pub-id pub-id-type="pmid">19837850</pub-id></element-citation></ref><ref id="B117"><label>117</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Van Eijk</surname><given-names>M</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Batenburg</surname><given-names>JJ</given-names></name><etal></etal></person-group><article-title>Interactions of influenza A virus with sialic acids present on porcine surfactant protein D</article-title><source><italic>American Journal of Respiratory Cell and Molecular Biology</italic></source><year>2004</year><volume>30</volume><issue>6</issue><fpage>871</fpage><lpage>879</lpage><pub-id pub-id-type="pmid">14672916</pub-id></element-citation></ref><ref id="B118"><label>118</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Van Eijk</surname><given-names>M</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Crouch</surname><given-names>EC</given-names></name><etal></etal></person-group><article-title>Porcine pulmonary collectins show distinct interactions with influenza A viruses: role of the N-linked oligosaccharides in the carbohydrate recognition domain</article-title><source><italic>Journal of Immunology</italic></source><year>2003</year><volume>171</volume><issue>3</issue><fpage>1431</fpage><lpage>1440</lpage></element-citation></ref><ref id="B119"><label>119</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hillaire</surname><given-names>MLB</given-names></name><name><surname>van Eijk</surname><given-names>M</given-names></name><name><surname>van Trierum</surname><given-names>SE</given-names></name><etal></etal></person-group><article-title>Assessment of the antiviral properties of recombinant porcine SP-D against various influenza A viruses in vitro</article-title><source><italic>PLoS One</italic></source><year>2011</year><volume>6</volume><issue>9</issue><comment>Article ID e25005.</comment></element-citation></ref><ref id="B120"><label>120</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Brown</surname><given-names>IH</given-names></name></person-group><article-title>The epidemiology and evolution of influenza viruses in pigs</article-title><source><italic>Veterinary Microbiology</italic></source><year>2000</year><volume>74</volume><issue>1-2</issue><fpage>29</fpage><lpage>46</lpage><pub-id pub-id-type="pmid">10799776</pub-id></element-citation></ref><ref id="B121"><label>121</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Laursen</surname><given-names>SB</given-names></name><name><surname>Dalgaard</surname><given-names>TS</given-names></name><name><surname>Thiel</surname><given-names>S</given-names></name><etal></etal></person-group><article-title>Cloning and sequencing of a cDNA encoding chicken mannan-binding lectin (MBL) and comparison with mammalian analogues</article-title><source><italic>Immunology</italic></source><year>1998</year><volume>93</volume><issue>3</issue><fpage>421</fpage><lpage>430</lpage><pub-id pub-id-type="pmid">9640255</pub-id></element-citation></ref><ref id="B122"><label>122</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hogenkamp</surname><given-names>A</given-names></name><name><surname>Van Eijk</surname><given-names>M</given-names></name><name><surname>Van Dijk</surname><given-names>A</given-names></name><name><surname>Van Asten</surname><given-names>AJAM</given-names></name><name><surname>Veldhuizen</surname><given-names>EJA</given-names></name><name><surname>Haagsman</surname><given-names>HP</given-names></name></person-group><article-title>Characterization and expression sites of newly identified chicken collectins</article-title><source><italic>Molecular Immunology</italic></source><year>2006</year><volume>43</volume><issue>10</issue><fpage>1604</fpage><lpage>1616</lpage><pub-id pub-id-type="pmid">16289291</pub-id></element-citation></ref><ref id="B123"><label>123</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hughes</surname><given-names>AL</given-names></name></person-group><article-title>Evolution of the lung surfactant proteins in birds and mammals</article-title><source><italic>Immunogenetics</italic></source><year>2007</year><volume>59</volume><issue>7</issue><fpage>565</fpage><lpage>572</lpage><pub-id pub-id-type="pmid">17457583</pub-id></element-citation></ref><ref