This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Li, X.
Right arrow Articles by Sodroski, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Li, X.
Right arrow Articles by Sodroski, J.

 Previous Article  |  Next Article 

Journal of Virology, July 2006, p. 6198-6206, Vol. 80, No. 13
0022-538X/06/$08.00+0     doi:10.1128/JVI.00283-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Functional Replacement of the RING, B-Box 2, and Coiled-Coil Domains of Tripartite Motif 5{alpha} (TRIM5{alpha}) by Heterologous TRIM Domains

Xing Li,1 Yuan Li,1 Matthew Stremlau,1 Wen Yuan,1 Byeongwoon Song,1 Michel Perron,1 and Joseph Sodroski1,2*

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

Received 8 February 2006/ Accepted 10 April 2006

Tripartite motif 5{alpha} (TRIM5{alpha}) restricts some retroviruses, including human immunodeficiency virus type 1 (HIV-1), from infecting the cells of particular species. TRIM5{alpha} is a member of the TRIM family of proteins, which contain RING, B-box, coiled-coil (CC), and, in some cases, B30.2(SPRY) domains. Here we investigated the abilities of domains from TRIM proteins (TRIM6, TRIM34, and TRIM21) that do not restrict HIV-1 infection to substitute for the domains of rhesus monkey TRIM5{alpha} (TRIM5{alpha}rh). The RING, B-box 2, and CC domains of the paralogous TRIM6 and TRIM34 proteins functionally replaced the corresponding TRIM5{alpha}rh domains, allowing HIV-1 restriction. By contrast, similar chimeras containing the components of TRIM21, a slightly more distant relative of TRIM5, did not restrict HIV-1 infection. The TRIM21 B-box 2 domain and its flanking linker regions contributed to the functional defectiveness of these chimeras. All of the chimeric proteins formed trimers. All of the chimeras that restricted HIV-1 infection bound the assembled HIV-1 capsid complexes. These results indicate that heterologous RING, B-box 2, and CC domains from related TRIM proteins can functionally substitute for TRIM5{alpha}rh domains.

* Corresponding author. Mailing address: Dana-Farber Cancer Institute, 44 Binney Street—JFB 824, Boston, MA 02115. Phone: (617) 632-3371. Fax: (671) 632-4338. E-mail: joseph_sodroski{at}dfci.harvard.edu.

Journal of Virology, July 2006, p. 6198-6206, Vol. 80, No. 13
0022-538X/06/$08.00+0     doi:10.1128/JVI.00283-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kar, A. K., Diaz-Griffero, F., Li, Y., Li, X., Sodroski, J. (2008). Biochemical and Biophysical Characterization of a Chimeric TRIM21-TRIM5{alpha} Protein. J. Virol. 82: 11669-11681 [Abstract] [Full Text]  
  • Li, X., Sodroski, J. (2008). The TRIM5{alpha} B-Box 2 Domain Promotes Cooperative Binding to the Retroviral Capsid by Mediating Higher-Order Self-Association. J. Virol. 82: 11495-11502 [Abstract] [Full Text]  
  • Keeble, A. H., Khan, Z., Forster, A., James, L. C. (2008). TRIM21 is an IgG receptor that is structurally, thermodynamically, and kinetically conserved. Proc. Natl. Acad. Sci. USA 105: 6045-6050 [Abstract] [Full Text]  
  • Schaller, T., Hue, S., Towers, G. J. (2007). An Active TRIM5 Protein in Rabbits Indicates a Common Antiviral Ancestor for Mammalian TRIM5 Proteins. J. Virol. 81: 11713-11721 [Abstract] [Full Text]  
  • Diaz-Griffero, F., Kar, A., Perron, M., Xiang, S.-H., Javanbakht, H., Li, X., Sodroski, J. (2007). Modulation of Retroviral Restriction and Proteasome Inhibitor-Resistant Turnover by Changes in the TRIM5{alpha} B-Box 2 Domain. J. Virol. 81: 10362-10378 [Abstract] [Full Text]  
  • Newman, R. M., Hall, L., Connole, M., Chen, G.-L., Sato, S., Yuste, E., Diehl, W., Hunter, E., Kaur, A., Miller, G. M., Johnson, W. E. (2006). Balancing selection and the evolution of functional polymorphism in Old World monkey TRIM5{alpha}. Proc. Natl. Acad. Sci. USA 103: 19134-19139 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»