BI-2 destabilizes HIV-1 cores during infection and Prevents Binding of CPSF6 to the HIV-1 Capsid

被引：44
|
作者：
Fricke, Thomas [1 ]
Buffone, Cindy [1 ]
Opp, Silvana [1 ]
Valle-Casuso, Jose [1 ]
Diaz-Griffero, Felipe [1 ,2 ]
机构：
[1] Albert Einstein Coll Med, Dept Microbiol & Immunol, Bronx, NY 10461 USA
[2] Albert Einstein Coll Med, New York, NY 10461 USA
来源：
RETROVIROLOGY | 2014年 / 11卷
基金：
美国国家卫生研究院;
关键词：
HIV-1; BI-2; PF74; Capsid; Stability; Uncoating; CPSF6; TRIM5-ALPHA RESTRICTION; RING DOMAIN; REPLICATION; INHIBITION; STABILIZE; ABILITY; CELLS;
D O I：
10.1186/s12977-014-0120-x
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
Background: The recently discovered small-molecule BI-2 potently blocks HIV-1 infection. BI-2 binds to the N-terminal domain of HIV-1 capsid. BI-2 utilizes the same capsid pocket used by the small molecule PF74. Although both drugs bind to the same pocket, it has been proposed that BI-2 uses a different mechanism to block HIV-1 infection when compared to PF74. Findings: This work demonstrates that BI-2 destabilizes the HIV-1 core during infection, and prevents the binding of the cellular factor CPSF6 to the HIV-1 core. Conclusions: Overall this short-form paper suggests that BI-2 is using a similar mechanism to the one used by PF74 to block HIV-1 infection.
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页数：7
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