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

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108 Scopus citations

Abstract

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
Volume79
Issue number22
DOIs
Publication statusPublished - Nov 1 2005
Externally publishedYes

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ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Cite this

Mische, C. C., Javanbakht, H., Song, B., Diaz-Griffero, F., Stremlau, M., Strack, B., ... Sodroski, J. (2005). Retroviral restriction factor TRIM5α is a trimer. Journal of virology, 79(22), 14446-14450. https://doi.org/10.1128/JVI.79.22.14446-14450.2005