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.
CITATION STYLE
de Vries, R. P., Zhu, X., McBride, R., Rigter, A., Hanson, A., Zhong, G., … Paulson, J. C. (2014). Hemagglutinin Receptor Specificity and Structural Analyses of Respiratory Droplet-Transmissible H5N1 Viruses. Journal of Virology, 88(1), 768–773. https://doi.org/10.1128/jvi.02690-13
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