Research Article

Crystal Structure of the Low-pH Form of the Vesicular Stomatitis Virus Glycoprotein G

Science  14 Jul 2006:
Vol. 313, Issue 5784, pp. 187-191
DOI: 10.1126/science.1127683

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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.

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