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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References
Gottschalk, A. in The Viruses Vol. 3 (eds Burnet, F. M. & Stanley, W. M.) 51–61 (Academic, New York, 1959).
Paulson, J. C. in The Receptors Vol. 2 (ed. Conn, P. M.) 131–219 (Academic, Orlando, 1985).
Paulson, J. C., Sadler, J. E. & Hill, R. L. J. biol. Chem. 254, 2120–2124 (1979).
Bergelson, L. D. et al. Eur. J. Biochem. 128, 467–474 (1982).
Suzuki, Y., Matsunaga, M. & Masumoto, M. J. biol. Chem. 260, 1362–1365 (1985).
Rogers, G. N. et al. Nature 304, 76–79 (1983).
Burley, S. K. & Petsko, G. A. Science 229, 23–28 (1985).
Quiocho, F. A. A. Rev. Biochem. 55, 287–315 (1986).
O'Connell, A. M. Acta crystallogr. B29, 2320–2328 (1973).
Richards, F. M. A. Rev. Biophys. Bioengng 6, 151–176 (1977).
Quiocho, F. A. in Current Topics in Microbiology and Immunology (in the press).
Quiocho, F. A., Sack, J. S. & Vyas, N. K. Nature 329, 561–564 (1987).
Wright, C. S. J. molec. Biol. 178, 91–104 (1984).
Kronis, K. A. & Carver, J. P. Biochemistry 24, 826–833 (1985).
Kelly, J. A., Sielecki, A. R., Sykes, B. D., James, M. N. G. & Phillips, D. C. Nature 282, 875–878 (1979).
Rogers, G. N. & Paulson, J. C. Virology 127, 361–373 (1983).
Pritchett, T. J., Brossmer, R., Rose, U. & Paulson, J. C. Virology, 160, 502–506 (1987).
Yewdell, J. W., Caton, A. J. & Gerhard, W. J. Virol. 57, 623–628 (1986).
Underwood, P. A. Arch. Virol. 84, 53–61 (1985).
Underwood, P. A., Skehel, J. J. & Wiley, D. C. J. Virol. 61, 206–208 (1987).
Daniels, R. S. et al. EMBO J. 6, 1459–1465 (1987).
Higa, H. H., Rogers, G. N. & Paulson, J. C. Virology 144, 279–282 (1985).
Anders, E. M., Scalzo, A. A., Rogers, G. N. & White, D. O. J. Virol. 60, 476–482 (1986).
Pritchett, T. J. thesis, Univ. of Calif., Los Angeles (1987).
Amit, A. G., Mariuzza, R. A., Phillips, S. E. V. & Poljak, R. J. Science 233, 747–753 (1986).
Colman, P. M. et al. Nature 326, 358–363 (1987).
Sheriff, S. et al. Proc. natn. Acad. Sci. U.S.A. 84, 8075–8079 (1987).
Mandel, B. Comprehensive Virology 15, 37–121 (eds Fraenkel-Conrat, H. & Wagner, R. R.) (Plenum, New York, 1979).
Dimmock, N. J. J. gen. Virol. 65, 1015–1022 (1984).
Dimmock, N. J. Trends biochem. Sci. 12, 70–75 (1987).
Naeve, C. W., Hinshaw, V. S. & Webster, R. G. J. Virol. 51, 567–569 (1984).
Laver, W. G. & Webster, R. G. Virology 51, 383–391 (1973).
Fang, R., Minjou, W., Huylebroeck, D., Devos, R. & Fiers, W. Cell 25, 315–323 (1981).
Ward, C. W. & Dopheide, T. A. Biochem. J. 195, 337–340 (1981).
Daniels, R. S., Skehel, J. J. & Wiley, D. C. J. gen. Virol. 66, 457–464 (1985).
Rogers, G. N. et al. J. biol. Chem. 260, 7362–7367 (1985).
Wilson, I. A., Skehel, J. J. & Wiley, D. C. Nature 289, 366–373 (1981).
Warren, L. J. biol. Chem. 234, 1971–1975 (1959).
Crawford, J. L. Ph. D. thesis, Harvard University (1977).
Kahn, R. et al. J. appl. Cryst. 15, 330–337 (1982).
Winkler, F. K., Schutt, C. E. & Harrison, S. C. Acta crystallogr. A35, 901–911 (1979).
Hendrikson, W. A. & Konnert, J. H. in Biomolecular Structure, Function, Conformation and Evolution (ed. Srinivasan, R.), Vol. 1, 43–57 (Pergamon, Oxford, 1981).
Skehel, J. J. et al. Proc. natn. Acad. Sci. U.S.A. 81, 1779–1783 (1984).
Colman, P. M., Varghese, J. N. & Laver, W. G. Nature 303, 41–44 (1983).
Wiley, D. C., Wilson, I. A. & Skehel, J. J. Nature 289, 373–378 (1981).
Rossmann, M. G. et al. Nature 317, 145–153 (1985).
Flippen, J. L. Acta crystallogr. B29, 1881–1886 (1973).
Bricogne, G. Acta crystallogr. A32, 832–847 (1976).
Weis, W. thesis, Harvard Univ. (1987).
Knossow, M. et al. Acta crystallogr. B42, 627–632 (1986).
Lesk, A. M. & Hardman, K. D. Science 216, 539–540 (1982).
Knossow, M., Daniels, R. S., Douglas, A. R., Skehel, J. J. & Wiley, D. C. Nature 311, 678–680 (1984).
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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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DOI: https://doi.org/10.1038/333426a0
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