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


ABSTRACT: 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" ?2-6 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.

SUBMITTER: de Vries RP 

PROVIDER: S-EPMC3911709 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature

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

de Vries Robert P RP   Zhu Xueyong X   McBride Ryan R   Rigter Alan A   Hanson Anthony A   Zhong Gongxun G   Hatta Masato M   Xu Rui R   Yu Wenli W   Kawaoka Yoshihiro Y   de Haan Cornelis A M CA   Wilson Ian A IA   Paulson James C JC  

Journal of virology 20131030 1


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  ...[more]

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