Abstract
Apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like (APOBEC) proteins are members of a protein family sharing the common characteristic of cytidine deaminase activity. The antiviral activity of APOBEC3G and APOBEC3F has been studied more extensively than that of the other members of this family. The antiviral activity of APOBEC3B and APOBEC3DE has also been described. Studies of other APOBEC proteins have not revealed any antiviral activities against HIV-1; however, further investigation is required. In the absence of human immunodeficiency virus type 1 (HIV-1) virion infectivity factor (Vif), APOBEC3G and APOBEC3F are incorporated into HIV-1 virions and hypermutate the viral genomic DNA by their cytidine deaminase activity. HIV-1 Vif protein suppresses the antiviral role of APOBEC proteins by several mechanisms that lead to inhibition of incorporation of APOBEC3G/3F into HIV-1 virions. The detailed mechanisms involved in the suppression of APOBEC proteins by Vif are still being elucidated. Novel studies in which as yet undefined aspects of the suppression of APOBEC proteins are investigated could reveal important and potentially exploitable information for addressing HIV-1 infection in humans.
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Anderson JL, Hope TJ (2004) HIV accessory proteins and surviving the host cell. Curr HIV/AIDS Rep 1:47–53
Anderson JL, Hope TJ (2003) Recent insights into HIV accessory proteins. Curr Infect Dis Rep 5:439–450
Anton LC, Schubert U, Bacik I, Princiotta MF, Wearsch PA, Gibbs J, Day PM, Realini C, Rechsteiner MC, Bennink JR, Yewdell JW (1999) Intracellular localization of proteasomal degradation of a viral antigen. J Cell Biol 146:113–124
Argyris EG, Pomerantz RJ (2004) HIV-1 Vif versus APOBEC3G: newly appreciated warriors in the ancient battle between virus and host. Trends Microbiol 12:145–148
Bach D, Peddy S, Mangeat B, Lakkaraju A, Strub K, Trono D (2008) Characterization of APOBEC3G binding to 7SL RNA. Retrovirology 5:54
Barboric M, Zhang F, Besenicar M, Plemenitas A, Peterlin BM (2005) Ubiquitylation of Cdk9 by Skp2 facilitates optimal Tat transactivation. J Virol 79:11135–11141
Bardy M, Gay B, Pebernard S, Chazal N, Courcoul M, Vigne R, Decroly E, Boulanger P (2001) Interaction of human immunodeficiency virus type 1 Vif with Gag and Gag-Pol precursors: co-encapsidation and interference with viral protease-mediated Gag processing. J Gen Virol 82:2719–2733
Belshaw R, Pereira V, Katzourakis A, Talbot G, Paces J, Burt A, Tristem M (2004) Long-term reinfection of the human genome by endogenous retroviruses. Proc Natl Acad Sci USA 101:4894–4899
Bennett RP, Diner E, Sowden MP, Lees JA, Wedekind JE, Smith HC (2006) APOBEC-1 and AID are nucleo-cytoplasmic trafficking proteins but APOBEC3G cannot traffic. Biochem Biophys Res Commun 350:214–219
Bernacchi S, Henriet S, Dumas P, Paillart JC, Marquet R (2007) RNA and DNA binding properties of HIV-1 Vif protein. J Biol Chem 282:26361–26368
Berthoux L, Sebastian S, Sayah DM, Luban J (2005) Disruption of human TRIM5α antiviral activity by nonhuman primate orthologues. J Virol 79:7883–7888
Bishop KN, Holmes RK, Malim MH (2006) Antiviral potency of APOBEC proteins does not correlate with cytidine deamination. J Virol 80:8450–8458
Bishop KN, Holmes RK, Sheehy AM, Malim MH (2004) APOBEC-mediated editing of viral RNA. Science 305:645
Bogerd HP, Doehle BP, Wiegand HL, Cullen BR (2004) A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor. Proc Natl Acad Sci USA 101:3770–3774
Bonvin M, Greeve J (2007) Effects of point mutations in the cytidine deaminase domains of APOBEC3B on replication and hypermutation of hepatitis B virus in vitro. J Gen Virol 88:3270–3274
Bukrinskaya AG (2004) HIV-1 assembly and maturation. Archiv Virol 149:1067–1082
Burnett A, Spearman P (2007) APOBEC3G multimers are recruited to the plasma membrane for packaging into human immunodeficiency virus type 1 virus-like particles in an RNA-dependent process requiring the NC basic linker. J Virol 81:5000–5013
Camaur D, Trono D (1996) Characterization of human immunodeficiency virus type 1 Vif particle incorporation. J Virol 70:6106–6111
Chelico L, Sacho EJ, Erie DA, Goodman MF (2008) A model for oligomeric regulation of APOBEC3G cytosine deaminase-dependent restriction of HIV. J Biol Chem 283:13780–13791
Chiu YL, Soros VB, Kreisberg JF, Stopak K, Yonemoto W, Greene WC (2005) Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells. Nature 435:108–114
