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Disruption of Human TRIM5α Antiviral Activity by Nonhuman Primate Orthologues

By Lionel Berthoux, Sarah Sebastian, David M. Sayah and Jeremy Luban

Abstract

TRIM5 is a determinant of species-specific differences in susceptibility to infection by retroviruses bearing particular capsids. Human immunodeficiency virus type 1 (HIV-1) infection is blocked by the alpha isoform of macaque TRIM5 (TRIM5α(rh)) or by the product of the owl monkey TRIM5-cyclophilin A gene fusion (TRIMCyp). Human TRIM5α potently restricts specific strains of murine leukemia virus (N-MLV) but has only a modest effect on HIV-1. The amino termini of TRIM5 orthologues are highly conserved and possess a coiled-coil domain that promotes homomultimerization. Here we show that heterologous expression of TRIM5α(rh) or TRIMCyp in human cells interferes with the anti-N-MLV activity of endogenous human TRIM5α (TRIM5α(hu)). Deletion of the cyclophilin domain from TRIMCyp has no effect on heteromultimerization or colocalization with TRIM5α(hu) but prevents interference with anti-N-MLV activity. These data demonstrate that TRIM5 orthologues form heteromultimers and indicate that C-terminal extensions alter virus recognition by multimers of these proteins

Topics: Cellular Response to Infection
Publisher: American Society for Microbiology
Year: 2005
DOI identifier: 10.1128/JVI.79.12.7883-7888.2005
OAI identifier: oai:pubmedcentral.nih.gov:1143641
Provided by: PubMed Central
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