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Amino acid substitutions that affect receptor binding and stability of the hemagglutinin of influenza A/H7N9 virus

tetano

Editor, Senior Moderator
J Virol. 2016 Jan 20. pii: JVI.03052-15. [Epub ahead of print]
[h=1]Amino acid substitutions that affect receptor binding and stability of the hemagglutinin of influenza A/H7N9 virus.[/h] Schrauwen EJ[SUP]1[/SUP], Richard M[SUP]2[/SUP], Burke DF[SUP]3[/SUP], Rimmelzwaan GF[SUP]1[/SUP], Herfst S[SUP]1[/SUP], Fouchier RA[SUP]1[/SUP].
[h=3]Author information[/h]

[h=3]Abstract[/h] Receptor-binding preference and stability of hemagglutinin have been implied 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.
Copyright ? 2016, American Society for Microbiology. All Rights Reserved.


PMID: 26792744 [PubMed - as supplied by publisher]
 
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