The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

vpr  -  p15

Human immunodeficiency virus 1

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of vpr

  • The HIV-1 vpr protein acts as a negative regulator of apoptosis in a human lymphoblastoid T cell line: possible implications for the pathogenesis of AIDS [1].
  • Altogether, these results suggest that low levels of the endogenous vpr protein can interfere with the physiological turnover of T lymphocytes at early stages of virus infection, thus facilitating HIV persistence and, subsequently, viral spread [1].
  • The two vpr- and vpx-related genes are found only in members of the HIV-2/SIVsm/SIVmac group, whereas primate lentiviruses from other lineages (HIV-1, SIVcpz, SIVagm, SIVmnd and SIVsyk) contain a single vpr gene [2].
  • Development of a live attenuated simian immunodeficiency virus (SIV) vaccine was undertaken in the macaque model using whole live SIV bearing multiple deletions in the nef, vpr and vpx genes [3].
  • Vpr is an auxiliary HIV-1 protein, which, unlike the other regulatory gene products, is present at high copy number in virus particles [1].

Psychiatry related information on vpr

  • Therefore, Vpr could play a critical role in the neuronal apoptosis observed postmortem in the brain of patients, often connected to a severe AIDS-related disease termed HIV-associated dementia (HAD) [4].

High impact information on vpr


Chemical compound and disease context of vpr


Biological context of vpr

  • In contrast, all the vpr-expressing clones showed an impressive protection from apoptosis independently of the inducer [1].
  • Moreover, the constitutive expression of HIV-1 vpr resulted in the upregulation of bcl-2, an oncogene endowed with antiapoptotic activities, and in the downmodulation of bax, a proapoptotic factor of the bcl-2 family [1].
  • However, elimination of the vif and vpr accessory genes together, but not individually, renders the virus incapable of causing cell death and G(2) cell cycle blockade [13].
  • We tested the effects of adCMV-vpr on cell growth of several tumor cell lines [14].
  • The Delta3 candidate vaccine strain of HIV-1 contains deletions in the viral long terminal repeat (LTR) promoter and the vpr and nef genes [15].

Anatomical context of vpr

  • We established stable transfectants of CD4+ T Jurkat cells constitutively expressing low levels of vpr [1].
  • As Bcl-2 is reported to interfere with apoptosis through the mitochondrial pathway, we examined the effect of adCMV-vpr in Bcl-2 over expressing cell lines [14].
  • Analysis of an established vpr transgenic line revealed that transgenic mice on FVB/N but not on C57BL/6 genetic background developed podocyte injury by 8 wk of age, with later glomerulosclerosis [16].
  • Interplay between HIV-1 Vpr and Sp1 modulates p21(WAF1) gene expression in human astrocytes [17].
  • Vpr has a critical role in long-term AIDS disease by inducing infection in nondividing cells such as monocytes and macrophages [18].

Associations of vpr with chemical compounds


Regulatory relationships of vpr


Other interactions of vpr

  • Consequently, efficient expression of the Vif, Vpr, Vpu, and Env proteins from these RNAs is dependent on Rev. These results exclude a mechanism whereby the sole function of Rev is simply to export RNAs from nucleus to cytoplasm [22].
  • These findings indicate that vpr and nef each can induce podocyte injury with a prominent synergistic interaction [16].
  • Depending on the genes studied, phylogenetic analysis showed that YBF30 branched either with SIVcpz-gab or between SIVcpz-gab and HIV-1 group M. The structural genes and tat, vpr, and nef of YBF30 are approximately equidistant from those of HIV-1 group M and SIVcpz-gab [23].
  • Using this approach we found that (i) Vpr-linked IN is efficiently packaged into virions independent of the Gag-Pol polyprotein, (ii) fusion proteins containing a natural RT/IN processing site are cleaved by the viral protease and (iii) only the cleaved IN protein complements IN-defective HIV-1 efficiently [24].
  • The extracellular portion of env, parts of vif and vpr, as well as most of the LTR are of subtype E origin, whereas the remainder of the genome is of subtype A origin [25].

