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New insights into influenza A specificity: an evolution of paradigms.


ABSTRACT: Understanding the molecular origin of influenza receptor specificity is complicated by the paucity of quantitative affinity measurements, and the qualitative and variable nature of glycan array data. Further obstacles arise from the varied impact of viral glycosylation and the relatively narrow spectrum of biologically relevant receptors present on glycan arrays. A survey of receptor conformational properties is presented, leading to the conclusion that conformational entropy plays a key role in defining specificity, as does the newly reported ability of biantennary receptors that terminate in Sia?2-6Gal sequences to form bidentate interactions to two binding sites in a hemagglutinin trimer. Bidentate binding provides a functional explanation for the observation that Sia?2-6 receptors adopt an open-umbrella topology when bound to hemagglutinins from human-infective viruses, and calls for a reassessment of virus avidity and tissue tropism.

SUBMITTER: Ji Y 

PROVIDER: S-EPMC5715462 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature

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New insights into influenza A specificity: an evolution of paradigms.

Ji Ye Y   White Yohanna Jb YJ   Hadden Jodi A JA   Grant Oliver C OC   Woods Robert J RJ  

Current opinion in structural biology 20170601


Understanding the molecular origin of influenza receptor specificity is complicated by the paucity of quantitative affinity measurements, and the qualitative and variable nature of glycan array data. Further obstacles arise from the varied impact of viral glycosylation and the relatively narrow spectrum of biologically relevant receptors present on glycan arrays. A survey of receptor conformational properties is presented, leading to the conclusion that conformational entropy plays a key role in  ...[more]

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