The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation - PubMed (original) (raw)
The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation
S Bour et al. J Virol. 1995 Mar.
Abstract
We have recently demonstrated that coexpression of Vpu and CD4 in HeLa cells results in the degradation of CD4 in the endoplasmic reticulum. The sensitivity of CD4 to Vpu-mediated degradation is conferred by the presence of specific sequences located between amino acids 402 and 420 in the CD4 cytoplasmic domain. Using an in vitro translation system, we also showed that degradation of CD4 by Vpu requires the two proteins to be present in the same membrane compartment. Although these results suggest that spatial proximity between CD4 and Vpu may be critical in triggering degradation, it remains unknown whether the two molecules have the ability to interact with each other. In order to better define the mechanisms involved in CD4 degradation, we investigated the existence and functional relevance of direct interactions between CD4 and Vpu. Coimmunoprecipitation experiments showed that Vpu specifically binds to the cytoplasmic tail of CD4. This phenomenon is relevant to the mechanism of CD4 degradation since the ability of CD8/CD4 chimeric molecules and various CD4 mutants to form complexes with Vpu correlates with their sensitivity to degradation. Accordingly, we found that amino acid residues in the CD4 cytoplasmic tail previously shown to be important for degradation are necessary for Vpu binding. We further demonstrate that a deletion mutant of Vpu as well as a phosphorylation mutant, both biologically inactive with regard to CD4 degradation, retained the capacity to interact with the CD4 cytoplasmic domain. Taken together, these results indicate that Vpu binding is necessary to trigger CD4 degradation. However, the binding to target molecules is not sufficient per se to cause degradation. Interaction between CD4 and Vpu is thus likely to be an early event critical in triggering a multistep process leading to CD4 degradation.
Similar articles
- Putative alpha-helical structures in the human immunodeficiency virus type 1 Vpu protein and CD4 are involved in binding and degradation of the CD4 molecule.
Tiganos E, Yao XJ, Friborg J, Daniel N, Cohen EA. Tiganos E, et al. J Virol. 1997 Jun;71(6):4452-60. doi: 10.1128/JVI.71.6.4452-4460.1997. J Virol. 1997. PMID: 9151836 Free PMC article. - Human immunodeficiency virus type 1 Vpu protein induces degradation of CD4 in vitro: the cytoplasmic domain of CD4 contributes to Vpu sensitivity.
Chen MY, Maldarelli F, Karczewski MK, Willey RL, Strebel K. Chen MY, et al. J Virol. 1993 Jul;67(7):3877-84. doi: 10.1128/JVI.67.7.3877-3884.1993. J Virol. 1993. PMID: 8510209 Free PMC article. - Vpu from HIV-1 on an atomic scale: experiments and computer simulations.
Fischer WB. Fischer WB. FEBS Lett. 2003 Sep 18;552(1):39-46. doi: 10.1016/s0014-5793(03)00782-8. FEBS Lett. 2003. PMID: 12972150 Review. - The human immunodeficiency virus type 1 Vpu protein: roles in virus release and CD4 downregulation.
Jabbar MA. Jabbar MA. Curr Top Microbiol Immunol. 1995;193:107-20. doi: 10.1007/978-3-642-78929-8_6. Curr Top Microbiol Immunol. 1995. PMID: 7648871 Review. No abstract available.
Cited by
- Plasma Membrane-Associated Restriction Factors and Their Counteraction by HIV-1 Accessory Proteins.
Ramirez PW, Sharma S, Singh R, Stoneham CA, Vollbrecht T, Guatelli J. Ramirez PW, et al. Cells. 2019 Sep 2;8(9):1020. doi: 10.3390/cells8091020. Cells. 2019. PMID: 31480747 Free PMC article. Review. - Impairment of human immunodeficiency virus type 1 (HIV-1) entry into Jurkat T cells by constitutive expression of the HIV-1 vpr protein: role of CD4 down-modulation.
Conti L, Varano B, Gauzzi MC, Matarrese P, Federico M, Malorni W, Belardelli F, Gessani S. Conti L, et al. J Virol. 2000 Nov;74(21):10207-11. doi: 10.1128/jvi.74.21.10207-10211.2000. J Virol. 2000. PMID: 11024150 Free PMC article. - Ion channels as antivirus targets.
Liang X, Li ZY. Liang X, et al. Virol Sin. 2010 Aug;25(4):267-80. doi: 10.1007/s12250-010-3136-y. Epub 2010 Jul 28. Virol Sin. 2010. PMID: 20960300 Free PMC article. Review. - The vpu protein of human immunodeficiency virus type 1 plays a protective role against virus-induced apoptosis in primary CD4(+) T lymphocytes.
Komoto S, Tsuji S, Ibrahim MS, Li YG, Warachit J, Taniguchi K, Ikuta K. Komoto S, et al. J Virol. 2003 Oct;77(19):10304-13. doi: 10.1128/jvi.77.19.10304-10313.2003. J Virol. 2003. PMID: 12970415 Free PMC article. - Interaction with cellular CD4 exposes HIV-1 envelope epitopes targeted by antibody-dependent cell-mediated cytotoxicity.
Veillette M, Désormeaux A, Medjahed H, Gharsallah NE, Coutu M, Baalwa J, Guan Y, Lewis G, Ferrari G, Hahn BH, Haynes BF, Robinson JE, Kaufmann DE, Bonsignori M, Sodroski J, Finzi A. Veillette M, et al. J Virol. 2014 Mar;88(5):2633-44. doi: 10.1128/JVI.03230-13. Epub 2013 Dec 18. J Virol. 2014. PMID: 24352444 Free PMC article.
References
- Nature. 1984 Dec 20-1985 Jan 2;312(5996):767-8 - PubMed
- J Virol. 1992 Jan;66(1):226-34 - PubMed
- Cell. 1986 Nov 7;47(3):333-48 - PubMed
- Science. 1986 Nov 28;234(4780):1123-7 - PubMed
- Nature. 1988 Jan 7;331(6151):82-4 - PubMed
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials