Amino Acid 226 in the Hemagglutinin of H4N6 Influenza Virus Determines Binding Affinity for α2,6-Linked Sialic Acid and Infectivity Levels in Primary Swine and Human Respiratory Epithelial Cells
Author:
Affiliation:
1. Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, Wisconsin
2. Russian Academy of Sciences, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia
Abstract
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JVI.00718-08
Reference49 articles.
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2. Brown, I. H. 2000. The epidemiology and evolution of influenza viruses in pigs. Vet. Microbiol.74:29-46.
3. Busch, M. G., A. C. Bateman, G. A. Landolt, A. I. Karasin, R. A. Brockman-Schneider, J. E. Gern, M. Suresh, and C. W. Olsen. 2008. Identification of amino acids in the HA of H3 influenza viruses that determine infectivity levels in primary swine respiratory epithelial cells. Virus Res.133:269-279.
4. Glycan topology determines human adaptation of avian H5N1 virus hemagglutinin
5. Chou, H. H., H. Takematsu, S. Diaz, J. Iber, E. Nickerson, K. L. Wright, E. A. Muchmore, D. L. Nelson, S. T. Warren, and A. Varki. 1998. A mutation in human CMP-sialic acid hydroxylase occurred after the Homo-Pan divergence. Proc. Natl. Acad. Sci. USA95:11751-11756.
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