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Viruses 2012, 4(1), 117-139;

Molecular and Cellular Aspects of Rhabdovirus Entry

Laboratoire de Virologie Moléculaire et Structurale, Centre de Recherche de Gif, CNRS (UPR 3296), Avenue de la Terrasse, 91198, Gif sur Yvette Cedex, France
Author to whom correspondence should be addressed.
Received: 25 November 2011 / Revised: 5 January 2012 / Accepted: 10 January 2012 / Published: 18 January 2012
(This article belongs to the Special Issue Virus-Induced Membrane Fusion)
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Rhabdoviruses enter the cell via the endocytic pathway and subsequently fuse with a cellular membrane within the acidic environment of the endosome. Both receptor recognition and membrane fusion are mediated by a single transmembrane viral glycoprotein (G). Fusion is triggered 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 elucidation of the atomic structures of these two conformations for the vesicular stomatitis virus (VSV) G has revealed that it is different from the previously characterized class I and class II fusion proteins. In this review, the pre- and post-fusion VSV G structures are presented in detail demonstrating that G combines the features of the class I and class II fusion proteins. In addition to these similarities, these G structures also reveal some particularities that expand our understanding of the working of fusion machineries. Combined with data from recent studies that revealed the cellular aspects of the initial stages of rhabdovirus infection, all these data give an integrated view of the entry pathway of rhabdoviruses into their host cell. View Full-Text
Keywords: rhabdovirus; rabies virus; vesicular stomatitis virus; endocytosis; membrane fusion; glycoprotein rhabdovirus; rabies virus; vesicular stomatitis virus; endocytosis; membrane fusion; glycoprotein

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MDPI and ACS Style

Albertini, A.A.V.; Baquero, E.; Ferlin, A.; Gaudin, Y. Molecular and Cellular Aspects of Rhabdovirus Entry. Viruses 2012, 4, 117-139.

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