title: The number and position of N-linked glycosylation sites in the hemagglutinin determine differential recognition of seasonal and 2009 pandemic H1N1 influenza virus by porcine surfactant protein D.
abstract: C-type lectins are important molecules of the innate immune system. These molecules, like surfactant protein D (SP-D) can recognize glycans on pathogens and neutralize these. Also influenza viruses are recognized by SP-D and their susceptibility to neutralization by SP-D is dependent on the number of N-linked glycosylation sites in the hemagglutinin in particular. Porcine SP-D displayed stronger neutralizing activity to human influenza A viruses than to swine influenza A viruses. Although viruses from these species differ with regard to the number of glycosylation sites in the hemagglutinin, the mechanism underlying the differential recognition by porcine SP-D is poorly understood. Here we investigated the molecular basis for the differential recognition of a seasonal H1N1 and a 2009 pandemic H1N1 virus by porcine SP-D. We demonstrated that the number and position of glycosylation sites determine viral susceptibility to the neutralizing activity of porcine SP-D. However, predicting the effect remains difficult as it was shown to be dependent on the strain and the position of the glycosylation sites.
authors.affiliation: Department of Virology, Erasmus Medical Center, Rotterdam, The Netherlands.
authors.forename: Marine L B
authors.initials: ML
authors.lastname: Hillaire
authors.forename: Martin
authors.initials: M
authors.lastname: van Eijk
authors.forename: Nella J
authors.initials: NJ
authors.lastname: Nieuwkoop
authors.forename: Stella E
authors.initials: SE
authors.lastname: Vogelzang-van Trierum
authors.forename: Ron A M
authors.initials: RA
authors.lastname: Fouchier
authors.forename: Albert D M E
authors.initials: AD
authors.lastname: Osterhaus
authors.forename: Henk P
authors.initials: HP
authors.lastname: Haagsman
authors.forename: Guus F
authors.initials: GF
authors.lastname: Rimmelzwaan
mesh_terms: D000818:Animals; D006031:Glycosylation; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000276:immunology* / Q000378:metabolism*; D006801:Humans; D053118:Influenza A Virus, H1N1 Subtype / Q000276:immunology*; D037102:Lectins / Q000276:immunology / Q000378:metabolism; D011485:Protein Binding; D037663:Pulmonary Surfactant-Associated Protein D / Q000276:immunology* / Q000378:metabolism*; D013552:Swine
chemical_list: D019267:Hemagglutinin Glycoproteins, Influenza Virus; D037102:Lectins; D037663:Pulmonary Surfactant-Associated Protein D; C483468:hemagglutinin, human influenza A virus