Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid

Nature. 1988 Jun 2;333(6172):426-31. doi: 10.1038/333426a0.


The three-dimensional structures of influenza virus haemagglutinins complexed with cell receptor analogues show sialic acids bound to a pocket of conserved amino acids surrounded by antibody-binding sites. Sialic acid fills the conserved pocket, demonstrating that it is the influenza virus receptor. The proximity of the antibody-binding sites suggests that antibodies neutralize virus infectivity by preventing virus-to-cell binding. The structures suggest approaches to the design of anti-viral drugs that could block attachment of viruses to cells.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies / metabolism
  • Antiviral Agents / metabolism
  • Binding Sites
  • Binding Sites, Antibody
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Hemagglutinins, Viral / genetics
  • Hemagglutinins, Viral / metabolism*
  • Models, Molecular
  • N-Acetylneuraminic Acid
  • Orthomyxoviridae / analysis*
  • Protein Binding
  • Protein Conformation
  • Receptors, Virus / immunology
  • Receptors, Virus / metabolism*
  • Sialic Acids / metabolism*


  • Antibodies
  • Antiviral Agents
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Hemagglutinins, Viral
  • Receptors, Virus
  • Sialic Acids
  • N-Acetylneuraminic Acid