Molecular and cellular aspects of rhabdovirus entry

Aurélie A V Albertini1, Eduard Baquero, Anna Ferlin

  • 1Laboratoire de Virologie Moléculaire et Structurale, Centre de Recherche de Gif, CNRS (UPR 3296), Avenue de la Terrasse, 91198, Gif sur Yvette Cedex, France. alberti@vms.cnrs-gif.fr

Viruses
|February 23, 2012
PubMed

Insights

Rhabdoviruses use a unique viral glycoprotein (G) for cell entry and membrane fusion. Structural analysis reveals G combines features of known fusion classes, offering new insights into viral infection mechanisms.

Area of Science:

  • Virology
  • Structural Biology
  • Cell Biology

Background:

  • Rhabdoviruses infect cells through endocytosis, requiring membrane fusion within acidic endosomes.
  • Viral glycoprotein G mediates both receptor binding and low-pH triggered membrane fusion.

Purpose of the Study:

  • To present the atomic structures of vesicular stomatitis virus (VSV) G in its pre- and post-fusion conformations.
  • To compare VSV G structure with known viral fusion proteins (class I and II).
  • To provide an integrated view of rhabdovirus entry pathways.

Main Methods:

  • Elucidation of atomic structures of VSV G in pre- and post-fusion states.
  • Comparative analysis of VSV G structures with established viral fusion protein classes.
  • Integration of structural data with recent findings on cellular aspects of rhabdovirus infection.

Main Results:

  • VSV G exhibits a pH-dependent equilibrium between pre- and post-fusion conformations.
  • VSV G structure shares features with both class I and class II viral fusion proteins.
  • Unique structural particularities of VSV G expand understanding of viral fusion machineries.

Conclusions:

  • VSV G is an atypical fusion protein, distinct from previously characterized classes.
  • Understanding VSV G structure provides novel insights into viral membrane fusion mechanisms.
  • Integrated data offer a comprehensive view of rhabdovirus host cell entry.

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