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学科主题: 基础医学
题名:
The C-Terminal alpha-Helix Domain of Apolipoprotein E Is Required for Interaction with Nonstructural Protein 5A and Assembly of Hepatitis C Virus
作者: Cun, Wei1; Jiang, Jieyun1; Luo, Guangxiang1,2
刊名: JOURNAL OF VIROLOGY
发表日期: 2010-11-01
DOI: 10.1128/JVI.01021-10
卷: 84, 期:21, 页:11532-11541
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Virology
研究领域[WOS]: Virology
关键词[WOS]: DENSITY-LIPOPROTEIN RECEPTOR ; CELL-CULTURE ; RNA REPLICATION ; NONTRANSLATED REGION ; TRANSPORT PROTEIN ; PLUS RIBAVIRIN ; CORE PROTEIN ; IN-VITRO ; SECRETION ; INFECTION
英文摘要:

We have recently demonstrated that human apolipoprotein E (apoE) is required for the infectivity and assembly of hepatitis C virus (HCV) (K.S. Chang, J. Jiang, Z. Cai, and G. Luo, J. Virol. 81:13783-13793, 2007; J. Jiang and G. Luo, J. Virol. 83:12680-12691, 2009). In the present study, we have determined the molecular basis underlying the importance of apoE in HCV assembly. Results derived from mammalian two-hybrid studies demonstrate a specific interaction between apoE and HCV nonstructural protein 5A (NS5A). The C-terminal third of apoE per se is sufficient for interaction with NS5A. Progressive deletion mutagenesis analysis identified that the C-terminal alpha-helix domain of apoE is important for NS5A binding. The N-terminal receptor-binding domain and the C-terminal 20 amino acids of apoE are dispensable for the apoE-NS5A interaction. The NS5A-binding domain of apoE was mapped to the middle of the C-terminal alpha-helix domain between amino acids 205 and 280. Likewise, deletion mutations disrupting the apoE-NS5A interaction resulted in blockade of HCV production. These findings demonstrate that the specific apoE-NS5A interaction is required for assembly of infectious HCV. Additionally, we have determined that using different major isoforms of apoE (E2, E3, and E4) made no significant difference in the apoE-NS5A interaction. Likewise, these three major isoforms of apoE are equally compatible with infectivity and assembly of infectious HCV, suggesting that apoE isoforms do not differentially modulate the infectivity and/or assembly of HCV in cell culture.

语种: 英语
所属项目编号: AI070769 ; DK079293
项目资助者: NIH
WOS记录号: WOS:000282643400057
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/68207
Appears in Collections:基础医学院_病原生物学系_期刊论文

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作者单位: 1.Univ Kentucky, Dept Microbiol Immunol & Mol Genet, Coll Med, Lexington, KY 40536 USA
2.Peking Univ, Sch Basic Med Sci, Dept Microbiol, Beijing 100871, Peoples R China

Recommended Citation:
Cun, Wei,Jiang, Jieyun,Luo, Guangxiang. The C-Terminal alpha-Helix Domain of Apolipoprotein E Is Required for Interaction with Nonstructural Protein 5A and Assembly of Hepatitis C Virus[J]. JOURNAL OF VIROLOGY,2010,84(21):11532-11541.
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