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Preferential recognition of avian-like receptors in human influenza A H7N9 viruses

Academic Article
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Overview

authors

  • Xu, R.
  • de Vries, R. P.
  • Zhu, X.
  • Nycholat, C. M.
  • McBride, R.
  • Yu, W.
  • Paulson, James
  • Wilson, Ian

publication date

  • December 2013

journal

  • Science  Journal

abstract

  • The 2013 outbreak of avian-origin H7N9 influenza in eastern China has raised concerns about its ability to transmit in the human population. The hemagglutinin glycoprotein of most human H7N9 viruses carries Leu(226), a residue linked to adaptation of H2N2 and H3N2 pandemic viruses to human receptors. However, glycan array analysis of the H7 hemagglutinin reveals negligible binding to humanlike α2-6-linked receptors and strong preference for a subset of avian-like α2-3-linked glycans recognized by all avian H7 viruses. Crystal structures of H7N9 hemagglutinin and six hemagglutinin-glycan complexes have elucidated the structural basis for preferential recognition of avian-like receptors. These findings suggest that the current human H7N9 viruses are poorly adapted for efficient human-to-human transmission.

subject areas

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Birds
  • Carbohydrate Conformation
  • Crystallography, X-Ray
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Humans
  • Influenza A Virus, H7N9 Subtype
  • Influenza in Birds
  • Influenza, Human
  • Ligands
  • Microarray Analysis
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Polysaccharides
  • Receptors, Virus
  • Recombinant Proteins
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Identity

PubMed Central ID

  • PMC3954636

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1243761

PubMed ID

  • 24311689
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Additional Document Info

start page

  • 1230

end page

  • 1235

volume

  • 342

issue

  • 6163

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