id="B124"><label>124</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hogenkamp</surname><given-names>A</given-names></name><name><surname>Isohadouten</surname><given-names>N</given-names></name><name><surname>Reemers</surname><given-names>SSN</given-names></name><etal></etal></person-group><article-title>Chicken lung lectin is a functional C-type lectin and inhibits haemagglutination by influenza A virus</article-title><source><italic>Veterinary Microbiology</italic></source><year>2008</year><volume>130</volume><issue>1-2</issue><fpage>37</fpage><lpage>46</lpage><pub-id pub-id-type="pmid">18261862</pub-id></element-citation></ref><ref id="B125"><label>125</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Reading</surname><given-names>PC</given-names></name><name><surname>Bozza</surname><given-names>S</given-names></name><name><surname>Gilbertson</surname><given-names>B</given-names></name><etal></etal></person-group><article-title>Antiviral activity of the long chain pentraxin PTX3 against influenza viruses</article-title><source><italic>Journal of Immunology</italic></source><year>2008</year><volume>180</volume><issue>5</issue><fpage>3391</fpage><lpage>3398</lpage></element-citation></ref><ref id="B126"><label>126</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Igarashi</surname><given-names>M</given-names></name><name><surname>Ito</surname><given-names>K</given-names></name><name><surname>Yoshida</surname><given-names>R</given-names></name><name><surname>Tomabechi</surname><given-names>D</given-names></name><name><surname>Kida</surname><given-names>H</given-names></name><name><surname>Takada</surname><given-names>A</given-names></name></person-group><article-title>Predicting the antigenic structure of the pandemic (H1N1) 2009 influenza virus hemagglutinin</article-title><source><italic>PLoS One</italic></source><year>2010</year><volume>5</volume><issue>1</issue><comment>Article ID e8553.</comment></element-citation></ref><ref id="B127"><label>127</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Qi</surname><given-names>L</given-names></name><name><surname>Kash</surname><given-names>JC</given-names></name><name><surname>Dugan</surname><given-names>VG</given-names></name><etal></etal></person-group><article-title>The ability of pandemic influenza virus hemagglutinins to induce lower respiratory pathology is associated with decreased surfactant protein D binding</article-title><source><italic>Virology</italic></source><year>2011</year><volume>412</volume><issue>2</issue><fpage>426</fpage><lpage>434</lpage><pub-id pub-id-type="pmid">21334038</pub-id></element-citation></ref><ref id="B128"><label>128</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Eisen</surname><given-names>DP</given-names></name><name><surname>Marshall</surname><given-names>C</given-names></name><name><surname>Dean</surname><given-names>MM</given-names></name><etal></etal></person-group><article-title>No association between mannose-binding lectin deficiency and H1N1 2009 infection observed during the first season of this novel pandemic influenza virus</article-title><source><italic>Human Immunology</italic></source><year>2011</year><volume>72</volume><issue>11</issue><fpage>1091</fpage><lpage>1094</lpage><pub-id pub-id-type="pmid">21920399</pub-id></element-citation></ref><ref id="B129"><label>129</label><element-citation publication-type="other"><collab>WHO</collab><article-title>Avian Influenza</article-title><comment><ext-link ext-link-type="uri" xlink:href="http://www.who.int/mediacentre/factsheets/avian_influenza/en/">http://www.who.int/mediacentre/factsheets/avian_influenza/en/</ext-link></comment></element-citation></ref><ref id="B130"><label>130</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kongchanagul</surname><given-names>A</given-names></name><name><surname>Suptawiwat</surname><given-names>O</given-names></name><name><surname>Boonarkart</surname><given-names>C</given-names></name><etal></etal></person-group><article-title>Decreased expression of surfactant protein D mRNA in human lungs in fatal cases of H5N1 avian influenza</article-title><source><italic>Journal of Medical Virology</italic></source><year>2011</year><volume>83</volume><issue>8</issue><fpage>1410</fpage><lpage>1417</lpage><pub-id pub-id-type="pmid">21678446</pub-id></element-citation></ref><ref