Structure of the Low pH Conformation of Chandipura Virus G Reveals Important Features in the Evolution of the Vesiculovirus Glycoprotein

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Chandipura virus (CHAV, belonging to vesiculovirus genus), is an emerging pathogen associated with deadly encephalitis, principally among children, in India. CHAV single envelope glycoprotein G is involved in two successive steps of virus entry: receptor recognition that allows endocytosis of the virion and fusion of viral and cellular membranes that allows release of the viral nucleocapsid into the cytoplasm for the subsequent steps of infection. As for other rhabdovirus, fusion is triggered at low pH and catalyzed by a conformational change of G from its pre-fusion toward its post-fusion conformation. We have determined the crystalline structure of CHAV-G in its post-fusion conformation. An overall comparison of this structure with the previously reported post-fusion conformation of vesicular stomatitis virus G reveals the selective pressure of the humoral immune response: The major antigenic site, located in the most exposed domain of the pre-fusion conformation of the glycoprotein, is also the most structurally divergent region of G. The structure also highlights the remarkable plasticity of G in terms of local structures particularly in some hinge regions and reveals that the vesiculovirus can be classified in two groups based on the nature of their pH sensitive switches which trigger the conformational change of G.

Vyšlo v časopise: Structure of the Low pH Conformation of Chandipura Virus G Reveals Important Features in the Evolution of the Vesiculovirus Glycoprotein. PLoS Pathog 11(3): e32767. doi:10.1371/journal.ppat.1004756
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004756

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