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

vpu  -  p16

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 vpu

 

High impact information on vpu

  • In contrast, vif and rev are closer to HIV-1 group M, and vpu is highly divergent [6].
  • When expressed in vitro, the 81-amino acid vpu protein reacted with about one-third of the serum samples from AIDS patients that were tested, indicating that the vpu open reading frame is expressed in vivo as well [7].
  • These data suggest that the vpu gene product is required for efficient virus replication and may have a role in assembly or maturation of progeny virions [7].
  • Introduction of a frame-shift mutation into the vpu open reading frame did not significantly interfere with expression of the major viral proteins in a transient expression system [7].
  • 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 [8].
 

Chemical compound and disease context of vpu

 

Biological context of vpu

  • We found that simultaneous mutations in both vpu and nef severely impaired virus replication [14].
  • Using a pathogenic variant of SHIV-4 known as SHIV(KU-1bMC33), we reported that a mutant of this virus with the majority of the vpu deleted was still capable of causing profound CD4(+) T cell loss and neuroAIDS in pig-tailed macaques (McCormick-Davis et al., 2000, Virology 272, 112-116) [15].
  • Especially, in the 5'tat/rev-vpu tree, they branched before the root of HIV-1 group M. These findings suggest that these Congolese SIVcpz genomes are mosaic, probably due to a recombinational event in the recent past, and it provides evidence for a rather recently occurring cross-species transmission between humans and chimpanzees [16].
  • Our studies have further revealed that phosphorylation of either of the two phosphoacceptor sites is not sufficient to generate a functional Vpu protein [9].
  • Taken together, these observations suggest that DeltavpuSHIV(KU-1bMC33) has a low pathogenic phenotype in macaques but that individual pig-tailed macaques can select for additional mutations within the Env and Nef which can compensate for the lack of an intact Vpu and ultimately increase its pathogenicity [15].
 

Anatomical context of vpu

 

Associations of vpu with chemical compounds

 

Regulatory relationships of vpu

  • This group contains nine bicistronic mRNAs producing Env and Vpu and three mRNAs expressing only the first exon of tat [25].
 

Other interactions of vpu

  • Vif, Vpu and Nef as a fusion protein with proteolytic cleavage sites (VVN-P) is able to induce a significant level of cellular immune responses [1].
  • Various viral proteins have been implicated in direct modulation like the regulatory proteins Tat, Nef and Vpu, but also the envelope proteins gp 120 and gp41 [26].
  • Northern and Southern blot analyses revealed no apparent deletion in the proviral DNA and mRNA prepared from these clones, except in the case of type I and II clones isolated from M10/vpu- which contained large deletions in the mRNAs for gag and gag-pol proteins [27].
 

