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J. Virol. doi:10.1128/JVI.02318-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The Human TRIM5 Restriction Factor Mediates Accelerated Uncoating of the N-tropic Murine Leukemia Virus Capsid

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

^* To whom correspondence should be addressed. Email: joseph_sodroski{at}dfci.harvard.edu.

	Abstract

The host cell factors TRIM5_hu and Fv-1 restrict N-tropic murine leukemia virus (N-MLV) infection at an early post-entry step either before or after reverse transcription, respectively. Interestingly, the identity of residue 110 of the MLV capsid determines susceptibility to both TRIM5_hu and Fv-1. In this study, we investigate the fate of the MLV capsid in cells expressing either the TRIM5_hu or Fv-1 restriction factors. The expression of TRIM5_hu, but not Fv-1, specifically promoted the premature conversion of particulate N-MLV capsids within infected cells to soluble capsid proteins. The TRIM5_hu-mediated disassembly of particulate N-MLV capsids was dependent upon residue 110 of the viral capsid. Furthermore, the deletion or disruption of TRIM5_hu domains necessary for potent N-MLV restriction completely abrogated the disappearance of particulate N-MLV capsids observed with wild-type TRIM5_hu. These results suggest that premature disassembly of the viral capsid contributes to the restriction of N-MLV infection by TRIM5_hu but not by Fv-1.

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