id="B131"><label>131</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Cameron</surname><given-names>CM</given-names></name><name><surname>Cameron</surname><given-names>MJ</given-names></name><name><surname>Bermejo-Martin</surname><given-names>JF</given-names></name><etal></etal></person-group><article-title>Gene expression analysis of host innate immune responses during lethal H5N1 infection in ferrets</article-title><source><italic>Journal of Virology</italic></source><year>2008</year><volume>82</volume><issue>22</issue><fpage>11308</fpage><lpage>11317</lpage><pub-id pub-id-type="pmid">18684821</pub-id></element-citation></ref><ref id="B132"><label>132</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Cillóniz</surname><given-names>C</given-names></name><name><surname>Shinya</surname><given-names>K</given-names></name><name><surname>Peng</surname><given-names>X</given-names></name><etal></etal></person-group><article-title>Lethal influenza virus infection in macaques is associated with early dysregulation of inflammatory related genes</article-title><source><italic>PLoS pathogens</italic></source><year>2009</year><volume>5</volume><issue>10</issue><comment>Article ID e1000604.</comment></element-citation></ref><ref id="B133"><label>133</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Herbert</surname><given-names>J</given-names></name><name><surname>Hutchinson</surname><given-names>WL</given-names></name><name><surname>Carr</surname><given-names>J</given-names></name><etal></etal></person-group><article-title>Influenza virus infection is not affected by serum amyloid P component</article-title><source><italic>Molecular Medicine</italic></source><year>2002</year><volume>8</volume><issue>1</issue><fpage>9</fpage><lpage>15</lpage><pub-id pub-id-type="pmid">11984001</pub-id></element-citation></ref><ref id="B134"><label>134</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Crouch</surname><given-names>E</given-names></name><name><surname>Chang</surname><given-names>D</given-names></name><etal></etal></person-group><article-title>Enhanced antiviral and opsonic activity of a human mannose-binding lectin and surfactant protein D chimera</article-title><source><italic>Journal of Immunology</italic></source><year>2000</year><volume>165</volume><issue>4</issue><fpage>2108</fpage><lpage>2115</lpage></element-citation></ref><ref id="B135"><label>135</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Chang</surname><given-names>WC</given-names></name><name><surname>Hartshorn</surname><given-names>KL</given-names></name><name><surname>White</surname><given-names>MR</given-names></name><etal></etal></person-group><article-title>Recombinant chimeric lectins consisting of mannose-binding lectin and L-ficolin are potent inhibitors of influenza A virus compared with mannose-binding lectin</article-title><source><italic>Biochemical Pharmacology</italic></source><year>2011</year><volume>81</volume><issue>3</issue><fpage>388</fpage><lpage>395</lpage><pub-id pub-id-type="pmid">21035429</pub-id></element-citation></ref><ref id="B136"><label>136</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Gardai</surname><given-names>SJ</given-names></name><name><surname>Xiao</surname><given-names>YQ</given-names></name><name><surname>Dickinson</surname><given-names>M</given-names></name><etal></etal></person-group><article-title>By binding SIRP<italic>α</italic> or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation</article-title><source><italic>Cell</italic></source><year>2003</year><volume>115</volume><issue>1</issue><fpage>13</fpage><lpage>23</lpage><pub-id pub-id-type="pmid">14531999</pub-id></element-citation></ref><ref id="B137"><label>137</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Crouch</surname><given-names>E</given-names></name><name><surname>Tu</surname><given-names>Y</given-names></name><name><surname>Briner</surname><given-names>D</given-names></name><etal></etal></person-group><article-title>Ligand specificity of human surfactant protein D: expression of a mutant trimeric collectin that shows enhanced interactions with influenza A virus</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>2005</year><volume>280</volume><issue>17</issue><fpage>17046</fpage><lpage>17056</lpage><pub-id pub-id-type="pmid">15711012</pub-id></element-citation></ref><ref