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Instruments / Technical Area	Publication Details	Published	Actions
I24-Microfocus Macromolecular Crystallography	A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71 Xiangxi Wang , Wei Peng , Jingshan Ren , Zhongyu Hu , Jiwei Xu , Zhiyong Lou , Xumei Li , Weidong Yin , Xinliang Shen , Claudine Porta , Thomas S. Walter , Danny Axford , Robin Owen , David J. Rowlands , Junzhi Wang , David I. Stuart , Elizabeth E. Fry , Zihe Rao , Gwyndaf Evans Nature Structural & Molecular Biology 19 (4), 424 - 429 DOI: 10.1038/nsmb.2255 PMID: 22388738 Open Access Show Abstract ▼ Abstract: Enterovirus 71 (EV71) is a major agent of hand, foot and mouth disease in children that can cause severe central nervous system disease and death. No vaccine or antiviral therapy is available. High-resolution structural analysis of the mature virus and natural empty particles shows that the mature virus is structurally similar to other enteroviruses. In contrast, the empty particles are markedly expanded and resemble elusive enterovirus-uncoating intermediates not previously characterized in atomic detail. Hydrophobic pockets in the EV71 capsid are collapsed in this expanded particle, providing a detailed explanation of the mechanism for receptor-binding triggered virus uncoating. These structures provide a model for enterovirus uncoating in which the VP1 GH loop acts as an adaptor-sensor for cellular receptor attachment, converting heterologous inputs to a generic uncoating mechanism, highlighting new opportunities for therapeutic intervention.	Mar 2012

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