Cyclophillin, TRIM5, and innate immunity to HIV-1

被引:70
作者
Sokolskaja, Elena
Luban, Jeremy
机构
[1] Columbia Univ, Dept Microbiol, New York, NY 10032 USA
[2] Columbia Univ, Dept Med, New York, NY 10032 USA
[3] Inst Biomed Res, CH-6500 Bellinzona, Switzerland
关键词
D O I
10.1016/j.mib.2006.06.011
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The peptidyl-prolyl isomerase cyclophilin A (CypA) binds a proline-rich loop on the surface of HIV-1 capsid (CA). This interaction increases HIV-1 infectivity in humans but promotes an anti-HIV-1 restriction activity in non-human primates. Efforts to understand these paradoxical effects of cyclophilin, along with more targeted approaches to uncover the genetic basis for HIV-1 restriction, led to the discovery of TRIM5 (tripartite motif protein 5), a CA-specific receptor for the retroviral core. The ensuing TRIM5 publication flurry established a paradigm of innate immunity in which the protein lattice of an invading retroviral core, rather than double-stranded RNA or lipopolysaccharide, is recognized by a multimeric, cytoplasmic receptor. CypA modulates HIV-1 virion core detection by this class of innate pattern recognition molecule, apparently by inducing subtle shifts in CA conformation.
引用
收藏
页码:404 / 408
页数:5
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