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Journal of Virology, November 2005, p. 14446-14450, Vol. 79, No. 22
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.22.14446-14450.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Retroviral Restriction Factor TRIM5 Is a Trimer

Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Division of AIDS, Harvard Medical School, Boston, Massachusetts 02115,¹ Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts 02115²

Received 12 May 2005/ Accepted 26 August 2005

The retrovirus restriction factor TRIM5 targets the viral capsid soon after entry. Here we show that the TRIM5 protein oligomerizes into trimers. The TRIM5 coiled-coil and B30.2(SPRY) domains make important contributions to the formation and/or stability of the trimers. A functionally defective TRIM5 mutant with the RING and B-box 2 domains deleted can form heterotrimers with wild-type TRIM5, accounting for the observed dominant-negative activity of the mutant protein. Trimerization potentially allows TRIM5 to interact with threefold pseudosymmetrical structures on retroviral capsids.

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