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Disruption of human TRIM5alpha antiviral activity by nonhuman primate orthologues.
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Disruption of human TRIM5alpha antiviral activity by nonhuman primate orthologues.

Author: L Berthoux Affiliation: Department of Microbiology, Columbia University College of Physicians and Surgeons, 701 West 168th St., New York, NY 10032, USA.; S Sebastian; DM Sayah; J Luban
Edition/Format: Article Article : English
Publication:Journal of virology, 2005 Jun; 79(12): 7883-8
Database:From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
Other Databases: British Library SerialsArticleFirst
Summary:
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  Read more...
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Document Type: Article
All Authors / Contributors: L Berthoux Affiliation: Department of Microbiology, Columbia University College of Physicians and Surgeons, 701 West 168th St., New York, NY 10032, USA.; S Sebastian; DM Sayah; J Luban
ISSN:0022-538X
Language Note: English
Unique Identifier: 112234892
Awards:

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.

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