Unique features of TRIM5alpha among closely related human TRIM family members

Virology. 2007 Apr 10;360(2):419-33. doi: 10.1016/j.virol.2006.10.035.

Xing Li ¹, Bert Gold, Colm O'hUigin, Felipe Diaz-Griffero, Byeongwoon Song, Zhihai Si, Yuan Li, Wen Yuan, Matthew Stremlau, Claudia Mische, Hassan Javanbakht, Mark Scally, Cheryl Winkler, Michael Dean, Joseph Sodroski

Affiliations

Affiliation

1 Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Division of AIDS, Harvard Medical School, Boston, MA 02115, USA.

PMID: 17156811 DOI: 10.1016/j.virol.2006.10.035

Abstract

The tripartite motif (TRIM) protein, TRIM5alpha, restricts some retroviruses, including human immunodeficiency virus (HIV-1), from infecting the cells of particular species. TRIM proteins contain RING, B-box, coiled-coil and, in some cases, B30.2(SPRY) domains. We investigated the properties of human TRIM family members closely related to TRIM5. These TRIM proteins, like TRIM5alpha, assembled into homotrimers and co-localized in the cytoplasm with TRIM5alpha. TRIM5alpha turned over more rapidly than related TRIM proteins. TRIM5alpha, TRIM34 and TRIM6 associated with HIV-1 capsid-nucleocapsid complexes assembled in vitro; the TRIM5alpha and TRIM34 interactions with these complexes were dependent on their B30.2(SPRY) domains. Only TRIM5alpha potently restricted Infection by the retroviruses studied; overexpression of TRIM34 resulted in modest inhibition of simian immunodeficiency virus (SIV(mac)) Infection. In contrast to the other TRIM genes examined, TRIM5 exhibited evidence of positive selection. The unique features of TRIM5alpha among its TRIM relatives underscore its special status as an Antiviral factor.

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