Analytical, diagnostic and therapeutic context of vpr

  • Vpr protein expression was confirmed by Western blot analysis in adCMV-vpr infected cells [14].
  • Using a combination of dynamic light scattering, circular dichroism, and NMR spectroscopy the N terminus of Vpr is shown to be a unique domain of the molecule that behaves differently from the C-terminal domain in terms of self-association and secondary structure folding [19].
  • Intracellularly expressed Vpr induced apoptosis within terminally differentiated neurons, as demonstrated by TUNEL assays [9].
  • In contrast, the vpr sequence analysis of HIV-1 strains derived from 30 different patients, who either died of AIDS-related illnesses or have AIDS, showed neither C-terminal defects nor length polymorphism in the vpr gene [26].
  • With a goal to investigate the molecular nature of HIV-1 strains infecting this patient, we amplified the nef and vpr genes directly from the fresh uncultured peripheral blood mononuclear cells (PBMCs), and carried out co-culture studies [27].


  1. The HIV-1 vpr protein acts as a negative regulator of apoptosis in a human lymphoblastoid T cell line: possible implications for the pathogenesis of AIDS. Conti, L., Rainaldi, G., Matarrese, P., Varano, B., Rivabene, R., Columba, S., Sato, A., Belardelli, F., Malorni, W., Gessani, S. J. Exp. Med. (1998) [Pubmed]
  2. The Vpr protein from HIV-1: distinct roles along the viral life cycle. Le Rouzic, E., Benichou, S. Retrovirology (2005) [Pubmed]
  3. New prospects for the development of a vaccine against human immunodeficiency virus type 1. An overview. Girard, M., Habel, A., Chanel, C. C. R. Acad. Sci. III, Sci. Vie (1999) [Pubmed]
  4. Critical implication of the (70-96) domain of human immunodeficiency virus type 1 Vpr protein in apoptosis of primary rat cortical and striatal neurons. Sabbah, E.N., Roques, B.P. J. Neurovirol. (2005) [Pubmed]
  5. Gene transfer by lentiviral vectors is limited by nuclear translocation and rescued by HIV-1 pol sequences. Follenzi, A., Ailles, L.E., Bakovic, S., Geuna, M., Naldini, L. Nat. Genet. (2000) [Pubmed]
  6. Induction of cell differentiation by human immunodeficiency virus 1 vpr. Levy, D.N., Fernandes, L.S., Williams, W.V., Weiner, D.B. Cell (1993) [Pubmed]
  7. Live attenuated, multiply deleted simian immunodeficiency virus causes AIDS in infant and adult macaques. Baba, T.W., Liska, V., Khimani, A.H., Ray, N.B., Dailey, P.J., Penninck, D., Bronson, R., Greene, M.F., McClure, H.M., Martin, L.N., Ruprecht, R.M. Nat. Med. (1999) [Pubmed]
  8. Human immunodeficiency virus type 1 Vpr-mediated G(2) cell cycle arrest: Vpr interferes with cell cycle signaling cascades by interacting with the B subunit of serine/threonine protein phosphatase 2A. Hrimech, M., Yao, X.J., Branton, P.E., Cohen, E.A. EMBO J. (2002) [Pubmed]
  9. Lentiviral expression of HIV-1 Vpr induces apoptosis in human neurons. Patel, C.A., Mukhtar, M., Harley, S., Kulkosky, J., Pomerantz, R.J. J. Neurovirol. (2002) [Pubmed]
  10. Human immunodeficiency virus type 1 vpr gene induces phenotypic effects similar to those of the DNA alkylating agent, nitrogen mustard. Poon, B., Jowett, J.B., Stewart, S.A., Armstrong, R.W., Rishton, G.M., Chen, I.S. J. Virol. (1997) [Pubmed]
  11. Identification of ribozymes within a ribozyme library that efficiently cleave a long substrate RNA. Campbell, T.B., Cech, T.R. RNA (1995) [Pubmed]
