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Crystal Structure of the Low-pH Form of the Vesicular Stomatitis Virus Glycoprotein G
Stéphane Roche,*Stéphane Bressanelli,*Félix A. Rey,Yves Gaudin
The vesicular stomatitis virus has an atypical membrane fusionglycoprotein (G) exhibiting a pH-dependent equilibrium betweentwo forms at the virus surface. Membrane fusion is triggeredduring the transition from the high- to low-pH form. The structureof G in its low-pH form shows the classic hairpin conformationobserved in all other fusion proteins in their postfusion conformation,in spite of a novel fold combining features of fusion proteinsfrom classes I and II. The structure provides a framework forunderstanding the reversibility of the G conformational change.Unexpectedly, G is homologous to gB of herpesviruses, whichraises important questions on viral evolution.
CNRS, Unité Mixte de Recherche (UMR) 2472, Institut Fédératif de Recherche (IFR) 115, Virologie Moléculaire et Structurale, 91198, Gif sur Yvette, France; Institut National de la Recherche Agronomique (INRA), UMR1157, Virologie Moléculaire et Structurale, 91198, Gif sur Yvette, France.
* These authors contributed equally to this work.
Present address: Département de Virologie, Institut Pasteur,25 rue du Docteur Roux, 75724 Paris cedex 15, France.
To whom correspondence should be addressed. E-mail: gaudin{at}vms.cnrs-gif.fr
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