id="B138"><label>138</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Crouch</surname><given-names>E</given-names></name><name><surname>Hartshorn</surname><given-names>K</given-names></name><name><surname>Horlacher</surname><given-names>T</given-names></name><etal></etal></person-group><article-title>Recognition of mannosylated ligands and influenza a virus by human surfactant protein D: contributions of an extended site and residue 343</article-title><source><italic>Biochemistry</italic></source><year>2009</year><volume>48</volume><issue>15</issue><fpage>3335</fpage><lpage>3345</lpage><pub-id pub-id-type="pmid">19249874</pub-id></element-citation></ref><ref id="B139"><label>139</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>White</surname><given-names>MR</given-names></name><name><surname>Boland</surname><given-names>P</given-names></name><name><surname>Tecle</surname><given-names>T</given-names></name><etal></etal></person-group><article-title>Enhancement of antiviral activity of collectin trimers through cross-linking and mutagenesis of the carbohydrate recognition domain</article-title><source><italic>Journal of Innate Immunity</italic></source><year>2010</year><volume>2</volume><issue>3</issue><fpage>267</fpage><lpage>279</lpage><pub-id pub-id-type="pmid">20375547</pub-id></element-citation></ref><ref id="B140"><label>140</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Crouch</surname><given-names>E</given-names></name><name><surname>Nikolaidis</surname><given-names>N</given-names></name><name><surname>McCormack</surname><given-names>FX</given-names></name><etal></etal></person-group><article-title>Mutagenesis of surfactant protein D informed by evolution and x-ray crystallography enhances defenses against influenza A virus in vivo</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>2011</year><volume>286</volume><issue>47</issue><fpage>40681</fpage><lpage>40692</lpage><pub-id pub-id-type="pmid">21965658</pub-id></element-citation></ref><ref id="B141"><label>141</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Van Eijk</surname><given-names>M</given-names></name><name><surname>Bruinsma</surname><given-names>L</given-names></name><name><surname>Hartshorn</surname><given-names>KL</given-names></name><etal></etal></person-group><article-title>Introduction of N-linked glycans in the lectin domain of surfactant protein D: impact on interactions with influenza A viruses</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>2011</year><volume>286</volume><issue>23</issue><fpage>20137</fpage><lpage>20151</lpage><pub-id pub-id-type="pmid">21489996</pub-id></element-citation></ref><ref id="B142"><label>142</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lu</surname><given-names>J</given-names></name><name><surname>Willis</surname><given-names>AC</given-names></name><name><surname>Reid</surname><given-names>KBM</given-names></name></person-group><article-title>Purification, characterization and cDNA cloning of human lung surfactant protein D</article-title><source><italic>Biochemical Journal</italic></source><year>1992</year><volume>284</volume><issue>3</issue><fpage>795</fpage><lpage>802</lpage><pub-id pub-id-type="pmid">1339284</pub-id></element-citation></ref><ref id="B143"><label>143</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hansen</surname><given-names>S</given-names></name><name><surname>Holm</surname><given-names>D</given-names></name><name><surname>Moeller</surname><given-names>V</given-names></name><etal></etal></person-group><article-title>CL-46, a novel collectin highly expressed in bovine thymus and liver</article-title><source><italic>Journal of Immunology</italic></source><year>2002</year><volume>169</volume><issue>10</issue><fpage>5726</fpage><lpage>5734</lpage></element-citation></ref><ref id="B144"><label>144</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lee</surname><given-names>RT</given-names></name><name><surname>Ichikawa</surname><given-names>Y</given-names></name><name><surname>Allen</surname><given-names>HJ</given-names></name><name><surname>Lee</surname><given-names>YC</given-names></name></person-group><article-title>Binding characteristics of galactoside-binding lectin (galaptin) from human spleen</article-title><source><italic>Journal of Biological Chemistry</italic></source><year>1990</year><volume>265</volume><issue>14</issue><fpage>7864</fpage><lpage>7871</lpage><pub-id pub-id-type="pmid">2335508</pub-id></element-citation></ref><ref