Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography

James E. Voss, Marie-Christine Vaney, Stéphane Duquerroy, Clemens Vonrhein, Christine Girard-Blanc, Elodie Crublet, Andrew Thompson, Gérard Bricogne and Félix A. Rey ()
Additional contact information
James E. Voss: Institut Pasteur, Unité de Virologie Structurale, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
Marie-Christine Vaney: Institut Pasteur, Unité de Virologie Structurale, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
Stéphane Duquerroy: Institut Pasteur, Unité de Virologie Structurale, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
Clemens Vonrhein: Global Phasing Ltd, Sheraton House, Castle Park
Christine Girard-Blanc: Institut Pasteur, Plateforme de Production de protéines recombinantes, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
Elodie Crublet: Institut Pasteur, Plateforme de Production de protéines recombinantes, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
Andrew Thompson: Synchrotron SOLEIL, L’Orme de Merisiers, BP 48 St Aubin, 91192 Gif sur Yvette, France
Gérard Bricogne: Global Phasing Ltd, Sheraton House, Castle Park
Félix A. Rey: Institut Pasteur, Unité de Virologie Structurale, 25 rue du Dr Roux, 75724 Paris Cedex 15, France

Nature, 2010, vol. 468, issue 7324, 709-712

Abstract: The pH-sensitive mechanism that gets alphaviruses into host cells Alphaviruses are significant animal and human pathogens — as demonstrated in recent outbreaks of infection with the mosquito-borne Chikungunya virus in India and southeast Asia. The E1 and E2 glycoproteins of alphaviruses are central to the way the virus infects host cells. The E1/E2 heterodimers that form spikes on the virus surface dissociate in the acidic conditions found in the internal vesicles of host cells, and E1 triggers infection by fusing with the endosomal membrane. Félix Rey and colleagues present the structure of Chikungunya virus envelope glycoprotein at neutral pH, and Michael Rossmann and colleagues reveal the structure of the envelope proteins of Sindbis virus at low pH. Sindbis virus can cause fever in humans and is the most extensively studied alphavirus. Comparison of the two structures provides insight into how fusion activation is controlled and points to possible vaccine targets.

Date: 2010
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DOI: 10.1038/nature09555

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