IR@PKUHSC  > 北京大学基础医学院  > 生物物理学系
学科主题基础医学
Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding
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
2009-08-04
DOI10.1073/pnas.0904848106
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
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 ; 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
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
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 ; 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
Cited Times:103[WOS]   [WOS Record]     [Related Records in WOS]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/56997
Collection北京大学基础医学院_生物物理学系
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
GB/T 7714
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.
APA Guu, Tom S. Y..,Liu, Zheng.,Ye, Qiaozhen.,Mata, Douglas A..,Li, Kunpeng.,...&Tao, Yizhi Jane.(2009).Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,106(31),12992-12997.
MLA Guu, Tom S. Y.,et al."Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 106.31(2009):12992-12997.
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