id="B145"><label>145</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Reading</surname><given-names>PC</given-names></name><name><surname>Holmskov</surname><given-names>U</given-names></name><name><surname>Anders</surname><given-names>EM</given-names></name></person-group><article-title>Antiviral activity of bovine collectins against rotaviruses</article-title><source><italic>Journal of General Virology</italic></source><year>1998</year><volume>79</volume><issue>9</issue><fpage>2255</fpage><lpage>2263</lpage><pub-id pub-id-type="pmid">9747736</pub-id></element-citation></ref></ref-list></back><floats-group><fig id="fig1" position="float"><label>Figure 1</label><caption><p>Subunit organization and assembly of mammalian lectins with antiviral activity against IAV. (a) Soluble C-type lectins of the collectin superfamily. Collectin subunits are comprised of 3 identical or similar polypeptide chains associated together to form triple helices. Each polypeptide chain bears a C-terminal CRD attached to a short “neck” region, a longer collagenous domain, and a noncollagenous N-terminal domain. CL-43 exists as a trimer whereas other collectins associate together to form multimers with characteristic “cruciform-like” (e.g., SP-D or conglutinin) or “bouquet-like” structures (e.g., MBL, SP-A) or higher-order oligomers (e.g., SP-D). (b) S-type lectins or galectins are a family of <italic>β</italic>-galactosidase-binding lectins containing homologous CRDs. Galectin-1 consists of a single CRD and a short N-terminal sequence and can form noncovalent dimers. (c) Pentraxin subunits are characterized by an 8 amino acid pentraxin signature (H-x-C-x-S/T-W-x-S/T, where x is any amino acid). Subunits assemble into multimers, usually noncovalently associated pentameric or decameric structures.</p></caption><graphic xlink:href="JBB2012-732191.001"></graphic></fig><table-wrap id="tab1" position="float"><label>Table 1</label><caption><p>Comparison of monosaccharide specificity of animal lectins with anti-IAV activity.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="left" rowspan="1" colspan="1">Lectin<sup>a</sup></th><th align="center" rowspan="1" colspan="1">Family</th><th align="left" rowspan="1" colspan="1">Monosaccharide preferences<sup>b</sup></th><th align="center" rowspan="1" colspan="1">Binding to IAV</th></tr></thead><tbody><tr><td align="left" rowspan="1" colspan="1">hSP-D</td><td align="center" rowspan="1" colspan="1">C-type</td><td align="left" rowspan="1" colspan="1">L-Fuc > Mann > Gluc > Gal > GlcNAc [<xref ref-type="bibr" rid="B142">142</xref>]</td><td align="center" rowspan="1" colspan="1"> Yes</td></tr><tr><td align="left" rowspan="1" colspan="1">hMBL</td><td align="center" rowspan="1" colspan="1">C-type</td><td align="left" rowspan="1" colspan="1">GlcNAc > L-Fuc, Mann > ManNAc > Gluc > GalNAc [<xref ref-type="bibr" rid="B74">74</xref>]</td><td align="center" rowspan="1" colspan="1"> Yes</td></tr><tr><td align="left" rowspan="1" colspan="1">hCL-L1</td><td align="center" rowspan="1" colspan="1">C-type</td><td align="left" rowspan="1" colspan="1">Mann = L-Fuc = Gal > GlcNAc > GalNAc [<xref ref-type="bibr" rid="B94">94</xref>]</td><td align="center" rowspan="1" colspan="1"> —</td></tr><tr><td align="left" rowspan="1" colspan="1">hCL-K1</td><td align="center" rowspan="1" colspan="1">C-type</td><td align="left" rowspan="1" colspan="1">L-Fuc > Mann > ManNAc > GlcNAc > Gal [<xref ref-type="bibr" rid="B96">96</xref>]</td><td align="center" rowspan="1" colspan="1"> Yes</td></tr><tr><td align="left" rowspan="1" colspan="1">bConglutinin</td><td align="center" rowspan="1" colspan="1">C-type</td><td align="left" rowspan="1" colspan="1">GlcNAc > Mann, L-Fuc > Gluc > ManNAc > GalNAc [<xref ref-type="bibr" rid="B74">74</xref>]</td><td align="center" rowspan="1" colspan="1"> Yes</td></tr><tr><td align="left" rowspan="1" colspan="1">bCL-43</td><td align="center" rowspan="1" colspan="1">C-type</td><td align="left" rowspan="1" colspan="1">Mann > ManNAc > L-Fuc > GlcNAc > Gluc > GalNAc [<xref ref-type="bibr" rid="B112">112</xref>]</td><td align="center" rowspan="1" colspan="1"> Yes</td></tr><tr><td align="left" rowspan="1" colspan="1"> bCL-46</td><td align="center" rowspan="1" colspan="1"> C-type</td><td align="left" rowspan="1" colspan="1"> GlcNAc > ManNAc > Mann, Gluc, L-Fuc > Gal [<xref ref-type="bibr" rid="B143">143</xref>]</td><td