Retroviral restriction factor TRIM5α is a trimer

Claudia C. Mische, Hassan Javanbakht, Byeongwoon Song, Felipe Diaz-Griffero, Matthew Stremlau, Bettina Strack, Zhihai Si, Joseph Sodroski

Research output: Contribution to journalArticle

109 Scopus citations


The retrovirus restriction factor TRIM5αa targets the viral capsid soon after entry. Here we show that the TRIM5α protein oligomerizes into trimers. The TRIM5α coiled-coil and B30.2(SPRY) domains make important contributions to the formation and/or stability of the trimers. A functionally defective TRIM5α mutant with the RING and B-box 2 domains deleted can form heterotrimers with wild-type TRIM5α, accounting for the observed dominant-negative activity of the mutant protein. Trimerization potentially allows TRIM5α to interact with threefold pseudosymmetrical structures on retroviral capsids.

Original languageEnglish (US)
Pages (from-to)14446-14450
Number of pages5
JournalJournal of virology
Issue number22
StatePublished - Nov 1 2005
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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  • Cite this

    Mische, C. C., Javanbakht, H., Song, B., Diaz-Griffero, F., Stremlau, M., Strack, B., Si, Z., & Sodroski, J. (2005). Retroviral restriction factor TRIM5α is a trimer. Journal of virology, 79(22), 14446-14450.