Abstract
The vesicular stomatitis virus has an atypical membrane fusion glycoprotein (G) exhibiting a pH-dependent equilibrium between two forms at the virus surface. Membrane fusion is triggered during the transition from the high- to low-pH form. The structure of G in its low-pH form shows the classic hairpin conformation observed in all other fusion proteins in their postfusion conformation, in spite of a novel fold combining features of fusion proteins from classes I and II. The structure provides a framework for understanding the reversibility of the G conformational change. Unexpectedly, G is homologous to gB of herpesviruses, which raises important questions on viral evolution.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Crystallization
-
Crystallography, X-Ray
-
Evolution, Molecular
-
Hydrogen-Ion Concentration
-
Membrane Glycoproteins / chemistry*
-
Membrane Glycoproteins / genetics
-
Membrane Glycoproteins / metabolism
-
Models, Molecular
-
Molecular Sequence Data
-
Mutation
-
Protein Conformation
-
Protein Folding
-
Protein Structure, Quaternary
-
Protein Structure, Secondary
-
Protein Structure, Tertiary
-
Protein Subunits / chemistry
-
Vesicular stomatitis Indiana virus / chemistry*
-
Viral Envelope Proteins / chemistry*
-
Viral Envelope Proteins / genetics
-
Viral Envelope Proteins / metabolism
-
Viral Fusion Proteins / chemistry*
-
Viral Fusion Proteins / genetics
-
Viral Fusion Proteins / metabolism
Substances
-
G protein, vesicular stomatitis virus
-
Membrane Glycoproteins
-
Protein Subunits
-
Viral Envelope Proteins
-
Viral Fusion Proteins