Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography
Top Cited Papers
- 1 December 2010
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 468 (7324) , 709-712
- https://doi.org/10.1038/nature09555
Abstract
The E1 and E2 glycoproteins of alphaviruses form heterodimers and assemble into spikes on the virus surface, which mediate receptor binding and endocytosis. When the virion encounters acidic pH in the endosome E1 and E2 dissociate and E1 triggers fusion with the endosomal membrane. Two papers now provide the first crystal structures for glycoprotein complexes incorporating E2 at acidic and neutral pH, respectively. Together they provide insight into how fusion activation is controlled in alphaviruses.Keywords
This publication has 54 references indexed in Scilit:
- Structural changes of envelope proteins during alphavirus fusionNature, 2010
- A virus-like particle vaccine for epidemic Chikungunya virus protects nonhuman primates against infectionNature Medicine, 2010
- Integration, scaling, space-group assignment and post-refinementActa Crystallographica Section D-Biological Crystallography, 2010
- TheBuccaneersoftware for automated model building. 1. Tracing protein chainsActa Crystallographica Section D-Biological Crystallography, 2006
- Virus membrane-fusion proteins: more than one way to make a hairpinNature Reviews Microbiology, 2006
- Scaling and assessment of data qualityActa Crystallographica Section D-Biological Crystallography, 2005
- Conformational change and protein–protein interactions of the fusion protein of Semliki Forest virusNature, 2004
- The Fusion Glycoprotein Shell of Semliki Forest VirusCell, 2001
- The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolutionNature, 1995
- An epidemic of virus disease in Southern Province, Tanganyika territory, in 1952–1953Transactions of the Royal Society of Tropical Medicine and Hygiene, 1955