scholarly journals Human Immunodeficiency Virus (HIV)-1 Viral Protein R Suppresses Transcriptional Activity of Peroxisome Proliferator-Activated Receptor γ and Inhibits Adipocyte Differentiation: Implications for HIV-Associated Lipodystrophy

2008 ◽  
Vol 22 (2) ◽  
pp. 234-247 ◽  
Author(s):  
Shashi Shrivastav ◽  
Tomoshige Kino ◽  
Tshaka Cunningham ◽  
Takamasa Ichijo ◽  
Ulrich Schubert ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Viral Protein ◽  
Transcriptional Activity ◽  
Adipocyte Differentiation ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Viral Protein R ◽  
Immunodeficiency Virus ◽  
Hiv 1

scholarly journals Comparative Modeling of Viral Protein R (VpR) from Human Immunodeficiency Virus 1 (HIV 1)

2008 ◽  
Vol 01 (02) ◽  
pp. 073-076 ◽  
Author(s):  
Seenivasagan Renganathan ◽  
Kasimani Renganathan ◽  
Marimuthu Parthiban ◽  
Kalidoss Ramamoorthy ◽  
Shanmughavel Piramanayagam
Keyword(s):  
Human Immunodeficiency Virus ◽  
Viral Protein ◽  
Comparative Modeling ◽  
Viral Protein R ◽  
Immunodeficiency Virus ◽  
Hiv 1 ◽  
Human Immunodeficiency Virus 1

scholarly journals The Susceptibility of Primate Lentiviruses to Nucleosides and Vpx during Infection of Dendritic Cells Is Regulated by CA

2015 ◽  
Vol 89 (7) ◽  
pp. 4030-4034 ◽  
Author(s):  
Véronique Barateau ◽  
Xuan-Nhi Nguyen ◽  
Fanny Bourguillault ◽  
Grégory Berger ◽  
Stéphanie Cordeil ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Dendritic Cells ◽  
Simian Immunodeficiency Virus ◽  
Viral Protein ◽  
Immunodeficiency Virus ◽  
Protein X ◽  
Primate Lentiviruses ◽  
Species Specific ◽  
Hiv 1

The block toward human immunodeficiency virus type 1 (HIV-1) infection of dendritic cells (DCs) can be relieved by Vpx (viral protein X), which degrades sterile alpha motif-hydroxylase domain 1 (SAMHD1) or by exogenously added deoxynucleosides (dNs), lending support to the hypothesis that SAMHD1 acts by limiting deoxynucleoside triphosphates (dNTPs). This notion has, however, been questioned. We show that while dNs and Vpx increase the infectivity of HIV-1, only the latter restores the infectivity of a simian immunodeficiency virus of macaques variant, SIVMACΔVpx virus. This distinct behavior seems to map to CA, suggesting that species-specific CA interactors modulate infection of DCs.

scholarly journals Novel Human Immunodeficiency Virus (HIV) Inhibitors That Have a Dual Mode of Anti-HIV Action

2003 ◽  
Vol 47 (10) ◽  
pp. 3109-3116 ◽  
Author(s):  
Miguel Stevens ◽  
Christophe Pannecouque ◽  
Erik De Clercq ◽  
Jan Balzarini
Keyword(s):  
Human Immunodeficiency Virus ◽  
Protein Expression ◽  
Viral Protein ◽  
Green Fluorescence Protein Expression ◽  
Wide Range ◽  
Immunodeficiency Virus ◽  
Infected Cells ◽  
Anti Hiv ◽  
Hiv 1

ABSTRACT We have found that novel pyridine oxide derivatives are inhibitors of a wide range of human immunodeficiency virus (HIV) type 1 (HIV-1) and HIV-2 strains in CEM cell cultures. Some of the compounds showed inhibitory activities against recombinant HIV-1 reverse transcriptase (RT), whereas others were totally inactive against this viral protein in vitro. Partial retention of anti-HIV-1 activity against virus strains that contain a variety of mutations characteristic of those for resistance to nonnucleoside RT inhibitors and a lack of inhibitory activity against recombinant HIV-2 RT suggested that these pyridine oxide derivatives possess a mode of antiviral action independent from HIV RT inhibition. Time-of-addition experiments revealed that these pyridine oxide derivatives interact at a postintegration step in the replication cycle of HIV. Furthermore, it was shown that these compounds are active not only in acutely HIV-1-infected cells but also in chronically HIV-infected cells. A dose-dependent inhibition of virus particle release and viral protein expression was observed upon exposure to the pyridine oxide derivatives. Finally, inhibition of HIV-1 long terminal repeat-mediated green fluorescence protein expression in quantitative transactivation bioassays indicated that the additional target of action of the pyridine oxide derivatives may be located at the level of HIV gene expression.

