Hemagglutinin receptor specificity and structural analyses of respiratory droplet-transmissible H5N1 viruses

J Virol. 2014 Jan;88(1):768-73. doi: 10.1128/JVI.02690-13. Epub 2013 Oct 30.


Two ferret-adapted H5N1 viruses capable of respiratory droplet transmission have been reported with mutations in the hemagglutinin receptor-binding site and stalk domains. Glycan microarray analysis reveals that both viruses exhibit a strong shift toward binding to "human-type" α2-6 sialosides but with notable differences in fine specificity. Crystal structure analysis further shows that the stalk mutation causes no obvious perturbation of the receptor-binding pocket, consistent with its impact on hemagglutinin stability without affecting receptor specificity.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Hemagglutinins / metabolism*
  • Humans
  • Influenza A Virus, H5N1 Subtype / physiology*


  • Hemagglutinins