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Rabies virus-induced membrane fusion.
Y Gaudin1, C Tuffereau, P Durrer
1Laboratoire de Génétique des Virus, CNRS, Gif sur Yvette, France.
Molecular Membrane Biology
|May 20, 1999
Summary
Rabies virus uses its glycoprotein G to fuse with cell membranes via endocytosis. Unlike other viruses, its fusion states maintain a pH-dependent equilibrium, crucial for understanding viral entry.
Area of Science:
- Virology
- Cell Biology
- Biochemistry
Background:
- Rabies virus, a rhabdovirus, enters host cells through receptor-mediated endocytosis.
- Viral envelope fusion with the endosomal membrane releases the nucleocapsid into the cytoplasm.
- This fusion is pH-dependent and mediated by the viral glycoprotein G.
Purpose of the Study:
- To review recent findings on rhabdovirus-induced membrane fusion.
- To highlight differences between rhabdovirus and influenza virus fusion mechanisms.
Main Methods:
- Biochemical and biophysical approaches were used.
- Analysis of glycoprotein G conformational states.
Main Results:
- Glycoprotein G exists in at least three states: native (N), activated (A), and fusion inactive (I).
- Rabies virus fusion involves pH-induced conformational changes in G.
- A pH-dependent equilibrium exists between these G states, unlike irreversible changes in other viruses.
Conclusions:
- Understanding the pH-dependent equilibrium of rabies virus glycoprotein G states is key to viral fusion.
- Differences in fusion mechanisms between rhabdoviruses and influenza virus are significant for a comprehensive understanding of viral fusion.