The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif

Nature Medicine

Volumn 9, Issue 11, 2003, Pages 1404-1407

  Sheehy, Ann M ^a   Gaddis, Nathan C ^b   Malim, Michael H ^a  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIRETROVIRUS AGENT; APOLIPOPROTEIN B MRNA EDITING ENZYME CATALYTIC POLYPEPTIDE LIKE 3G; PROTEASOME; UNCLASSIFIED DRUG; VIF PROTEIN; VIRUS DNA;

ARTICLE; CONTROLLED STUDY; DEAMINATION; EMBRYO; ENZYME DEGRADATION; ENZYME INACTIVATION; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; NONHUMAN; PRIORITY JOURNAL; PROGENY; PROTEIN FUNCTION; VIRION;

CYSTEINE ENDOPEPTIDASES; GENE PRODUCTS, VIF; HIV INFECTIONS; HIV-1; HUMANS; MULTIENZYME COMPLEXES; NUCLEOSIDE DEAMINASES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEINS; REPRESSOR PROTEINS; VIRUS ASSEMBLY;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1; RNA VIRUSES;

EID: 0344413641     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm945     Document Type: Article

References (25)

1. Harris, R.S. et al. DNA deamination mediates innate immunity to retroviral infection. Cell 113, 803-809 (2003).
2. Mangeat, B. et al. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424, 99-103 (2003).
3. Sheehy, A.M., Gaddis, N.C., Choi, J.D. & Malim, M.H. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418, 646-650 (2002).
4. Simon, J.H.M. & Malim, M.H. The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes. J. Virol. 70, 5297-5305 (1996).
5. Zhang, H. et al. The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424, 94-98 (2003).
6. Klarmann, G.J., Chen, X., North, T.W. & Preston, B.D. Incorporation of uracil into minus strand DNA affects the specificity of plus strand synthesis initiation during lentiviral reverse transcription. J. Biol. Chem. 278, 7902-7909 (2003).
7. Mariani, R. et al. Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 114, 21-31 (2003).
8. Hershko, A. & Ciechanover, A. The ubiquitin system. Annu. Rev. Biochem. 67, 425-479 (1998).
9. Pickart, C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533 (2001).
10. Ma, X.-Y., Sova, P., Chao, W. & Volsky, D.J. Cysteine residues in the Vif protein of human immunodeficiency virus type I are essential for viral infectivity. J. Virol. 68, 1714-1720 (1994).
11. Simon, J.H., Sheehy, A.M., Carpenter, E.A., Fouchier, R.A. & Malim, M.H. Mutational analysis of the human immunodeficiency virus type 1 Vif protein. J. Virol. 73, 2675-2681 (1999).
12. Yang, X., Gonclaves, J. & Gabuzda, D. Phosphorylation of Vif and its role in HIV-1 replication. J. Biol. Chem. 271, 10121-10129 (1996).
13. Camaur, D. & Trono, D. Characterization of human immunodeficiency virus type 1 Vif particle incorporation. J. Virol. 70, 6106-6111 (1996).
14. Fouchier, R.A.M., Simon, J.H.M., Jaffe, A.B. & Malim, M.H. Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env-encoded proteins. J. Virol. 70, 8263-8269 (1996).
15. Liu, H. et al. The Vif protein of human and simian immunodeficiency viruses is packaged into virions and associates with viral core structures. J. Virol. 69, 7630-7638 (1995).
16. Margottin, F. et al. A novel human WD protein, h-βTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol. Cell 1, 565-574 (1998).
17. Lama, J., Mangasarian, A. & Trono, D. Cell-surface expression of CD4 reduces HIV-1 infectivity by blocking Env incorporation in a Nef- and Vpu-inhibitable manner. Curr. Biol. 9, 622-631 (1999).
18. Levesque, K., Zhao, Y.S. & Cohen, E.A. Vpu exerts a positive effect on HIV-1 infectivity by down-modulating CD4 receptor molecules at the surface of HIV-1 producing cells. J. Biol. Chem. 278, 28346-28353 (2003).
19. Demirov, D.G., Ono, A., Orenstein, J.M. & Freed, E.O. Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function. Proc. Natl. Acad. Sci. USA 99, 955-960 (2002).
20. Garrus, J.E. et al. Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell 107, 55-65 (2001).
21. Martin-Serrano, J., Zang, T. & Bieniasz, P.D. Role of ESCRT-I in retroviral budding. J. Virol. 77, 4794-4804 (2003).
22. VerPlank, L. et al. Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag). Proc. Natl. Acad. Sci. USA 98, 7724-7729 (2001).
23. Ward, C.L., Omura, S. & Kopito, R.R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127 (1995).
24. Simon, J.H.M., Southerling, T.E., Peterson, J.C., Meyer, B.E. & Malim, M.H. Complementation of vif-defective human immunodeficiency virus type 1 by primate, but not nonprimate, lentivirus vifgenes. J. Virol. 69, 4166-4172 (1995).
25. Piñol-Roma, S. & Dreyfuss, G. Transcription-dependent and transcription-independent nuclear transport of hnRNP proteins. Science 253, 312-314 (1991).