National Center for
4N5Z: Crystal Structure Of Aerosol Transmissible Influenza H5 Hemagglutinin Mutant (n158d, N224k, Q226l And T318i) From The Influenza Virus A/viet Nam/1203/2004 (h5n1)
Hemagglutinin Receptor Specificity and Structural Analyses of Respiratory Droplet-Transmissible H5N1 Viruses
J. Virol. (2014) 88 p.768-773
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" alpha2-6 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.