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	3.3 angstrom cryo-em structure of a nonenveloped virus reveals a priming mechanism for cell entry
	Zhang, Xing1; Jin, Lei1; Fang, Qin2; Hui, Wong H.3; Zhou, Z. Hong1,3
刊名	Cell
	2010-04-30
卷号	141期号:3页码:472-482
ISSN号	0092-8674
DOI	10.1016/j.cell.2010.03.041
通讯作者	Zhou, z. hong(hong.zhou@ucla.edu)
英文摘要	To achieve cell entry, many nonenveloped viruses must transform from a dormant to a primed state. in contrast to the membrane fusion mechanism of enveloped viruses (e.g., influenza virus), this membrane penetration mechanism is poorly understood. here, using single-particle cryo-electron microscopy, we report a 3.3 angstrom structure of the primed, infectious subvirion particle of aquareovirus. the density map reveals side-chain densities of all types of amino acids (except glycine), enabling construction of a full-atom model of the viral particle. our structure and biochemical results show that priming involves autocleavage of the membrane penetration protein and suggest that lys84 and glu76 may facilitate this autocleavage in a nucleophilic attack. we observe a myristoyl group, covalently linked to the n terminus of the penetration protein and embedded in a hydrophobic pocket. these results suggest a well-orchestrated process of nonenveloped virus entry involving autocleavage of the penetration protein prior to exposure of its membrane-insertion finger.
WOS关键词	GRASS CARP REOVIRUS ; CAPSID PROTEIN MU-1 ; INFECTIOUS SUBVIRION PARTICLES ; MEMBRANE-PENETRATION PROTEIN ; ELECTRON CRYOMICROSCOPY ; CRYOELECTRON MICROSCOPY ; MAMMALIAN REOVIRUSES ; PUTATIVE AUTOCLEAVAGE ; IMAGE-RECONSTRUCTION ; 3D RECONSTRUCTION
WOS研究方向	Biochemistry & Molecular Biology ; Cell Biology
WOS类目	Biochemistry & Molecular Biology ; Cell Biology
语种	英语
出版者	CELL PRESS
WOS记录号	WOS:000277180800018
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2375735
专题	武汉病毒研究所
通讯作者	Zhou, Z. Hong
作者单位	1.Univ Calif Los Angeles, Dept Microbiol Mol Genet & Immunol, Los Angeles, CA 90095 USA 2.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Hubei, Peoples R China 3.Univ Calif Los Angeles, Calif NanoSyst Inst, Los Angeles, CA 90095 USA
推荐引用方式 GB/T 7714	Zhang, Xing,Jin, Lei,Fang, Qin,et al. 3.3 angstrom cryo-em structure of a nonenveloped virus reveals a priming mechanism for cell entry[J]. Cell,2010,141(3):472-482.
APA	Zhang, Xing,Jin, Lei,Fang, Qin,Hui, Wong H.,&Zhou, Z. Hong.(2010).3.3 angstrom cryo-em structure of a nonenveloped virus reveals a priming mechanism for cell entry.Cell,141(3),472-482.
MLA	Zhang, Xing,et al."3.3 angstrom cryo-em structure of a nonenveloped virus reveals a priming mechanism for cell entry".Cell 141.3(2010):472-482.

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