Dang Y, Wang X, Esselman WJ, Zheng YH (2006) Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J Virol 80:10522–10533
DeHart JL, Bosque A, Harris RS, Planelles V (2008) Human immunodeficiency virus type 1 Vif induces cell cycle delay via recruitment of the same E3 ubiquitin ligase complex that targets APOBEC3 proteins for degradation. J Virol 82:9265–9272
Dettenhofer M, Cen S, Carlson BA, Kleiman L, Yu XF (2000) Association of human immunodeficiency virus type 1 Vif with RNA and its role in reverse transcription. J Virol 74:8938–8945
Emerman M, Malim MH (1998) HIV-1 regulatory/accessory genes: keys to unraveling viral and host cell biology. Science 280:1880–1884
Esnault CC, Millet J, Schwartz O, Heidmann T (2006) Dual inhibitory effects of APOBEC family proteins on retrotransposition of mammalian endogenous retroviruses. Nucleic Acid Res 34:1522–1531
Farrow MA, Sheehy AM (2008) Vif and APOBEC3G in the innate immune response to HIV: a tale of two proteins. Future Microbiol 3:145–154
Franca R, Spadari S, Maga G (2005) Human immunodeficiency virus (HIV-1) auxiliary protein Vif and cellular APOBEC deaminases: their role unveiled? J Biol Sci 5:855–863
Gaddis NC, Chertova E, Sheehy AM, Henderson LE, Malim MH (2003) Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions. J Virol 77:5810–5820
Gandhi SK, Siliciano JD, Bailey JR, Siliciano RF, Blankson JN (2008) Role of APOBEC3G/F-mediated hypermutation in the control of human immunodeficiency virus type 1 in elite suppressors. J Virol 82:3125–3130
Goncalves J, Santa-Marta M (2004) HIV-1 Vif and APOBEC3G: multiple roads to one goal. Retrovirology. doi:10.1186/1742-4690-1181-1128
Guo F, Cen S, Niu M, Saadatmand J, Kleiman L (2006) The inhibition of tRNALys3-primed reverse transcription by human APOBEC3G during HIV-1 replication. J Virol. doi:10.1128/JVI.01038-01006
Hache G, Mansky LM, Harris RS (2006) Human APOBEC3 proteins, retrovirus restriction, and HIV drug resistance. AIDS Rev 8:148–157
Hache G, Shindo K, Albin J, Harris R (2008) Evolution of HIV-1 isolates that use a novel Vif-independent mechanism to resist restriction by human APOBEC3G. Curr Biol 18:819–824
Harris RS, Bishop KN, Sheehy AM, Craig H, Petersen-Mahrt S, Watt I, Neuberger M, Malim M (2003) DNA deamination mediates innate immunity to retroviral infection. Cell 113:803–809
Harris RS, Petersen-Mahrt S, Neuberger M (2002) RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators. Mol Cell 10:1247–1253
Henriet S, Richer D, Bernacchi S, Decroly E, Vigne R, Ehresmann B, Ehresmann C, Paillart JC, Marquet R (2005) Cooperative and specific binding of Vif to the 50 region of HIV-1 genomic RNA. J Mol Biol 354:55–72
Heuverswyn FV, Peeters M (2007) The origins of HIV and implications for the global epidemic. Curr Infect Dis Rep 9:338–346
Hill MS, Ruiz A, Gomez LM, Miller JM, Berman NEJ, Stephens EB (2007) APOBEC3G expression is restricted to epithelial cells of the proximal convoluted tubules and is not expressed in the glomeruli of macaques. J Histochem Cytochem 55:63–70
Holmes RK, Koning FA, Bishop KN, Malim MH (2007) APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. J Biol Chem 282:2587–2595
Hope TJ, Huang X, McDonald D, Parslow TG (1990) Steroid-receptor fusion of the human immunodeficiency virus type 1 Rev transactivator: mapping cryptic functions of the arginine-rich motif. Biochemistry 87:7787–7791
Jin X, Brooks A, Chen H, Bennett R, Reichman R, Smith H (2005) APOBEC3G/CEM15 (hA3G) mRNA levels associate inversely with human immunodeficiency virus viremia. J Virol 79:11513–11516
Kao S, Miyagi E, Khan MA, Takeuchi H, Opi S, Goila-Gaur R, Strebel K (2004) Production of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cells. Retrovirology 17:1–27
Khamsri B, Fujita M, Kamada K, Piroozmand A, Yamashita T, Uchiyama T, Adachi A (2006) Effects of lysine to arginine mutations in HIV-1 Vif on its expression and viral infectivity. Int J Mol Med 18:679–683
Khan M, Kao S, Miyagi E (2005) Viral RNA is required for the association of APOBEC3G with human immunodeficiency virus type 1 nucleoprotein complexes. J Virol 79:5870–5874
Kock J, Blum HE (2008) Hypermutation of hepatitis B virus genomes by APOBEC3G, APOBEC3C and APOBEC3H. J Gen Virol 89:1184–1191
Kotler M, Simm M, Zhao YS, Sova P, Chao W, Ohnona SF, Roller R, Krachmarow C, Potash MJ, Volsky DJ (1997) Human immunodeficiency virus type 1 (HIV-1) protein Vif inhibits the activity of HIV-1 protease in bacteria and in vitro. J Virol 71:5774–5781
Langlois MA, Beale RCL, Conticello SG, Neuberger MS (2005) Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities. