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    J Virol. 2005 Jun;79(12):7883-8.

    Disruption of human TRIM5alpha antiviral activity by nonhuman primate orthologues.

    Berthoux L, Sebastian S, Sayah DM, Luban J.

    Source

    Department of Microbiology, Columbia University College of Physicians and Surgeons, 701 West 168th St., New York, NY 10032, USA.

    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 (TRIM5alpha(rh)) or by the product of the owl monkey TRIM5-cyclophilin A gene fusion (TRIMCyp). Human TRIM5alpha 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 TRIM5alpha(rh) or TRIMCyp in human cells interferes with the anti-N-MLV activity of endogenous human TRIM5alpha (TRIM5alpha(hu)). Deletion of the cyclophilin domain from TRIMCyp has no effect on heteromultimerization or colocalization with TRIM5alpha(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.

    PMID:
    15919943
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC1143641
    Free PMC Article

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