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Cellular and Molecular Life Sciences

, Volume 65, Issue 11, pp 1716–1728 | Cite as

Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited

  • S. Roche
  • A. A. V. Albertini
  • J. Lepault
  • S. Bressanelli
  • Y. GaudinEmail author
Open Access
Review

Abstract.

Glycoprotein G of the vesicular stomatitis virus (VSV) is involved in receptor recognition at the host cell surface and then, after endocytosis of the virion, triggers membrane fusion via a low pH-induced structural rearrangement. G is an atypical fusion protein, as there is a pH-dependent equilibrium between its pre- and post-fusion conformations. The atomic structures of these two conformations reveal that it is homologous to glycoprotein gB of herpesviruses and that it combines features of the previously characterized class I and class II fusion proteins. Comparison of the structures of G pre- and postfusion states shows a dramatic reorganization of the molecule that is reminiscent of that of paramyxovirus fusion protein F. It also allows identification of conserved key residues that constitute pH-sensitive molecular switches. Besides the similarities with other viral fusion machineries, the fusion properties and structures of G also reveal some striking particularities that invite us to reconsider a few dogmas concerning fusion proteins.

Keywords.

Vesicular stomatitis virus rhabdovirus paramyxovirus glycoprotein membrane fusion viral entry conformational change 

Copyright information

© Birkhaueser 2008

Authors and Affiliations

  • S. Roche
    • 1
    • 2
  • A. A. V. Albertini
    • 1
  • J. Lepault
    • 1
  • S. Bressanelli
    • 1
  • Y. Gaudin
    • 1
    Email author
  1. 1.CNRS, UMR2472, INRA, UMR1157, IFR 115Gif sur YvetteFrance
  2. 2.Max Planck Institute of BiochemistryMartinsriedGermany

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