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学科主题: 基础医学
题名:
Dissection of Influenza A Virus M1 Protein: pH-Dependent Oligomerization of N-Terminal Domain and Dimerization of C-Terminal Domain
作者: Zhang, Ke1,2; Wang, Zhao3; Liu, Xiaoling1; Yin, Changcheng3; Basit, Zeshan1; Xia, Bin4; Liu, Wenjun1,2
刊名: PLOS ONE
发表日期: 2012-05-24
DOI: 10.1371/journal.pone.0037786
卷: 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
所属项目编号: 2011CB504705 ; KSCX2-YW-N-054 ; KSCX2-YW-R-158 ; 30972185 ; 30901073
项目资助者: National Basic Research Program (973) of China ; Chinese Academy of Sciences Innovation ; National Natural Science Foundation of China
WOS记录号: WOS:000305338900044
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/57349
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.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

Recommended Citation:
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).
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