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A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71

DOI: 10.1038/nsmb.2255 DOI Help
PMID: 22388738 PMID Help

Authors: Xiangxi Wang (Chinese Academy of Science, Beijing, China) , Wei Peng (Chinese Academy of Science, Beijing, China) , Jingshan Ren (University of Oxford) , Zhongyu Hu (National Institutes for Food and Drug Control, Beijing, China) , Jiwei Xu (Chinese Academy of Science, Beijing, China) , Zhiyong Lou (Tsinghua University, Beijing, China) , Xumei Li (Chinese Academy of Science, Beijing, China) , Weidong Yin (National Institutes for Food and Drug Control, Beijing, China) , Xinliang Shen (National Institutes for Food and Drug Control, Beijing, China) , Claudine Porta (University of Oxford) , Thomas S. Walter (University of Oxford) , Danny Axford (Diamond Light Source) , Robin Owen (Diamond Light Source) , David J. Rowlands (University of Leeds) , Junzhi Wang (National Institutes for Food and Drug Control, Beijing, China) , Dave Stuart (Diamond Light Source) , Elizabeth E. Fry (University of Oxford) , Zihe Rao (Chinese Academy of Science and Tsinghua University, Beijing, China) , Gwyndaf Evans
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Structural & Molecular Biology , VOL 19 (4) , PAGES 424 - –429

State: Published (Approved)
Published: March 2012

Open Access Open Access

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.

Journal Keywords: Capsid; Crystallography; X-Ray; Enterovirus; Human; Enterovirus; Hand; Foot; Humans; Models; Molecular; Virion

Subject Areas: Biology and Bio-materials, Medicine

Instruments: I24-Microfocus Macromolecular Crystallography

Other Facilities: Photon Factory, Japan; National Synchrotron Radiation Laboratory (NSRL), China

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