HIV-1 uncoating: connection to nuclear entry and regulation by host proteins

被引:129
作者
Ambrose, Zandrea [1 ]
Aiken, Christopher [2 ]
机构
[1] Univ Pittsburgh, Sch Med, Dept Med, Div Infect Dis, Pittsburgh, PA 15261 USA
[2] Vanderbilt Univ, Sch Med, Dept Pathol Microbiol & Immunol, Nashville, TN 37232 USA
基金
美国国家卫生研究院;
关键词
Human immunodefiency virus; HIV-1; Uncoating; Capsid; Nuclear entry; Virus-host interactions; IMMUNODEFICIENCY-VIRUS TYPE-1; CYCLOSPORINE-A-RESISTANT; N-TERMINAL DOMAIN; CYCLOPHILIN-A; REVERSE TRANSCRIPTION; CAPSID PROTEIN; TRIM5-ALPHA RESTRICTION; IN-VITRO; PREINTEGRATION COMPLEXES; CRYOELECTRON MICROSCOPY;
D O I
10.1016/j.virol.2014.02.004
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The RNA genome of human immunodeficiency virus type 1 (HIV-1) is enclosed by a capsid shell that dissociates within the cell in a multistep process known as uncoating, which influences completion of reverse transcription of the viral genome. Double-stranded viral DNA is imported into the nucleus for integration into the host genome, a hallmark of retroviral infection. Reverse transcription, nuclear entry, and integration are coordinated by a capsid uncoating process that is regulated by cellular proteins. Although uncoating is not well understood, recent studies have revealed insights into the process, particularly with respect to nuclear import pathways and protection of the viral genome from DNA sensors. Understanding uncoating will be valuable toward developing novel antiretroviral therapies for HIV-infected individuals. (C) 2014 Elsevier Inc. All rights reserved.
引用
收藏
页码:371 / 379
页数:9
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