期刊
VIROLOGY
卷 367, 期 1, 页码 19-29出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2007.04.034
关键词
cyclophilin A; HIV-1; FIV; retroviral capsid; coiled-coil domain; multimerization; restriction; TRIMS; TRIMCyp
类别
资金
- NHLBI NIH HHS [P50 HL054785, HL54785] Funding Source: Medline
- NIAID NIH HHS [AI28691, R01 AI063987, P30 AI028691, R01 AI063987-03, AI063987] Funding Source: Medline
In owl monkeys, the typical retroviral restriction factor of primates, TRIM5 alpha, is replaced by TRIMCyp. TRIMCyp consists of the TRIMS RING, B-box 2 and coiled-coil domains, as well as the intervening linker regions, fused with cyclophilin A. TRIMCyp restricts infection of retroviruses, such as human immunodeficiency virus (HIV-1) and feline immunodeficiency virus (FIV), with capsids that can bind cyclophilin A. The TRIMS coiled coil promotes the trimerization of TRIMCyp. Here we show that cyclophilin A that is oligomeric as a result of fusion with a heterologous multimer exhibits substantial antiretroviral activity. The addition of the TRIMS RING, B-box 2 and Linker 2 to oligomeric cyclophilin A generated a protein with antiretroviral activity approaching that of wild-type TRIMCyp. Multimerization increased the binding of cyclophilin A to the HIV-1 capsid, promoting accelerated uncoating of the capsid and restriction of infection. (C) 2007 Elsevier Inc. All rights reserved.
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