align="center" rowspan="1" colspan="1"> Yes</td></tr><tr><td align="left" rowspan="1" colspan="1">hGalectin-1</td><td align="center" rowspan="1" colspan="1">S-type</td><td align="left" rowspan="1" colspan="1">Gal > GalNAc > GlcNAc, Mann [<xref ref-type="bibr" rid="B144">144</xref>]</td><td align="center" rowspan="1" colspan="1"> Yes</td></tr><tr><td align="left" rowspan="1" colspan="1">hSAP</td><td align="center" rowspan="1" colspan="1">Pentraxin</td><td align="left" rowspan="1" colspan="1">Mann > GlcNAc > L-Fuc, Gal, GalNAc [<xref ref-type="bibr" rid="B32">32</xref>]</td><td align="center" rowspan="1" colspan="1"> Yes</td></tr></tbody></table><table-wrap-foot><fn><p><sup>a</sup>Data reported for human (h) or bovine (b) lectins as indicated.</p></fn><fn><p><sup>b</sup>Abbreviation of monosaccharides: L-Fuc: L-fucose; Mann: D-mannose; Gal: D-galactose; ManNAc: N-acetyl-D-mannosamine; GlcNAc: N-acetyl-D-glucosamine; GalNAc: N-acetyl-D-galactosamine.</p></fn><fn><p>—: not reported to date.</p></fn></table-wrap-foot></table-wrap><table-wrap id="tab2" position="float"><label>Table 2</label><caption><p>Summary of antiviral activities mediated by animal lectins against IAV.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="left" rowspan="2" colspan="1">Lectin<sup>a</sup></th><th align="center" rowspan="1" colspan="1">HI</th><th align="center" rowspan="1" colspan="1">NA inhibition</th><th align="center" rowspan="1" colspan="1">Neutralization</th><th align="center" rowspan="1" colspan="1">Aggregation</th><th align="center" colspan="2" rowspan="1">Neutrophil</th><th align="center" rowspan="1" colspan="1">Selected references</th></tr><tr><th align="center" rowspan="1" colspan="1"></th><th align="center" rowspan="1" colspan="1"></th><th align="center" rowspan="1" colspan="1"></th><th align="center" rowspan="1" colspan="1"></th><th rowspan="1" colspan="1">(i) ↑ uptake</th><th align="center" rowspan="1" colspan="1">(ii) ↑ H<sub>2</sub>O<sub>2</sub></th><th align="center" rowspan="1" colspan="1"></th></tr></thead><tbody><tr><td align="left" rowspan="1" colspan="1">hSP-D</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B42">42</xref>, <xref ref-type="bibr" rid="B60">60</xref>, <xref ref-type="bibr" rid="B61">61</xref>, <xref ref-type="bibr" rid="B87">87</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">hMBL</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B60">60</xref>, <xref ref-type="bibr" rid="B85">85</xref>–<xref ref-type="bibr" rid="B88">88</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">hCL-K1</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B96">96</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">bConglutinin</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes<sup>b</sup></td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B39">39</xref>, <xref ref-type="bibr" rid="B60">60</xref>, <xref ref-type="bibr" rid="B105">105</xref>–<xref ref-type="bibr" rid="B107">107</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">bCL-43</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">No</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">No</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B60">60</xref>, <xref ref-type="bibr" rid="B103">103</xref>, <xref ref-type="bibr" rid="B115">115</xref>, <xref ref-type="bibr" rid="B145">145</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">bCL-46<sup>c</sup></td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B115">115</xref>, <xref ref-type="bibr" rid="B116">116</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">hGalectin-1</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B28">28</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1">hSAP</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">Yes</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">—</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B32">32</xref>, <xref ref-type="bibr" rid="B33">33</xref>]</td></tr></tbody></table><table-wrap-foot><fn><p><sup>a</sup>Data reported for human (h) or bovine (b) lectins as indicated.</p></fn><fn><p><sup>b</sup>Reported using recombinant chimeric protein containing the N-terminus and collagen domain of rat SP-D expressed with the neck and CRD of conglutinin.</p></fn><fn><p><sup>c</sup>Reported using CL-46 NCRDs.</p></fn><fn><p>—: not reported to date.