Recruitment of the nuclear form of uracil DNA glycosylase into virus particles 1 participates in the full infectivity of HIV - 1
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چکیده
*Corresponding authors: 14 Serge Benichou 15 Institut Cochin, 27 Rue du Faubourg Saint-Jacques, 75014 Paris, France 16 Phone: (33) 1 40 51 65 78; Fax: (33) 1 40 51 65 70 17 E-mail:[email protected] 18 19 Louis M. Mansky 20 Institute for Molecular Virology, University of Minnesota, 18-242 Moos Tower, 515 Delaware 21 St. SE, Minneapolis, MN 55455 USA 22 Phone: 612-626-5525; Fax: 612-626-5515 23 E-mail: [email protected] 24 25 Copyright © 2011, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved. J. Virol. doi:10.1128/JVI.05163-11 JVI Accepts, published online ahead of print on 14 December 2011
منابع مشابه
Recruitment of the nuclear form of uracil DNA glycosylase into virus particles participates in the full infectivity of HIV-1.
The HIV-1 Vpr protein participates in the early steps of the virus life cycle by influencing the accuracy of reverse transcription. This role of Vpr was related to the recruitment of the nuclear form of the uracil DNA glycosylase (UNG2) enzyme into virus particles, but several conflicting findings have been reported regarding the role of UNG2 encapsidation on viral infectivity. Here, we report ...
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Human immunodeficiency virus type 1 is able to infect nondividing cells, such as macrophages, and the viral Vpr protein has been shown to participate in this process. Here, we investigated the impact of the recruitment into virus particles of the nuclear form of uracil DNA glycosylase (UNG2), a cellular DNA repair enzyme, on the virus mutation rate and on replication in macrophages. We demonstr...
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The Vpr protein, encoded by the human immunodeficiency virus type 1 (HIV-1) genome, is one of the nonstructural proteins packaged in large amounts into viral particles. We have previously reported that Vpr associates with the DNA repair enzyme uracil DNA glycosylase (UDG). In this study, we extended these observations by investigating whether UDG is incorporated into virions and whether this in...
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The human immunodeficiency virus type 1 (HIV-1) Vpr protein binds to the cellular uracil-DNA glycosylase UNG2 and induces its degradation through the assembly with the DDB1-CUL4 ubiquitin ligase complex. This interaction counteracts the antiviral activity exerted by UNG2 on HIV-1 gene transcription, as previously reported by us. In this work, we show that Vpr expression in the context of HIV-1 ...
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