Requirements for capsid-binding and an effector function in TRIMCyp-mediated restriction of HIV-1
2006; Elsevier BV; Volume: 351; Issue: 2 Linguagem: Inglês
10.1016/j.virol.2006.03.023
ISSN1096-0341
AutoresFelipe Diaz‐Griffero, Nick Vandegraaff, Yuan Li, Kathleen McGee-Estrada, Matthew Stremlau, Sohanya Welikala, Zhihai Si, Alan Engelman, Joseph Sodroski,
Tópico(s)Immune Cell Function and Interaction
ResumoIn owl monkeys, a retrotransposition event replaced the gene encoding the retroviral restriction factor TRIM5α with one encoding TRIMCyp, a fusion between the RING, B-box 2 and coiled-coil domains of TRIM5 and cyclophilin A. TRIMCyp restricts human immunodeficiency virus (HIV-1) infection by a mechanism dependent on the interaction of the cyclophilin A moiety and the HIV-1 capsid protein. Here, we show that infection by retroviruses other than HIV-1 can be restricted by TRIMCyp, providing an explanation for the evolutionary retention of the TRIMCyp gene in owl monkey lineages. The TRIMCyp-mediated block to HIV-1 infection occurs before the earliest step of reverse transcription. TRIMCyp-mediated restriction involves at least two functions: (1) capsid binding, which occurs most efficiently for trimeric TRIMCyp proteins that retain the coiled-coil and cyclophilin A domains, and (2) an effector function that depends upon the B-box 2 domain.
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