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学科主题: 基础医学
题名:
Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding
作者: Guu, Tom S. Y.2; Liu, Zheng3; Ye, Qiaozhen2; Mata, Douglas A.2; Li, Kunpeng1; Yin, Changcheng3; Zhang, Jingqiang1; Tao, Yizhi Jane2
关键词: capsid ; HEV
刊名: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
发表日期: 2009-08-04
DOI: 10.1073/pnas.0904848106
卷: 106, 期:31, 页:12992-12997
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Multidisciplinary Sciences
研究领域[WOS]: Science & Technology - Other Topics
关键词[WOS]: CAPSID PROTEIN ; CRYSTAL-STRUCTURE ; ANGSTROM RESOLUTION ; MUTATIONAL ANALYSIS ; ATOMIC-STRUCTURE ; ORF2 PROTEIN ; RECONSTRUCTIONS ; EXPRESSION ; SOFTWARE ; INSIGHTS
英文摘要:

Hepatitis E virus (HEV), a small, non-enveloped RNA virus in the family Hepeviridae, is associated with endemic and epidemic acute viral hepatitis in developing countries. Our 3.5-angstrom structure of a HEV-like particle (VLP) shows that each capsid protein contains 3 linear domains that form distinct structural elements: S, the continuous capsid; P1, 3-fold protrusions; and P2, 2-fold spikes. The S domain adopts a jelly-roll fold commonly observed in small RNA viruses. The P1 and P2 domains both adopt beta-barrel folds. Each domain possesses a potential polysaccharide-binding site that may function in cell-receptor binding. Sugar binding to P1 at the capsid protein interface may lead to capsid disassembly and cell entry. Structural modeling indicates that native T = 3 capsid contains flat dimers, with less curvature than those of T = 1 VLP. Our findings significantly advance the understanding of HEV molecular biology and have application to the development of vaccines and antiviral medications.

语种: 英语
项目资助者: National Institutes of Health ; National Natural Scientific Foundation of China ; Major State Basic Research Development Program of China ; Major State Science and Technology Project of China ; Welch Foundation ; Hamill Foundation ; Kresge Science Initiative Endowment Fund at Rice University
WOS记录号: WOS:000268667600077
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/56997
Appears in Collections:基础医学院_生物物理学系_期刊论文

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作者单位: 1.Rice Univ, Dept Biochem & Cell Biol, Houston, TX 77005 USA
2.Sun Yat Sen Univ, State Key Lab Biocontrol, Guangzhou 510275, Guangdong, Peoples R China
3.Peking Univ, Dept Biophys, Hlth Sci Ctr, Beijing 100191, Peoples R China

Recommended Citation:
Guu, Tom S. Y.,Liu, Zheng,Ye, Qiaozhen,et al. Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2009,106(31):12992-12997.
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