The Structure and Receptor Binding Properties of the 1918 Influenza Hemagglutinin

Science

Volumn 303, Issue 5665, 2004, Pages 1838-1842

  Gamblin, S J ^a,d   Haire, L F ^a,d   Russell, R J ^a,d   Stevens, D J ^a   Xiao, B ^a   Ha, Y ^b,c   Vasisht, N ^a   Steinhauer, D A ^a,d   Daniels, R S ^a   Elliot, A ^a   Wiley, D C ^b   Skehel, J J ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^b HARVARD UNIVERSITY   (United States)

^c YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; DISEASES; PROTEINS; VIRUSES;

RECEPTOR BINDING; VIRUS INFECTIONS;

BIOMEDICAL ENGINEERING;

CARBOHYDRATE; GLYCOLIPID; GLYCOPROTEIN; SIALIC ACID; VIRUS HEMAGGLUTININ;

INFLUENZA; MEDICINE;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; HEMAGGLUTINATION; HUMAN; HYDROGEN BOND; INFLUENZA VIRUS; NONHUMAN; PRIORITY JOURNAL; RECEPTOR BINDING;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BIRDS; CRYSTALLOGRAPHY, X-RAY; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; HISTORY, 20TH CENTURY; HUMANS; HYDROGEN BONDING; INFLUENZA A VIRUS; INFLUENZA, HUMAN; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, VIRUS; SEQUENCE ALIGNMENT; SIALIC ACIDS; SPECIES SPECIFICITY; SWINE;

AVES; INFLUENZA VIRUS;

EID: 12144288130     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1093155     Document Type: Article

References (30)

1. J. J. Skehel, D. C. Wiley, Annu. Rev. Biochem. 69, 531 (2000).
2. M. B. Eisen, S. Sabesan, J. J. Skehel, D. C. Wiley, Virology 232, 19 (1997).
3. Y. Ha, D. J. Stevens, J. J. Skehel, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 98, 11181 (2001).
4. M. Matrosovich et al., J. Virol. 74, 8502 (2000).
5. G. N. Rogers, J. C. Paulson, Virology 127, 361 (1983).
6. G. N. Rogers et al., Nature 304, 76 (1983).
7. N. K. Sauter et al., Biochemistry 28, 8388 (1989).
8. W. Weis et al., Nature 333, 426 (1988).
9. E. Nobusawa et al., Virology 182, 475 (1991).
10. T. Ito et al., J. Virol. 72, 7367 (1998).
11. G. N. Rogers, B. L. D'Souza, Virology 173, 317 (1989).
12. L. G. Baum, J. C. Paulson, Acta Histochem. Suppl. 40, 35 (1990).
13. J. N. Couceiro, J. C. Paulson, L. G. Baum, Virus Res. 29, 155 (1993).
14. R. G. Webster, Proc. Natl. Acad. Sci. U.S.A. 96, 1164 (1999).
15. C. W. Naeve, V. S. Hinshaw, R. G. Webster, J. Virol. 51, 567 (1984).
16. R. J. Connor, Y. Kawaoka, R. G. Webster, J. C. Paulson, Virology 205, 17 (1994).
17. A. H. Reid, T. G. Fanning, J. V. Hultin, J. K. Taubenberger, Proc. Natl. Acad. Sci. U.S.A. 96, 1651 (1999).
18. T. Francis, Science 80, 457 (1936).
19. R. E. Shope, J. Exp. Med. 54, 373 (1931).
20. W. Smith, C. H. Andrewes, P. O. Laidlaw, Lancet 1, 66 (1933).
21. Y. Ha, D. J. Stevens, J. J. Skehel, D. C. Willey, EMBO J. 21, 865 (2002).
22. R. Russell et al., in preparation.
23. Y. Ha, D. J. Stevens, J. J. Skehel, D. C. Wiley, Virology 309, 209 (2003).
24. A. H. Reid et al., Emerg. Infect. Dis. 9, 1249 (2003).
25. F. L. Raymond, A. J. Caton, N. J. Cox, A. P. Kendal, G. G. Brownlee, Nucleic Acids Res. 11, 7191 (1983).
26. M. N. Matrosovich et al., Virology 196, 111 (1993).
27. A. S. Gambaryan et al., Virology 232, 345 (1997).
28. M. Matrosovich, N. Zhou, Y. Kawaoka, R. Webster, J. Virol. 73, 1146 (1999).
29. M. Bennett, V. Gregory, Y.-P. Lin, A. J. Hay, unpublished data.
30. We thank S. Smerdon and P. Walker for assistance and discussion. Diffraction data were collected at Daresbury Synchrotron Radiation Source (SRS) and European Synchrotron Radiation Facility (ESRF) Grenoble. We thank J. Nicholson (SRS) and S. McSweeney (ESRF) for rapid access to and assistance with beamtime as well as other beamline staff. This research was supported by the MRC (UK), NIH grant AI-13654, by a supplement to this grant for Expanded International Research on Emerging and Re-Emerging Diseases, by an International Partnership Research Award in Veterinary Epidemiology of the Wellcome Trust, and by the Howard Hughes Medical Institute. The coordinates for the 1918-human, 1934-human, 1934-human/human, 1934-human/avian, 1930-swine, 1930-swine/human, and 1930-swine/avian HAs have been deposited in the Protein Data Bank (accession codes 1RUZ, 1RU7, 1RVZ, 1RVX, 1RUY, 1RVT, and 1RVO).