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dc.contributor.authorHartshorn, Kevan L.en_US
dc.contributor.authorWebby, Richarden_US
dc.contributor.authorWhite, Mitchell R.en_US
dc.contributor.authorTecle, Tesfaldeten_US
dc.contributor.authorPan, Clarken_US
dc.contributor.authorBoucher, Susanen_US
dc.contributor.authorMoreland, Rodney J.en_US
dc.contributor.authorCrouch, Erika C.en_US
dc.contributor.authorScheule, Ronald K.en_US
dc.date.accessioned2012-01-09T21:04:09Z
dc.date.available2012-01-09T21:04:09Z
dc.date.copyright2008
dc.date.issued2008-9-23
dc.identifier.citationHartshorn, Kevan L, Richard Webby, Mitchell R White, Tesfaldet Tecle, Clark Pan, Susan Boucher, Rodney J Moreland, Erika C Crouch, Ronald K Scheule. "Role of viral hemagglutinin glycosylation in anti-influenza activities of recombinant surfactant protein D" Respiratory Research 9(1):65. (2008)
dc.identifier.issn1465-993X
dc.identifier.urihttps://hdl.handle.net/2144/2990
dc.description.abstractBACKGROUND. Surfactant protein D (SP-D) plays an important role in innate defense against influenza A viruses (IAVs) and other pathogens. METHODS. We tested antiviral activities of recombinant human SP-D against a panel of IAV strains that vary in glycosylation sites on their hemagglutinin (HA). For these experiments a recombinant version of human SP-D of the Met11, Ala160 genotype was used after it was characterized biochemically and structurally. RESULTS. Oligosaccharides at amino acid 165 on the HA in the H3N2 subtype and 104 in the H1N1 subtype are absent in collectin-resistant strains developed in vitro and are important for mediating antiviral activity of SP-D; however, other glycans on the HA of these viral subtypes also are involved in inhibition by SP-D. H3N2 strains obtained shortly after introduction into the human population were largely resistant to SP-D, despite having the glycan at 165. H3N2 strains have become steadily more sensitive to SP-D over time in the human population, in association with addition of other glycans to the head region of the HA. In contrast, H1N1 strains were most sensitive in the 1970s-1980s and more recent strains have become less sensitive, despite retaining the glycan at 104. Two H5N1 strains were also resistant to inhibition by SP-D. By comparing sites of glycan attachment on sensitive vs. resistant strains, specific glycan sites on the head domain of the HA are implicated as important for inhibition by SP-D. Molecular modeling of the glycan attachment sites on HA and the carbohydrate recognition domain of SPD are consistent with these observations. CONCLUSION. Inhibition by SP-D correlates with presence of several glycan attachment sites on the HA. Pandemic and avian strains appear to lack susceptibility to SP-D and this could be a contributory factor to their virulence.en_US
dc.description.sponsorshipNational Institutes of Health (HL-06931, HL-44015, HL-29594)en_US
dc.language.isoen
dc.publisherRespiratory Researchen_US
dc.rightsCopyright 2008 Hartshorn et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.en_US
dc.rights.urihttp://creativecommons.org/licenses/by/2.0
dc.titleRole of Viral Hemagglutinin Glycosylation in Anti-Influenza Activities of Recombinant Surfactant Protein Den_US
dc.typeArticleen_US
dc.identifier.doi10.1186/1465-9921-9-65
dc.identifier.pmid18811961
dc.identifier.pmcid2564921


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Copyright 2008 Hartshorn et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Except where otherwise noted, this item's license is described as Copyright 2008 Hartshorn et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.