2010
DOI: 10.1128/jvi.02318-09
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Identification of Dominant Negative Human Immunodeficiency Virus Type 1 Vif Mutants That Interfere with the Functional Inactivation of APOBEC3G by Virus-Encoded Vif

Abstract: APOBEC3G (A3G) is a host cytidine deaminase that serves as a potent intrinsic inhibitor of retroviral replication. A3G is packaged into human immunodeficiency virus type 1 virions and deaminates deoxycytidine to deoxyuridine on nascent minus-strand retroviral cDNA, leading to hyper-deoxyguanine-to-deoxyadenine mutations on positive-strand cDNA and inhibition of viral replication. The antiviral activity of A3G is suppressed by Vif, a lentiviral accessory protein that prevents encapsidation of A3G. In this study… Show more

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Cited by 30 publications
(38 citation statements)
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“…Thus, these two proteins were also efficiently expressed in HeLa cells. As previously observed (40,57), these Vif AALA mutants were inefficient in counteracting A3G ( Fig. 2A, lanes 4, 6, and 8, and B), confirming the importance of the PPLP motif in the A3G regulation.…”
Section: Expression Of Egfp-and Mcherry-vif Fusion Proteinssupporting
confidence: 87%
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“…Thus, these two proteins were also efficiently expressed in HeLa cells. As previously observed (40,57), these Vif AALA mutants were inefficient in counteracting A3G ( Fig. 2A, lanes 4, 6, and 8, and B), confirming the importance of the PPLP motif in the A3G regulation.…”
Section: Expression Of Egfp-and Mcherry-vif Fusion Proteinssupporting
confidence: 87%
“…Altogether, these results demonstrate that the binding of A3G to the N terminus and/or the PPLP motif of Vif affects the capacity of Vif to form oligomers. As previously mentioned, this could be explained by the partial overlap of the A3G binding site and the PPLP motif of Vif (40,41,57). Indeed, the Hck kinase significantly reduced the oligomerization of Vif (Fig.…”
Section: Besides Its Interaction With Pr55mentioning
confidence: 53%
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