Mutagenesis of Surfactant Protein D Informed by Evolution and X-ray Crystallography Enhances Defenses against Influenza A Virus in Vivo

The recognition of influenza A virus (IAV) by surfactant protein D (SP-D) is mediated by interactions between the SP-D carbohydrate recognition domains (CRD) and glycans displayed on envelope glycoproteins. Although native human SP-D shows potent antiviral and aggregating activity, trimeric recombin...

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Veröffentlicht in:	The Journal of biological chemistry 2011-11, Vol.286 (47), p.40681-40692
Hauptverfasser:	Crouch, Erika, Nikolaidis, Nikolaos, McCormack, Francis X., McDonald, Barbara, Allen, Kimberly, Rynkiewicz, Michael J., Cafarella, Tanya M., White, Mitchell, Lewnard, Kara, Leymarie, Nancy, Zaia, Joseph, Seaton, Barbara A., Hartshorn, Kevan L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antiviral Agents - metabolism Antiviral Agents - pharmacology Collectins Crystallography, X-Ray Disease Resistance - genetics Evolution, Molecular Female Hemagglutinin Glycoproteins, Influenza Virus - chemistry Hemagglutinin Glycoproteins, Influenza Virus - metabolism Humans Influenza A Virus, H1N1 Subtype - drug effects Influenza A Virus, H1N1 Subtype - metabolism Influenza A Virus, H1N1 Subtype - physiology Innate Immunity Lectin Lung Mass Spectrometry Mice Microbiology Models, Molecular Mouse Mutagenesis, Site-Directed Orthomyxoviridae Infections - virology Protein Multimerization Protein Structure, Quaternary Protein Structure, Tertiary Pulmonary Surfactant-Associated Protein D - chemistry Pulmonary Surfactant-Associated Protein D - genetics Pulmonary Surfactant-Associated Protein D - metabolism Species Specificity Surface Plasmon Resonance - methods Surfactant Protein D Virus
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