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学科主题基础医学
Dissection of Influenza A Virus M1 Protein: pH-Dependent Oligomerization of N-Terminal Domain and Dimerization of C-Terminal Domain
Zhang, Ke1,2; Wang, Zhao3; Liu, Xiaoling1; Yin, Changcheng3; Basit, Zeshan1; Xia, Bin4; Liu, Wenjun1,2
刊名PLOS ONE
2012-05-24
DOI10.1371/journal.pone.0037786
7期:5
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]RNA-BINDING-PROTEIN ; MATRIX PROTEIN ; MEMBRANE ASSOCIATION ; M2 PROTEIN ; PARTICLES ; REPLICATION ; MORPHOGENESIS ; GLYCOPROTEINS ; TRANSPORT ; RIBONUCLEOPROTEINS
英文摘要

Background: The matrix 1 (M1) protein of Influenza A virus plays many critical roles throughout the virus life cycle. The oligomerization of M1 is essential for the formation of the viral matrix layer during the assembly and budding process.

Methodology/Principal Findings: In the present study, we report that M1 can oligomerize in vitro, and that the oligomerization is pH-dependent. The N-terminal domain of M1 alone exists as multiple-order oligomers at pH 7.4, and the C-terminal domain alone forms an exclusively stable dimer. As a result, intact M1 can display different forms of oligomers and dimer is the smallest oligomerization state, at neutral pH. At pH 5.0, oligomers of the N-terminal domain completely dissociate into monomers, while the C-terminal domain remains in dimeric form. As a result, oligomers of intact M1 dissociate into a stable dimer at acidic pH.

Conclusions/Significance: Oligomerization of M1 involves both the N- and C-terminal domains. The N-terminal domain determines the pH-dependent oligomerization characteristic, and C-terminal domain forms a stable dimer, which contributes to the dimerization of M1. The present study will help to unveil the mechanisms of influenza A virus assembly and uncoating process.

语种英语
WOS记录号WOS:000305338900044
项目编号2011CB504705 ; KSCX2-YW-N-054 ; KSCX2-YW-R-158 ; 30972185 ; 30901073
资助机构National Basic Research Program (973) of China ; Chinese Academy of Sciences Innovation ; National Natural Science Foundation of China
引用统计
被引频次:24[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/57349
专题北京大学基础医学院_生物物理学系
北京大学基础医学院
北京大学口腔医学院_儿童口腔科
作者单位1.Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Ctr Mol Virol, Beijing, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing, Peoples R China
3.Peking Univ, Hlth Sci Ctr, Dept Biophys, Beijing 100871, Peoples R China
4.Peking Univ, Beijing Nucl Magnet Resonance Ctr, Beijing 100871, Peoples R China
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GB/T 7714
Zhang, Ke,Wang, Zhao,Liu, Xiaoling,et al. Dissection of Influenza A Virus M1 Protein: pH-Dependent Oligomerization of N-Terminal Domain and Dimerization of C-Terminal Domain[J]. PLOS ONE,2012,7(5).
APA Zhang, Ke.,Wang, Zhao.,Liu, Xiaoling.,Yin, Changcheng.,Basit, Zeshan.,...&Liu, Wenjun.(2012).Dissection of Influenza A Virus M1 Protein: pH-Dependent Oligomerization of N-Terminal Domain and Dimerization of C-Terminal Domain.PLOS ONE,7(5).
MLA Zhang, Ke,et al."Dissection of Influenza A Virus M1 Protein: pH-Dependent Oligomerization of N-Terminal Domain and Dimerization of C-Terminal Domain".PLOS ONE 7.5(2012).
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