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

Marine Hillaire, M (Marco) van Eijk, Nella Nieuwkoop, Stella Trierum, Ron Fouchier, Ab Osterhaus, HP Haagsman, Guus Rimmelzwaan

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18 Citations (Scopus)


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. (C) 2012 Elsevier B.V. All rights reserved.
Original languageUndefined/Unknown
Pages (from-to)301-305
Number of pages5
JournalVirus Research
Issue number1
Publication statusPublished - 2012

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  • EMC MM-04-27-01

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