The prospect of APOBEC3G for the future of HIV therapy

HIV Therapy

Volumn 3, Issue 1, 2009, Pages 7-10

  Prochnow, Courtney ^a   Bransteitter, Ronda ^a   Goodman, Myron F ^a   Chen, Xiaojiang S ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; RN 18; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIF PROTEIN;

ACQUIRED IMMUNE DEFICIENCY SYNDROME; ANTIVIRAL ACTIVITY; ANTIVIRAL THERAPY; DRUG DESIGN; DRUG PROTEIN BINDING; DRUG SAFETY; DRUG TARGETING; EDITORIAL; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1 INFECTION; INFECTION PREVENTION; PROTEIN PROTEIN INTERACTION; PROTEIN RNA BINDING; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; VIRUS INACTIVATION; VIRUS MUTATION; VIRUS REPLICATION; VIRUS RESISTANCE;

EID: 67149120661     PISSN: 17584310     EISSN: None     Source Type: Journal    
DOI: 10.2217/17584310.3.1.7     Document Type: Editorial

References (26)

1. Chen TK, Aldrovandi GM: Review of HIV antiretroviral drug resistance. Pediatr. Infect. Dis. J. 27(8), 749-752 (2008).
2. Sheehy AM, Gaddis NC, Choi JD, Malim MH: Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418(6898), 646-650 (2002).
3. Sheehy AM, Gaddis NC, Malim MH: The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat. Med. 9(11), 1404-1407 (2003).
4. Yu Y, Xiao Z, Ehrlich ES, Yu X, Yu XF: Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev. 18(23), 2867-2872 (2004).
5. Mariani R, Chen D, Schrofelbauer B et al.: Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 114(1), 21-31 (2003).
6. Stopak K, de Noronha C, Yonemoto W, Greene WC: HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol. Cell. 12(3), 591-601 (2003).
7. Zhang H, Yang B, Pomerantz RJ, Zhang C, Arunachalam SC, Gao L: The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424(6944), 94-98 (2003).
8. Li XY, Guo F, Zhang L, Kleiman L, Cen S: APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription. J. Biol. Chem. 282(44), 32065-32074 (2007).
9. Guo F, Cen S, Niu M, Yang Y, Gorelick RJ, Kleiman L: The interaction of APOBEC3G with human immunodeficiency virus type 1 nucleocapsid inhibits tRNA3Lys annealing to viral RNA. J. Virol. 81(20), 11322-11331 (2007).
10. Luo K, Wang T, Liu B et al.: Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation. J. Virol. 81(13), 7238-7248 (2007).
11. Mbisa JL, Barr R, Thomas JA et al.: Human immunodeficiency virus type 1 cDNAs produced in the presence of APOBEC3G exhibit defects in plus-strand DNA transfer and integration. J. Virol. 81(13), 7099-7110 (2007).
12. Goila-Gaur R, Strebel K: HIV-1 Vif, APOBEC, and intrinsic immunity. Retrovirology 5, 51 (2008).
13. Prochnow C, Bransteitter R, Klein MG, Goodman MF, Chen XS: The APOBEC-2 crystal structure and functional implications for the deaminase AID. Nature 445(7126), 447-451 (2007).
14. Holden LG, Prochnow C, Chang YP et al.: Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications. Nature 456(7218), 121-124 (2008).
15. Chen KM, Harjes E, Gross PJ et al.: Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. Nature 452(7183), 116-119 (2008).
16. Zhang KL, Mangeat B, Ortiz M et al.: Model structure of human APOBEC3G. PLoS ONE 2(4), e378 (2007).
17. Chelico L, Sacho EJ, Erie DA, Goodman MF: A model for oligomeric regulation of APOBEC3G cytosine deaminase-dependent restriction of HIV. J. Biol. Chem. 283(20), 13780-13791 (2008).
18. Wedekind JE, Gillilan R, Janda A et al.: Nanostructures of APOBEC3G support a hierarchical assembly model of high molecular mass ribonucleoprotein particles from dimeric subunits. J. Biol. Chem. 281(50), 38122-38126 (2006).
19. Stanley BJ, Ehrlich ES, Short L et al.: Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly. J. Virol. 82, 8656-8663 (2008).
20. Greene WC, Debyser Z, Ikeda Y et al.: Novel targets for HIV therapy. Antiviral Res. 80(3), 251-265 (2008).
21. Balaji S, Kalpana R, Shapshak P: Paradigm development: comparative and predictive 3D modeling of HIV-1 virion infectivity factor (Vif ). Bioinformation 1(8), 290-309 (2006).
22. Kavlock RJ, Ankley G, Blancato J et al.: Computational toxicology: a state of the science mini review. Toxicol. Sci. 103(1), 14-27 (2008).
23. Nathans R, Cao H, Sharova N et al.: Small-molecule inhibition of HIV-1 Vif. Nat. Biotechnol. 26, 1187-1192 (2008).
24. Harris R: Enhancing immunity to HIV through APOBEC. Nat. Biotechnol. 26, 1089-1090 (2008).
25. Miller JH, Presnyak V, Smith HC: The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G. Retrovirology 4, 1-11 (2007).
26. Jacobs GB, Nistal M, Laten A et al.: Molecular analysis of HIV type 1 Vif sequences from Cape Town, South Africa. AIDS Res. Hum. Retroviruses 24, 991-994 (2008).