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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{alpha} Is a Trimer

Claudia C. Mische,1 Hassan Javanbakht,1 Byeongwoon Song,1 Felipe Diaz-Griffero,1 Matthew Stremlau,1 Bettina Strack,1 Zhihai Si,1 and Joseph Sodroski1,2*

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

* Corresponding author. Mailing address: Dana-Farber Cancer Institute, 44 Binney Street, JFB 824, Boston, MA 02115. Phone: (617) 632-3371. Fax: (617) 632-4338. E-mail: joseph_sodroski{at}dfci.harvard.edu.

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.



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