期刊
FEBS OPEN BIO
卷 5, 期 -, 页码 283-291出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.fob.2015.04.003
关键词
HIV-1; Virus assembly; Gag cleavage; Nucleocapsid; Matrix; Membrane association
资金
- Taipei Veterans General Hospital [V100C-002, V101C-059]
- Ministry of Science and Technology, Taiwan [NSC 97-2320-B-010-002-MY3, 100-2320-B-010-015-MY3]
- Ministry of Education, Aiming for the Top University Plan
Human immunodeficiency virus type 1 nucleocapsid (NC) basic residues presumably contribute to virus assembly via RNA, which serves as a scaffold for Gag-Gag interaction during particle assembly. To determine whether NC basic residues play a role in Gag cleavage (thereby impacting virus assembly), Gag processing efficiency and virus particle production were analyzed for an HIV-1 mutant NC15A, with alanine serving as a substitute for all NC basic residues. Results indicate that NC15A significantly impaired virus maturation in addition to significantly affecting Gag membrane binding and assembly. Interestingly, removal of the matrix (MA) central globular domain ameliorated the NC15A assembly and processing defects, likely through enhancement of Gag multimerization and membrane binding capacities. (C) 2015 The Authors. Published by Elsevier B.V.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据