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A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin

Academic Article
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Overview

authors

  • Xu, R.
  • Krause, J. C.
  • McBride, R.
  • Paulson, James
  • Crowe, J. E.
  • Wilson, Ian

publication date

  • March 2013

journal

  • Nature Structural & Molecular Biology  Journal

abstract

  • Influenza virus hemagglutinin (HA) mediates receptor binding and viral entry during influenza infection. The development of receptor analogs as viral-entry blockers has not been successful, which suggests that sialic acid may not be an ideal scaffold to obtain broad, potent HA inhibitors. Here, we report crystal structures of Fab fragments from three human antibodies that neutralize the 1957 pandemic H2N2 influenza virus in complex with H2 HA. All three antibodies use an aromatic residue to plug a conserved cavity in the HA receptor-binding site. Each antibody interacts with the absolutely conserved HA1 Trp153 at the cavity base through π-π stacking with the signature Phe54 of two VH1-69-encoded antibodies or a tyrosine from HCDR3 in the other antibody. This highly conserved interaction can be used as a starting point to design inhibitors targeting this conserved hydrophobic pocket in influenza viruses.

subject areas

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Antibodies, Neutralizing
  • Antibodies, Viral
  • Antigen-Antibody Complex
  • Binding Sites
  • Crystallography, X-Ray
  • Epitopes
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Humans
  • Immunoglobulin Fab Fragments
  • Influenza A Virus, H2N2 Subtype
  • Molecular Sequence Data
  • Mutation
  • Protein Conformation
  • Tryptophan
  • Tyrosine
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Identity

PubMed Central ID

  • PMC3594569

International Standard Serial Number (ISSN)

  • 1545-9993

Digital Object Identifier (DOI)

  • 10.1038/nsmb.2500

PubMed ID

  • 23396351
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Additional Document Info

start page

  • 363

end page

  • 370

volume

  • 20

issue

  • 3

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