  12. The glucocorticoid receptor type II complex is a target of the HIV-1 vpr gene product. Refaeli, Y., Levy, D.N., Weiner, D.B. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  13. The Vif and Vpr accessory proteins independently cause HIV-1-induced T cell cytopathicity and cell cycle arrest. Sakai, K., Dimas, J., Lenardo, M.J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  14. Adenovirus encoding HIV-1 Vpr activates caspase 9 and induces apoptotic cell death in both p53 positive and negative human tumor cell lines. Muthumani, K., Zhang, D., Hwang, D.S., Kudchodkar, S., Dayes, N.S., Desai, B.M., Malik, A.S., Yang, J.S., Chattergoon, M.A., Maguire, H.C., Weiner, D.B. Oncogene (2002) [Pubmed]
  15. Genetic instability of live, attenuated human immunodeficiency virus type 1 vaccine strains. Berkhout, B., Verhoef, K., van Wamel, J.L., Back, N.K. J. Virol. (1999) [Pubmed]
  16. HIV-1 Genes vpr and nef Synergistically Damage Podocytes, Leading to Glomerulosclerosis. Zuo, Y., Matsusaka, T., Zhong, J., Ma, J., Ma, L.J., Hanna, Z., Jolicoeur, P., Fogo, A.B., Ichikawa, I. J. Am. Soc. Nephrol. (2006) [Pubmed]
  17. Interplay between HIV-1 Vpr and Sp1 modulates p21(WAF1) gene expression in human astrocytes. Amini, S., Saunders, M., Kelley, K., Khalili, K., Sawaya, B.E. J. Biol. Chem. (2004) [Pubmed]
  18. NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr. Wecker, K., Roques, B.P. Eur. J. Biochem. (1999) [Pubmed]
  19. Structural characterization of the HIV-1 Vpr N terminus: evidence of cis/trans-proline isomerism. Bruns, K., Fossen, T., Wray, V., Henklein, P., Tessmer, U., Schubert, U. J. Biol. Chem. (2003) [Pubmed]
  20. Structure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solution. Engler, A., Stangler, T., Willbold, D. Eur. J. Biochem. (2002) [Pubmed]
  21. Superinfection of a defective human immunodeficiency virus type 1 provirus-carrying T cell clone with vif or vpu mutants gives cytopathic virus particles by homologous recombination. Kishi, M., Tokunaga, K., Zheng, Y.H., Bahmani, M.K., Kakinuma, M., Nonoyama, M., Lai, P.K., Ikuta, K. AIDS Res. Hum. Retroviruses (1995) [Pubmed]
  22. Rev is necessary for translation but not cytoplasmic accumulation of HIV-1 vif, vpr, and env/vpu 2 RNAs. Arrigo, S.J., Chen, I.S. Genes Dev. (1991) [Pubmed]
  23. Identification of a new human immunodeficiency virus type 1 distinct from group M and group O. Simon, F., Mauclère, P., Roques, P., Loussert-Ajaka, I., Müller-Trutwin, M.C., Saragosti, S., Georges-Courbot, M.C., Barré-Sinoussi, F., Brun-Vézinet, F. Nat. Med. (1998) [Pubmed]
  24. Complementation of integrase function in HIV-1 virions. Fletcher, T.M., Soares, M.A., McPhearson, S., Hui, H., Wiskerchen, M., Muesing, M.A., Shaw, G.M., Leavitt, A.D., Boeke, J.D., Hahn, B.H. EMBO J. (1997) [Pubmed]
  25. The heterosexual human immunodeficiency virus type 1 epidemic in Thailand is caused by an intersubtype (A/E) recombinant of African origin. Gao, F., Robertson, D.L., Morrison, S.G., Hui, H., Craig, S., Decker, J., Fultz, P.N., Girard, M., Shaw, G.M., Hahn, B.H., Sharp, P.M. J. Virol. (1996) [Pubmed]
  26. Gene defects clustered at the C-terminus of the vpr gene of HIV-1 in long-term nonprogressing mother and child pair: in vivo evolution of vpr quasispecies in blood and plasma. Wang, B., Ge, Y.C., Palasanthiran, P., Xiang, S.H., Ziegler, J., Dwyer, D.E., Randle, C., Dowton, D., Cunningham, A., Saksena, N.K. Virology (1996) [Pubmed]
  27. An HIV-1 infected long-term non-progressor (LTNP): molecular analysis of HIV-1 strains in the vpr and nef genes. Saksena, N.K., Ge, Y.C., Wang, B., Xiang, S.H., Dwyer, D.E., Randle, C., Palasanthiran, P., Ziegler, J., Cunningham, A.L. Ann. Acad. Med. Singap. (1996) [Pubmed]
WikiGenes - Universities