Receptor specificity of subtype H1 influenza A viruses isolated from swine and humans in the United States |
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| Authors: | Chen Li-Mei Rivailler Pierre Hossain Jaber Carney Paul Balish Amanda Perry Ijeoma Davis C Todd Garten Rebecca Shu Bo Xu Xiyan Klimov Alexander Paulson James C Cox Nancy J Swenson Sabrina Stevens James Vincent Amy Gramer Marie Donis Ruben O |
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| Affiliation: | a Influenza Division, Centers for Disease Control and Prevention, Atlanta, GA, USAb Departments of Chemical Physiology and Molecular Biology, The Scripps Research Institute, La Jolla, CA, USAc USDA-APHIS, National Veterinary Services Laboratories, Ames, IA, USAd USDA-ARS, National Animal Disease Center, Ames, IA, USAe University of Minnesota Veterinary Diagnostic Laboratory, Saint Paul, MN, USA |
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| Abstract: | The evolution of classical swine influenza viruses receptor specificity preceding the emergence of the 2009 H1N1 pandemic virus was analyzed in glycan microarrays. Classical swine influenza viruses from the α, β, and γ antigenic clusters isolated between 1945 and 2009 revealed a binding profile very similar to that of 2009 pandemic H1N1 viruses, with selectivity for α2-6-linked sialosides and very limited binding to α2-3 sialosides. Despite considerable genetic divergence, the ‘human-like’ H1N1 viruses circulating in swine retained strong binding preference for α2-6 sialylated glycans. Interspecies transmission of H1N1 influenza viruses from swine to humans or from humans to swine has not driven selection of viruses with distinct novel receptor binding specificities. Classical swine and human seasonal H1N1 influenza viruses have conserved specificity for similar α2-6-sialoside receptors in spite of long term circulation in separate hosts, suggesting that humans and swine impose analogous selection pressures on the evolution of receptor binding function. |
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| Keywords: | Influenza Swine Human H1 hemagglutinin Receptor Binding Sialic acid |
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