Disease relevance of HIV2gp4

• The Vpr protein of primate lentiviruses arrests cell cycling at the G(2)/M phase through an inactivation of cyclin B-p34(cdc2) and its upstream regulator cdc25 [1].
• Vpr protein of human immunodeficiency virus type 1 forms cation-selective channels in planar lipid bilayers [2].
• The specificity of the Vpr protein for the HIV-1 virus particle makes it an attractive molecule for the development of antiviral agents targeting the events associated with virus maturation [3].
• Mutagenesis of the putative alpha-helical domain of the Vpr protein of human immunodeficiency virus type 1: effect on stability and virion incorporation [4].
• We studied the role of the HIV type 2 (HIV-2) nef and vpr genes in viral tropism [5].

Psychiatry related information on HIV2gp4

• Extracellular Vpr protein increases cellular permissiveness to human immunodeficiency virus replication and reactivates virus from latency [6].

High impact information on HIV2gp4

• Production of various domains by gene expression showed that this effect arose from within the carboxyl-terminal third of the Vpr protein and implicated the sequence HFRIGCRHSRIG, containing two H(S/F)RIG motifs [7].
• The human immunodeficiency virus (HIV) Vpr protein plays a critical role in AIDS pathogenesis, especially by allowing viral replication within nondividing cells such as mononuclear phagocytes [8].
• 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 [9].
• The HIV-1 genome contains several genes coding for auxiliary proteins, including the small Vpr protein [10].
• Vpr protein of human immunodeficiency virus type 1 binds to 14-3-3 proteins and facilitates complex formation with Cdc25C: implications for cell cycle arrest [11].

Chemical compound and disease context of HIV2gp4

• We report here the detection of a 13 kD vpr protein in sucrose gradient-purified HIV-1 [12].

Biological context of HIV2gp4

• A carboxy-terminally truncated form of the human immunodeficiency virus type 1 Vpr protein induces apoptosis via G(1) cell cycle arrest [13].
• This observation demonstrates that more than one accessory gene product can be present in the virions of this family of retroviruses and raises the possibility that the vpr protein may have a role in early part of the virus life cycle [14].
• Human immunodeficiency virus type 1 vpr protein transactivation function: mechanism and identification of domains involved [15].
• The Vpr protein encoded by human immunodeficiency virus type 1 (HIV-1) is important for growth of virus in macrophages and prevents infected cells from passing into mitosis (G2 arrest) [16].
• Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme [17].

Anatomical context of HIV2gp4

• Interaction of the human immunodeficiency virus type 1 Vpr protein with the nuclear pore complex [18].
• Here we show that purified recombinant Vpr protein, in concentrations of < 100 pg/ml to 100 ng/ml, increases wild-type HIV-1 replication in newly infected transformed cell lines via a long-lasting increase in cellular permissiveness to HIV replication [6].
• To identify the domains of Vpr that are involved nuclear localization, we transfected HeLa cells with a panel of expression vectors that encode mutant Vpr protein with deletions or substitutions within putative domains [19].
• The 14-kDa Vpr protein of human immunodeficiency virus type 1 (HIV-1) serves multiple functions in the retroviral life cycle, including the enhancement of viral replication in nondividing macrophages, the induction of G2 cell-cycle arrest in proliferating T lymphocytes, and the modulation of HIV-1-induced apoptosis [20].
• This vector delivers a functional Vpr protein to immune cells including antigen-presenting cells (APCs) [21].

Associations of HIV2gp4 with chemical compounds

• The phosphorothioate oligonucleotides, targeted to the initiating methionine of the Vpr protein, had an inhibitory effect at both 20 and 10 microM only when the size was increased from 24 to 27 bases [22].
• Thus, conservation of Vpx/Vpr protein functions in caprine cells suggests a possible role for these proteins in the virus life cycle and its ability to adapt to new hosts [23].

Analytical, diagnostic and therapeutic context of HIV2gp4

• By gel filtration analysis of highly purified Vpr protein and its mutants, we demonstrate that HIV-1 Vpr exists as an oligomer [24].
• Effects of extracellular human immunodeficiency virus type 1 vpr protein in primary rat cortical cell cultures [25].
• Western blotting analysis of subcellular fractions prepared from the cells producing wildtype vpr protein strongly suggested that the protein was membrane associated [26].
• The synthetic vpr protein was characterized by amino acid analysis, sequence analysis, RP-HPLC, and urea-SDS PAGE [27].

References