Viral protein R of HIV-1

Bukrinsky, Michael; Adzhubei, Alexei A.

doi:10.1002/(sici)1099-1654(199901/03)9:1<39::aid-rmv235>3.0.co;2-3

Cited by 75 publications

(52 citation statements)

References 80 publications

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“…However, treatment with doxycycline (Dox) for 48 h resulted in a marked increase of recombinant Vpr protein expression without any detectable change in b-actin expression in parental cells and all clones. At different time points after Dox addition, JPV clone 5, JNFV clones (3, 4, 7) and JGF clones (2,8,9) were assayed for cell viability and apoptosis signs using Hoechst 33342 and PI staining. Hoechst 33342 staining showed HIVVpr-induced apoptosis accompanied by changes in nuclear morphology, such as nuclear condensation or fragmentation in control JNFV clones at 24, 48, 72 h after Dox treatment, while JGFV clones treated with Dox expressing HIV-Vpr failed to show any morphological nuclear changes ( Fig.…”

Section: Resistance Of Gelsolin-overexpressed Jurkat T-cells Tomentioning

confidence: 99%

Gelsolin segment 5 inhibits HIV‐induced T‐cell apoptosis via Vpr‐binding to VDAC

Qiao

McMillan

2007

FEBS Letters

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Viral protein R (Vpr) from the human immunodeficiency virus induces cell cycle arrest in proliferating cells, stimulates virus transcription, and regulates activation and apoptosis of infected T-lymphocytes. We report that Jurkat cells overexpressing full-length gelsolin show resistance to Vpr-induced T-cell apoptosis with abrogation of mitochondrial membrane potential loss and the release of cytochrome c. Co-immunoprecipitation assays in HEK293T cells demonstrated that overexpression of fulllength or segment 5 (G5) but not G5-deleted gelsolin (DG5) bound to the voltage-dependent anion channel (VDAC), and that the G5 subunit can inhibit HIV-1-Vpr-binding to VDAC. We also confirmed that full-length gelsolin has the same effect in Jurkat cells. Clonogenic analysis showed that transfection of G5 but not DG5 cDNA protects Jurkat T cells from HIV-Vpr-Tet induced T-cell apoptosis and promoted cell survival, as did full-length gelsolin. These results suggest that the gelsolin G5 domain inhibits HIVVpr-induced T-cell apoptosis by blocking the interaction between Vpr and VDAC, and might be used as a protective treatment against HIV-Vpr-induced T-cell apoptosis.

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Section: Resistance Of Gelsolin-overexpressed Jurkat T-cells Tomentioning

confidence: 99%

Gelsolin segment 5 inhibits HIV‐induced T‐cell apoptosis via Vpr‐binding to VDAC

Qiao

McMillan

2007

FEBS Letters

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“…Vpr is thought to inactivate Cdc2, which is a component of maturation-promoting factor, by phosphorylating tyrosine 15 (Bukrinsky and Adzhubei, 1999;Elder et al, 2002). Recent studies have shown that Vpr-induced G2 arrest is attenuated by the introduction of wee-1 siRNA or deletion of the wee-1 gene (Yuan et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

HIV-1 Vpr induces ATM-dependent cellular signal with enhanced homologous recombination

et al. 2006

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“…Accordingly, we review the questions surrounding the biochemical mechanism of Vpr-induced cell death. Other reviews have previously described the elucidated mechanism of Vpr-regulated cell death, 3,11,12 but this review will concentrate on the puzzles and enigmas associated with this death.…”

Section: Introductionmentioning

confidence: 99%

Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism

et al. 2005

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The destruction of CD4 þ T cells and eventual induction of immunodeficiency is a hallmark of the human immunodeficiency virus type 1 infection (HIV-1). However, the mechanism of this destruction remains unresolved. Several auxiliary proteins have been proposed to play a role in this aspect of HIV pathogenesis including a 14 kDa protein named viral protein R (Vpr). Vpr has been implicated in the regulation of various cellular functions including apoptosis, cell cycle arrest, differentiation, and immune suppression. However, the mechanism(s) involved in Vprmediated apoptosis remains unresolved, and several proposed mechanisms for these effects are under investigation. In this review, we discuss the possibility that some of these proposed pathways might converge to modulate Vpr's behavior. Further, we also discuss caveats and future directions for investigation of the interesting biology of this HIV accessory gene.

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Viral protein R of HIV-1

Cited by 75 publications

References 80 publications

Gelsolin segment 5 inhibits HIV‐induced T‐cell apoptosis via Vpr‐binding to VDAC

Gelsolin segment 5 inhibits HIV‐induced T‐cell apoptosis via Vpr‐binding to VDAC

HIV-1 Vpr induces ATM-dependent cellular signal with enhanced homologous recombination

Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism

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