on would be potential candidates for HIV-1 suppression, and purification of these Vif complexes in homogeneous form would provide the basis for screens to identify and evaluate inhibitor candidates. Thus, our strategy for purifying Vif-Cul5- 7 Interaction between Vif, CBFb, E3 Ligase Complexes CBFb-EloB/C complexes may lead to useful screening approaches for identifying novel anti-HIV drug candidates. Antibody against Vif was obtained through the AIDS Research and Reference Reagent Program, Division of AIDS, NIAID, National Institutes of Health. Acknowledgments We are grateful to Drs. Egbert Hoiczyck, Sean T. Prigge, and Colleen A. McHugh for advice and helpful discussions, as well as Drs. Alex Bullock, Rahul 7544432 M. Kohli, James T. Stivers, and Nancy A. Speck for plasmids. We thank Wenyan Zhang, Anjie Zhen, Brian Learn, Juan Du, and Ke Zhao for technical assistance and Dr. Deborah McClellan for editorial assistance. Author Contributions Conceived and designed the experiments: XFY XZ SLE. Performed the experiments: XZ SLE XH YL. Analyzed the data: XZ SLE XH XFY. Contributed reagents/materials/analysis tools: XZ SLE XFY. Wrote the paper: XZ SLE XFY. Reference 1. 2. Malim MH, Emerman M HIV-1 accessory proteinsensuring viral survival in a hostile environment. Cell Host Microbe 3: 388398. Chiu YL, Greene WC The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements. Annu Rev Immunol ” 26: order Relebactam 317353. Hache G, Mansky LM, Harris RS Human APOBEC3 proteins, retrovirus restriction, and HIV drug resistance. AIDS Rev 8: 148157. Niewiadomska AM, Yu XF Host restriction of HIV-1 by APOBEC3 and viral evasion through Vif. Curr Top Microbiol Immunol 339: 125. Cullen BR Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors. J Virol 80: 10671076. Goila-Gaur R, Strebel K HIV-1 Vif, APOBEC, and intrinsic immunity. Retrovirology 5: 51. 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: 646650. Luo K, Liu B, Xiao Z, Yu Y, Yu X, et al. Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging. J Virol 78: 1184111852. 9. Zennou V, Perez-Caballero D, Gottlinger H, Bieniasz PD APOBEC3G incorporation into human immunodeficiency virus type 1 particles. J Virol 78: 1205812061. Alce TM, Popik W APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein. J Biol Chem 279: 3408334086. Douaisi M, Dussart S, Courcoul M, Bessou G, Vigne R, et al. HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles. Biochem Biophys Res Commun 321: 566573. Schafer A, Bogerd HP, Cullen BR Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor. Virology 328: 163168. Cen S, Guo F, Niu M, Saadatmand J, Deflassieux J, et al. The interaction between HIV-1 Gag and APOBEC3G. J Biol Chem 279: 3317733184. Navarro F, Bollman B, Chen H, Konig R, Yu Q, et al. Complementary function of the two catalytic domains of APOBEC3G. Virology 333: 374386. Burnett A, Spearman P APOBEC3G multimers are recruited to the plasma membrane for packaging into human immunodeficiency virus type 1 10. 3. 4. 5. 6. 7. 11. 12. 13. 14. 8. 15. 8 Interaction between Vif, CBFb, E3 Ligase Complexes 16. 17. 18. 19. 20. 21. 22. 23. 24. 25. 2
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