Amino Acid Substitutions That Affect Receptor Binding and Stability of the Hemagglutinin of Influenza A/H7N9 Virus.
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Authors
Abstract
Receptor-binding preference and stability of hemagglutinin have been implicated as crucial determinants of airborne transmission of influenza viruses. Here, amino acid substitutions previously identified to affect these traits were tested in the context of an A/H7N9 virus. Some combinations of substitutions, most notably G219S and K58I, resulted in relatively high affinity for α2,6-linked sialic acid receptor and acid and temperature stability. Thus, the hemagglutinin of the A/H7N9 virus may adopt traits associated with airborne transmission.
Description
Keywords
Amino Acid Substitution, Cell Line, Hemagglutinin Glycoproteins, Influenza Virus, Humans, Influenza A Virus, H7N9 Subtype, Mutant Proteins, Sialic Acids, Temperature, Virus Attachment
Journal Title
J Virol
Conference Name
Journal ISSN
0022-538X
1098-5514
1098-5514
Volume Title
90
Publisher
American Society for Microbiology
Publisher DOI
Sponsorship
European Commission (278976)
National Institutes of Health (NIH) (via Mount Sinai School of Medicine (MSSM)) (HHSN272201400008C)
National Institutes of Health (NIH) (via Mount Sinai School of Medicine (MSSM)) (HHSN272201400008C)
HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) provided funding to Eefje J. A. Schrauwen, Mathilde Richard, David Burke, Sander Herfst, and Ron A. M. Fouchier under grant number HHSN272201400008C. EU FP7 provided funding to Eefje J. A. Schrauwen, Mathilde Richard, Guus F Rimmelzwaan, Sander Herfst, and Ron A. M. Fouchier under grant number 278976 (7th Framework Programme ANTIGONE).