scholarly journals Homeostatic levels of SRC-2 and SRC-3 promote early human adipogenesis

2011 ◽  
Vol 192 (1) ◽  
pp. 55-67 ◽  
Author(s):  
Sean M. Hartig ◽  
Bin He ◽  
Weiwen Long ◽  
Benjamin M. Buehrer ◽  
Michael A. Mancini
Keyword(s):  
Transcriptional Activity ◽  
Adipocyte Differentiation ◽  
Cellular Heterogeneity ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Human Adipocyte ◽  
Lipogenic Gene ◽  
Protein Levels ◽  
High Content Analysis ◽  
Early Human

The related coactivators SRC-2 and SRC-3 interact with peroxisome proliferator activated receptor γ (PPARγ) to coordinate transcriptional circuits to promote adipogenesis. To identify potential coactivator redundancy during human adipogenesis at single cell resolution, we used high content analysis to quantify links between PPARγ, SRC-2, SRC-3, and lipogenesis. Because we detected robust increases and significant cell–cell heterogeneity in PPARγ and lipogenesis, without changes in SRC-2 or SRC-3, we hypothesized that permissive coregulator levels comprise a necessary adipogenic equilibrium. We probed this equilibrium by down-regulating SRC-2 and SRC-3 while simultaneously quantifying PPARγ. Individual or joint knockdown equally inhibits lipid accumulation by preventing lipogenic gene engagement, without affecting PPARγ protein levels. Supporting dominant, pro-adipogenic roles for SRC-2 and SRC-3, SRC-1 knockdown does not affect adipogenesis. SRC-2 and SRC-3 knockdown increases the proportion of cells in a PPARγhi/lipidlo state while increasing phospho-PPARγ–S114, an inhibitor of PPARγ transcriptional activity and adipogenesis. Together, we demonstrate that SRC-2 and SRC-3 concomitantly promote human adipocyte differentiation by attenuating phospho-PPARγ–S114 and modulating PPARγ cellular heterogeneity.

scholarly journals Multifunctional viral protein R of human immunodeficiency virus-1 as a potential drug target

2014 ◽  
Vol 3 (4) ◽  
pp. 104
Author(s):  
Vivek Darapaneni
Keyword(s):  
Human Immunodeficiency Virus ◽  
Binding Sites ◽  
Viral Protein ◽  
Drug Target ◽  
Amino Acid Sequences ◽  
The Novel ◽  
Conservation Analysis ◽  
Viral Protein R ◽  
Immunodeficiency Virus ◽  
Human Immunodeficiency Virus 1

<p>The viral protein R (Vpr) plays a pivotal role in the infectious lifecycle of human immunodeficiency virus-1. The objective of this study is to find the degree of conservation of Vpr and to detect conserved binding sites, which might be used as target sites for potential anti-Vpr drugs. The conservation analysis was based on 5301 amino acid sequences identified novel conserved and highly conserved sites.  The novel conserved sites which have been identified are: Leu42, Gly43 and Val57; Arg73 and Cys76; Glu24, His33, Cys76 and Ser79.<strong> </strong>The outcome of this study provide the foundation for developing anti-Vpr drugs which have abridged potential to induce drug resistance through mutations.</p>

scholarly journals Production of Uninfectious Human Immunodeficiency Virus Type 1 Containing Viral Protein R Fused to a Single-Chain Antibody against Viral Integrase

1998 ◽  
Vol 72 (8) ◽  
pp. 6960-6964 ◽  
Author(s):  
Nobuo Okui ◽  
Noriko Kobayashi ◽  
Yoshihiro Kitamura
Keyword(s):  
Human Immunodeficiency Virus ◽  
Fusion Protein ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Viral Protein ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT A single-chain antibody (scAb) against human immunodeficiency virus type 1 (HIV-1) integrase was expressed as a fusion protein of scAb and HIV-1 viral protein R (Vpr), together with the HIV-1 genome, in human 293T cells. The expression did not affect virion production much but markedly reduced the infectivity of progeny virions. The fusion protein was found to be incorporated into the virions. The incorporation appears to account for the reduced infectivity.

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