Low pH deforms the influenza virus envelope

References

1. Adrian M., Dubochet J., Lepault J., McDowall A. W. 1984; Cryo-electron microscopy of viruses. Nature, London 308:32–37
   [Google Scholar]
2. Booy F. P., Ruigrok R. W. H., van Bruggen E. F. J. 1985; Electron microscopy of influenza virus. A comparison of negatively stained and ice-embedded particles. Journal of Molecular Biology 184:667–676
   [Google Scholar]
3. Cusack S., Ruigrok R. W. H., Krijgsman P. C. J., Mellema J. E. 1985; Structure and composition of influenza virus. A small angle neutron scattering study. Journal of Molecular Biology 186:565–582
   [Google Scholar]
4. Doms R. W., Helenius A. 1986; Quarternary structure of the influenza virus hemagglutinin after acid treatment. Journal of Virology 60:833–839
   [Google Scholar]
5. Dubochet J., Groom M., Mueller-Neuteboom S. 1982; The mounting of macromolecules for electron microscopy with particular reference to surface phenomena and the treatment of support films by glow discharge. Advances in Optical and Electron Microscopy 8:107–135
   [Google Scholar]
6. Harter C., James P., Bachi T., Semenza G., Brunner J. 1989; Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the fusion peptide. Journal of Biological Chemistry 264:6459–6464
   [Google Scholar]
7. Martin K., Helenius A. 1991; Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import. Cell 67:117–130
   [Google Scholar]
8. Ruigrok R. W. H., Hewat E. A. 1992; Comparison of negatively stained and frozen hydrated samples of influenza viruses A and B and of vesicular stomatitis virus. Micron et microscopica acta (in press)
   [Google Scholar]
9. Ruigrok R. W. H., Andree P. J., Hooft van Huysduynen R. A. M., Mellema J. E. 1984; Characterization of three highly purified influenza virus strains by electron microscopy. Journal of General Virology 65:799–802
   [Google Scholar]
10. Ruigrok R. W. H., Wrigley N. G., Calder L. J., Cusack S., Wharton S. A., Brown E. B., Skehel J. J. 1986; Electron microscopy of the low pH structure of influenza virus haemagglutinin. EMBO Journal 5:41–49
    [Google Scholar]
11. Skehel J. J., Schild G. C. 1971; The polypeptide composition of influenza A viruses. Virology 44:396–408
    [Google Scholar]
12. Skehel J. J., Bayley P. M., Brown E. B., Martin S. R., Waterfield M. D., White J. M., Wilson I. A., Wiley D. C. 1982; Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion. Proceedings of the National Academy of Sciences, U.S.A 79:968–972
    [Google Scholar]
13. Stegmann T., Hoekstra D., Scherphof G., Wilschut J. 1986; Fusion activity of influenza virus. A comparison between biological and artificial target membrane vesicles. Journal of Biological Chemistry 261:10966–10969
    [Google Scholar]
14. Stegmann T., Doms R. W., Helenius A. 1989; Protein mediated membrane fusion. Annual Review of Biophysics and Biophysical Chemistry 18:187–211
    [Google Scholar]
15. White J., Kartenbeck J., Helenius A. 1982; Membrane fusion activity of influenza virus. EMBO Journal 1:217–222
    [Google Scholar]
16. White J., Kielian M., Helenius A. 1983; Membrane fusion proteins of enveloped viruses. Quarterly Review of Biophysics 16:151–195
    [Google Scholar]
17. Wiley D. C., Skehel J. J. 1987; The structure and function of the HA membrane glycoprotein of influenza virus. Annual Review of Biochemistry 56:365–394
    [Google Scholar]
18. Wiley D. C., Wilson I. A., Skehel J. J. 1981; Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature, London 289:373–378
    [Google Scholar]
19. Wilson I. A., Skehel J. J., Wiley D. C. 1981; Structure of the haemagglutinin membrane protein of influenza virus at 3A resolution. Nature, London 289:366–373
    [Google Scholar]
20. Yoshimura A., Kuroda K., Kawasaki K., Yamishina S., Maeda T., Ohnishi S.-I. 1982; Infectious cell entry mechanism of influenza virus. Journal of Virology 43:284–293
    [Google Scholar]