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dc.contributor.authorHartshorn, Kevan Len_US
dc.contributor.authorWhite, Mitchell Ren_US
dc.contributor.authorTecle, Tesfaldeten_US
dc.contributor.authorTornoe, Idaen_US
dc.contributor.authorSorensen, Grith Len_US
dc.contributor.authorCrouch, Erika Cen_US
dc.contributor.authorHolmskov, Uffeen_US
dc.date.accessioned2012-01-09T21:04:09Z
dc.date.available2012-01-09T21:04:09Z
dc.date.copyright2007en_US
dc.date.issued2007-2-5en_US
dc.identifier.citationHartshorn, Kevan L, Mitchell R White, Tesfaldet Tecle, Ida Tornoe, Grith L Sorensen, Erika C Crouch, Uffe Holmskov. "Reduced influenza viral neutralizing activity of natural human trimers of surfactant protein D" Respiratory Research 8(1):9. (2007)en_US
dc.identifier.issn1465-993Xen_US
dc.identifier.urihttp://hdl.handle.net/2144/2989
dc.description.abstractBACKGROUND. Surfactant protein D (SP-D) plays important roles in innate host defense against influenza A virus (IAV) infection. Common human polymorphisms of SP-D have been found in many human populations and associated with increased risk of certain infections. We recently reported that the Thr/Thr 11 form of SP-D is associated with low serum levels and assembles predominantly as trimers as opposed to the more common multimeric forms of SP-D. METHODS. Preliminary experiments were done to establish the effects of different monoclonal antibodies against SP-D on ability of SP-D to bind to or neutralize the virus. We then purified natural human trimeric and multimeric forms of SP-D from amniotic fluid and tested ability of these preparations to bind to IAV, to inhibit infectivity and hemagglutination activity of IAV in vitro. RESULTS. In initial experiments mAbs directed against different areas on the CRD of SP-D were found to have differing effects on antiviral activity. Using an mAb that did not interfere with antiviral activity of SP-D, we confirm that natural SP-D trimers had reduced ability to bind to IAV. In addition, the trimers had reduced ability to neutralize IAV as compared to natural human SP-D multimers as well as reduced hemagglutination inhibiting activity against several strains of IAV. Natural SP-D trimers also had different interactions with human neutrophil peptide defensins (HNPs) in viral neutralization assays as compared to multimeric SP-D. CONCLUSION. These studies indicate that a common human polymorphic form of SP-D may modulate host defense against IAV and give impetus to clinical studies correlating this genotype with risk for IAV infection in susceptible groups. We also show that mAbs directed against different areas on the carbohydrate recognition domain of SP-D can be useful for dissecting out different functional properties of the protein.en_US
dc.language.isoenen_US
dc.publisherBioMed Centralen_US
dc.rightsCopyright 2007 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/2.0en_US
dc.titleReduced Influenza Viral Neutralizing Activity of Natural Human Trimers of Surfactant Protein Den_US
dc.typearticleen_US
dc.identifier.doi10.1186/1465-9921-8-9en_US
dc.identifier.pubmedid17280604en_US
dc.identifier.pmcid1797806en_US


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Copyright 2007 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 2007 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.