Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G |
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Authors: | Roche Stéphane Bressanelli Stéphane Rey Félix A Gaudin Yves |
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Institution: | CNRS, Unité Mixte de Recherche (UMR) 2472, Institut Fédératif de Recherche (IFR) 115, Virologie Moléculaire et Structurale, 91198, Gif sur Yvette, France. |
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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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