Analytical, diagnostic and therapeutic context of vpu

References

  1. Immunogenicity of a novel DNA vaccine cassette expressing multiple human immunodeficiency virus (HIV-1) accessory genes. Ayyavoo, V., Kudchodkar, S., Ramanathan, M.P., Le, P., Muthumani, K., Megalai, N.M., Dentchev, T., Santiago-Barrios, L., Mrinalini, C., Weiner, D.B. AIDS (2000) [Pubmed]
  2. Characterization of a novel simian immunodeficiency virus (SIVmonNG1) genome sequence from a mona monkey (Cercopithecus mona). Barlow, K.L., Ajao, A.O., Clewley, J.P. J. Virol. (2003) [Pubmed]
  3. Murine retroviral vector that induces long-term expression of HIV-1 envelope protein. Fujita, K., Maldarelli, F., Purcell, D.F., Silver, J. J. Virol. Methods (1994) [Pubmed]
  4. Contribution of Vpu, Env, and Nef to CD4 down-modulation and resistance of human immunodeficiency virus type 1-infected T cells to superinfection. Wildum, S., Schindler, M., Münch, J., Kirchhoff, F. J. Virol. (2006) [Pubmed]
  5. The human immunodeficiency virus type 1 (HIV-1) Vpu protein interferes with an early step in the biosynthesis of major histocompatibility complex (MHC) class I molecules. Kerkau, T., Bacik, I., Bennink, J.R., Yewdell, J.W., Húnig, T., Schimpl, A., Schubert, U. J. Exp. Med. (1997) [Pubmed]
  6. 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]
  7. A novel gene of HIV-1, vpu, and its 16-kilodalton product. Strebel, K., Klimkait, T., Martin, M.A. Science (1988) [Pubmed]
  8. 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]
  9. Phosphorylation of both phosphoacceptor sites in the HIV-1 Vpu cytoplasmic domain is essential for Vpu-mediated ER degradation of CD4. Paul, M., Jabbar, M.A. Virology (1997) [Pubmed]
  10. Functional analysis of the phosphorylation sites on the human immunodeficiency virus type 1 Vpu protein. Friborg, J., Ladha, A., Göttlinger, H., Haseltine, W.A., Cohen, E.A. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. (1995) [Pubmed]
  11. The presence of the casein kinase II phosphorylation sites of Vpu enhances the CD4(+) T cell loss caused by the simian-human immunodeficiency virus SHIV(KU-lbMC33) in pig-tailed macaques. Singh, D.K., Griffin, D.M., Pacyniak, E., Jackson, M., Werle, M.J., Wisdom, B., Sun, F., Hout, D.R., Pinson, D.M., Gunderson, R.S., Powers, M.F., Wong, S.W., Stephens, E.B. Virology (2003) [Pubmed]
  12. The human immunodeficiency virus type 1 Vpu protein enhances membrane permeability. González, M.E., Carrasco, L. Biochemistry (1998) [Pubmed]
  13. Substitution of the transmembrane domain of Vpu in simian-human immunodeficiency virus (SHIVKU1bMC33) with that of M2 of influenza A results in a virus that is sensitive to inhibitors of the M2 ion channel and is pathogenic for pig-tailed macaques. Hout, D.R., Gomez, M.L., Pacyniak, E., Gomez, L.M., Fegley, B., Mulcahy, E.R., Hill, M.S., Culley, N., Pinson, D.M., Nothnick, W., Powers, M.F., Wong, S.W., Stephens, E.B. Virology (2006) [Pubmed]
  14. Downregulation of CD4 is required for maintenance of viral infectivity of HIV-1. Tanaka, M., Ueno, T., Nakahara, T., Sasaki, K., Ishimoto, A., Sakai, H. Virology (2003) [Pubmed]
  15. A simian human immunodeficiency virus with a nonfunctional Vpu (deltavpuSHIV(KU-1bMC33)) isolated from a macaque with neuroAIDS has selected for mutations in env and nef that contributed to its pathogenic phenotype. Singh, D.K., McCormick, C., Pacyniak, E., Lawrence, K., Dalton, S.B., Pinson, D.M., Sun, F., Berman, N.E., Calvert, M., Gunderson, R.S., Wong, S.W., Stephens, E.B. Virology (2001) [Pubmed]
  16. Natural infection of chimpanzees with new lentiviruses related to HIV-1/SIVcpz. Takehisa, J., Bikandou, B., Ido, E., Mboudjeka, I., M'Vouenze, R., Nzoukoudi, M.Y., Harada, Y., Yamaguchi-Kabata, Y., Miura, T., M'Pandi, M., Parra, H.J., M'Pelé, P., Hayami, M. J. Med. Primatol. (1999) [Pubmed]
  17. 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]
  18. A molecular clone of simian-human immunodeficiency virus (DeltavpuSHIV(KU-1bMC33)) with a truncated, non-membrane-bound vpu results in rapid CD4(+) T cell loss and neuro-AIDS in pig-tailed macaques. McCormick-Davis, C., Dalton, S.B., Hout, D.R., Singh, D.K., Berman, N.E., Yong, C., Pinson, D.M., Foresman, L., Stephens, E.B. Virology (2000) [Pubmed]
  19. Intracellular membrane traffic of human immunodeficiency virus type 1 envelope glycoproteins: vpu liberates Golgi-targeted gp160 from CD4-dependent retention in the endoplasmic reticulum. Kimura, T., Nishikawa, M., Ohyama, A. J. Biochem. (1994) [Pubmed]
  20. A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Margottin, F., Bour, S.P., Durand, H., Selig, L., Benichou, S., Richard, V., Thomas, D., Strebel, K., Benarous, R. Mol. Cell (1998) [Pubmed]
  21. Membrane interactions and alignment of structures within the HIV-1 Vpu cytoplasmic domain: effect of phosphorylation of serines 52 and 56. Henklein, P., Kinder, R., Schubert, U., Bechinger, B. FEBS Lett. (2000) [Pubmed]
  22. The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted alpha-helix-turn-alpha-helix-motif. Schubert, U., Henklein, P., Boldyreff, B., Wingender, E., Strebel, K., Porstmann, T. J. Mol. Biol. (1994) [Pubmed]
  23. Degradation of CD4 induced by human immunodeficiency virus type 1 Vpu protein: a predicted alpha-helix structure in the proximal cytoplasmic region of CD4 contributes to Vpu sensitivity. Yao, X.J., Friborg, J., Checroune, F., Gratton, S., Boisvert, F., Sékaly, R.P., Cohen, E.A. Virology (1995) [Pubmed]
  24. Changes in the host range and growth potential of an HIV-1 clone are conferred by the vpu gene. Du, B., Wolf, A., Lee, S., Terwilliger, E. Virology (1993) [Pubmed]
  25. Env and Vpu proteins of human immunodeficiency virus type 1 are produced from multiple bicistronic mRNAs. Schwartz, S., Felber, B.K., Fenyö, E.M., Pavlakis, G.N. J. Virol. (1990) [Pubmed]
  26. Modulation of cell surface protein expression by infection with HIV-1. Speth, C., Dierich, M.P. Leukemia (1999) [Pubmed]
  27. Cells surviving infection by human immunodeficiency virus type 1: vif or vpu mutants produce non-infectious or markedly less cytopathic viruses. Kishi, M., Nishino, Y., Sumiya, M., Ohki, K., Kimura, T., Goto, T., Nakai, M., Kakinuma, M., Ikuta, K. J. Gen. Virol. (1992) [Pubmed]
  28. Association of Vpu-binding protein with microtubules and Vpu-dependent redistribution of HIV-1 Gag protein. Handley, M.A., Paddock, S., Dall, A., Panganiban, A.T. Virology (2001) [Pubmed]
  29. Interaction between the cytoplasmic domains of HIV-1 Vpu and CD4: role of Vpu residues involved in CD4 interaction and in vitro CD4 degradation. Margottin, F., Benichou, S., Durand, H., Richard, V., Liu, L.X., Gomas, E., Benarous, R. Virology (1996) [Pubmed]
  30. Human-immunodeficiency-virus-type-1-encoded Vpu protein is phosphorylated by casein kinase II. Schubert, U., Schneider, T., Henklein, P., Hoffmann, K., Berthold, E., Hauser, H., Pauli, G., Porstmann, T. Eur. J. Biochem. (1992) [Pubmed]
  31. Presence of Intact vpu and nef genes in nonpathogenic SHIV is essential for acquisition of pathogenicity of this virus by serial passage in macaques. Mackay, G.A., Niu, Y., Liu, Z.Q., Mukherjee, S., Li, Z., Adany, I., Buch, S., Zhuge, W., McClure, H.M., Narayan, O., Smith, M.S. Virology (2002) [Pubmed]
 
WikiGenes - Universities