Unique features of TRIM5α among closely related human TRIM family members

Xing Li, 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

Research output: Contribution to journalArticlepeer-review

60 Scopus citations


The tripartite motif (TRIM) protein, TRIM5α, 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 TRIM5α, assembled into homotrimers and co-localized in the cytoplasm with TRIM5α. TRIM5α turned over more rapidly than related TRIM proteins. TRIM5α, TRIM34 and TRIM6 associated with HIV-1 capsid-nucleocapsid complexes assembled in vitro; the TRIM5α and TRIM34 interactions with these complexes were dependent on their B30.2(SPRY) domains. Only TRIM5α potently restricted infection by the retroviruses studied; overexpression of TRIM34 resulted in modest inhibition of simian immunodeficiency virus (SIVmac) infection. In contrast to the other TRIM genes examined, TRIM5 exhibited evidence of positive selection. The unique features of TRIM5α among its TRIM relatives underscore its special status as an antiviral factor.

Original languageEnglish (US)
Pages (from-to)419-433
Number of pages15
Issue number2
StatePublished - Apr 10 2007
Externally publishedYes


  • B30.2(SPRY) domain
  • Capsid binding
  • Nonsynonymous/synonymous
  • Positive selection
  • RBCC
  • RING
  • Restriction factor
  • Retrovirus
  • Tripartite motif

ASJC Scopus subject areas

  • Virology


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