Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography
Autor(es): Voss James E, Vaney Marie-Christine, Duquerroy Stéphane, Vonrhein Clemens, Girard-Blanc Christine, Crublet Elodie, Thompson Andrew, Bricogne Gérard, Rey Félix A
Resumo: Chikungunya virus (CHIKV) is an emerging mosquito-borne alphavirus that has caused widespread outbreaks of debilitating human disease in the past five years. CHIKV invasion of susceptible cells is mediated by two viral glycoproteins, E1 - E2, which carry the main antigenic determinants - form an icosahedral shell at the virion surface. Glycoprotein E2, derived from furin cleavage of the p62 precursor into E3 - E2, is responsible for receptor binding, - E1 for membrane fusion. In the context of a concerted multidisciplinary effort to underst- the biology of CHIKV, here we report the crystal structures of the precursor p62-E1 heterodimer - of the mature E3-E2-E1 glycoprotein complexes. The resulting atomic models allow the synthesis of a wealth of genetic, biochemical, immunological - electron microscopy data accumulated over the years on alphaviruses in general. This combination yields a detailed picture of the functional architecture of the 25 MDa alphavirus surface glycoprotein shell. Together with the accompanying report on the structure of the Sindbis virus E2-E1 heterodimer at acidic pH (ref. 3), this work also provides new insight into the acid-triggered conformational change on the virus particle - its inbuilt inhibition mechanism in the immature complex.
Imprenta: Nature, v. 468, n. 7324, p. 709-712, 2010
Identificador do objeto digital: 10.1038/nature09555
Descritores: Chikungunya virus - Cell ; Chikungunya virus - Molecular structure ; Chikungunya virus - Protein synthesis ; Chikungunya virus - Proteins ; Chikungunya Virus - Virus
Data de publicação: 2010
