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

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Abstract

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.

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Author information

Author notes

  1. S. Cusack

    Present address: EMBL, c/o I.L.L., 156x, 38042, Grenoble Cedex, France

  2. W. Weis

    Present address: Department of Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University, 260 Whitney Avenue, New Haven, Connecticut, 06511, USA

  3. D. C. Wiley: To whom correspondence should be addressed.

Authors and Affiliations

  1. Depaortment of Biochemistry and Molecular Biology and Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts, 02138, USA

    W. Weis, J. H. Brown, S. Cusack & D. C. Wiley

  2. Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, California, 90024, USA

    J. C. Paulson

  3. National Institute for Medical Research, Mill Hill, London, NW7 1AA, UK

    J. J. Skehel

  4. EMBL, c/o I.L.L., 156x, 38042, Grenoble Cedex, France

    W. Weis

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  1. W. Weis
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  5. J. J. Skehel
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Weis, W., Brown, J., Cusack, S. et al. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333, 426–431 (1988). https://doi.org/10.1038/333426a0

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