Manipulation of the host protein acetylation network by human immunodeficiency virus type 1

被引:20
作者
Jeng, Mark Y. [1 ,2 ]
Ali, Ibraheem [1 ,2 ]
Ott, Melanie [1 ,2 ]
机构
[1] Gladstone Inst Virol & Immunol, 1650 Owens St, San Francisco, CA 94158 USA
[2] Univ Calif San Francisco, Dept Med, San Francisco, CA USA
关键词
Epigenetic regulation; latency; post-translational modification; therapeutic inhibitors; virus-host interactions; viral infection; HISTONE DEACETYLASE INHIBITOR; CD4(+) T-CELLS; NF-KAPPA-B; BET BROMODOMAIN INHIBITION; LONG TERMINAL REPEAT; ELONGATION-FACTOR B; TANDEM PHD FINGER; RNA-POLYMERASE-II; HIV-1; TAT; P-TEFB;
D O I
10.3109/10409238.2015.1061973
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
Over the past 15 years, protein acetylation has emerged as a globally important post-translational modification that fine-tunes major cellular processes in many life forms. This dynamic regulatory system is critical both for complex eukaryotic cells and for the viruses that infect them. HIV-1 accesses the host acetylation network by interacting with several key enzymes, thereby promoting infection at multiple steps during the viral life cycle. Inhibitors of host histone deacetylases and bromodomain-containing proteins are now being pursued as therapeutic strategies to enhance current antiretroviral treatment. As more acetylation-targeting compounds are reaching clinical trials, it is time to review the role of reversible protein acetylation in HIV-infected CD4(+) T cells.
引用
收藏
页码:314 / 325
页数:12
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