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Cell Mol Life Sci. 2008 Jun;65(11):1716-28. doi: 10.1007/s00018-008-7534-3.

Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited.

Author information

1
CNRS, UMR2472, INRA, UMR1157, IFR 115, Virologie Mol├ęculaire et Structurale, Gif sur Yvette, France.

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.

PMID:
18345480
DOI:
10.1007/s00018-008-7534-3
[Indexed for MEDLINE]

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