The capsid protein of human immunodeficiency virus: interactions of HIV-1 capsid with host protein factors

被引：30

作者：

Mascarenhas, Anjali P. ^{[1
]}

Musier-Forsyth, Karin ^{[1
,2
]}

机构：

[1] Ohio State Univ, Dept Chem, Columbus, OH 43210 USA

[2] Ohio State Univ, Dept Biochem, Columbus, OH 43210 USA

来源：

FEBS JOURNAL | 2009年 / 276卷 / 21期

基金：

美国国家卫生研究院;

关键词：

cyclophilin A; cyclophilins; Gag; HIV-1; capsid; Lysyl-tRNA synthetase; TRIM proteins; TRIM alpha; tRNA primer packaging; viral assembly; TRANSFER-RNA SYNTHETASE; HUMAN CYCLOPHILIN-A; C-TERMINAL DOMAIN; RESTRICTION FACTOR TRIM5-ALPHA; MURINE LEUKEMIA-VIRUS; RETROVIRAL RESTRICTION; CRYSTAL-STRUCTURE; TRNA(LYS) INCORPORATION; REVERSE TRANSCRIPTION; B30.2(SPRY) DOMAIN;

D O I：

10.1111/j.1742-4658.2009.07315.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

HIV-1 is a retrovirus that causes AIDS in humans. The RNA genome of the virus encodes a Gag polyprotein, which is further processed into matrix, capsid and nucleocapsid proteins. These proteins play a significant role at several steps in the viral life cycle. In addition, various stages of assembly, infection and replication of the virus involve necessary interactions with a large number of supplementary proteins/cofactors within the infected host cell. This minireview focuses on the proteomics of the capsid protein, its influence on the packaging of nonviral molecules into HIV-1 virions and the subsequent role of the molecules themselves. These interactions and their characterization present novel frontiers for the design and advancement of antiviral therapeutics.

引用

页码：6118 / 6127

页数：10

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