</p></fn></table-wrap-foot></table-wrap><table-wrap id="tab3" position="float"><label>Table 3</label><caption><p>Virulence of different IAVs in mice genetically deficient in particular animal lectins.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="left" rowspan="1" colspan="1">Mice deficient in</th><th align="center" rowspan="1" colspan="1">IAV strain<sup>a</sup></th><th align="center" rowspan="1" colspan="1">Susceptibility to IAV infection</th><th align="center" rowspan="1" colspan="1">Virus growth in lungs</th><th align="left" rowspan="1" colspan="1">Comments</th><th align="center" rowspan="1" colspan="1">References</th></tr></thead><tbody><tr><td align="left" rowspan="1" colspan="1">SP-D</td><td align="center" rowspan="1" colspan="1">Phil/82</td><td align="center" rowspan="1" colspan="1">↑</td><td align="center" rowspan="1" colspan="1">↑</td><td align="left" rowspan="1" colspan="1">↑ lung inflammation</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B47">47</xref>, <xref ref-type="bibr" rid="B48">48</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1"></td><td align="center" rowspan="1" colspan="1">Phil/82Δ167</td><td align="center" rowspan="1" colspan="1">ND</td><td align="center" rowspan="1" colspan="1">ND</td><td align="left" rowspan="1" colspan="1">Lacking Asn<sub>165</sub> = less sensitive to SP-D</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B47">47</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1"></td><td align="center" rowspan="1" colspan="1">Mem71</td><td align="center" rowspan="1" colspan="1">ND</td><td align="center" rowspan="1" colspan="1">ND</td><td align="left" rowspan="1" colspan="1">Strain less sensitive to SP-D than Phil/82</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B48">48</xref>] </td></tr><tr><td align="left" colspan="6" rowspan="1"><hr></hr></td></tr><tr><td align="left" rowspan="1" colspan="1">MBL-A/C</td><td align="center" rowspan="1" colspan="1">Phil/82</td><td align="center" rowspan="1" colspan="1">↑</td><td align="center" rowspan="1" colspan="1">↑</td><td align="left" rowspan="1" colspan="1">↑ inflammation and lung injury</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B84">84</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1"></td><td align="center" rowspan="1" colspan="1">Cal/09</td><td align="center" rowspan="1" colspan="1">↓</td><td align="center" rowspan="1" colspan="1">ND</td><td align="left" rowspan="1" colspan="1">↓ inflammation and lung injury</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B93">93</xref>]</td></tr><tr><td align="left" rowspan="1" colspan="1"></td><td align="center" rowspan="1" colspan="1">H9N2/G1</td><td align="center" rowspan="1" colspan="1">↓</td><td align="center" rowspan="1" colspan="1">↓</td><td align="left" rowspan="1" colspan="1">↓ inflammation and lung injury</td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B93">93</xref>] </td></tr><tr><td align="left" colspan="6" rowspan="1"><hr></hr></td></tr><tr><td align="left" rowspan="1" colspan="1">Galectin-1</td><td align="center" rowspan="1" colspan="1">WSN/33</td><td align="center" rowspan="1" colspan="1">↑</td><td align="center" rowspan="1" colspan="1">—</td><td align="left" rowspan="1" colspan="1">HI and neutralization against IAV <italic>in vitro </italic></td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B28">28</xref>]</td></tr><tr><td align="left" colspan="6" rowspan="1"><hr></hr></td></tr><tr><td align="left" rowspan="1" colspan="1">SAP</td><td align="center" rowspan="1" colspan="1">PR8, WS/33, Shg/24</td><td align="center" rowspan="1" colspan="1">ND</td><td align="center" rowspan="1" colspan="1">ND</td><td align="left" rowspan="1" colspan="1">HI and neutralization against IAV <italic>in vitro </italic></td><td align="center" rowspan="1" colspan="1">[<xref ref-type="bibr" rid="B133">133</xref>]</td></tr></tbody></table><table-wrap-foot><fn><p><sup>a</sup>IAV strains used: A/Philippines/82 (Phil/82, H3N2); A/Mem71<sub>H</sub>-Bel<sub>N</sub> (Mem/71, H3N1); A/WSN/33 (WSN/33, H1N1); A/PR/8/34 (PR8, H1N1), A/WS/33 (WS/33, H1N1), A/California/04/09 (Cal/09, H1N1 pdm), A/Shanghai/24/90 (Shg/24, H3N2), A/Quail/Hong Kong/61/97 (H9N2/G1).</p></fn><fn><p>↑, ↓, or ND: increased, decreased, or not different to wild-type mice, respectively.</p></fn><fn><p>—: not reported to 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