Amino Acid Substitutions That Affect Receptor Binding and Stability of the Hemagglutinin of Influenza A/H7N9 Virus.
2016
Schrauwen, Eefje JA | Richard, Mathilde | Burke, David F | Rimmelzwaan, Guus F | Herfst, Sander | Fouchier, Ron AM
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.
显示更多 [+] 显示较少 [-]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).
显示更多 [+] 显示较少 [-]This is the author accepted manuscript. The final version is available from the American Society for Microbiology via http://dx.doi.org/10.1128/JVI.03052-15
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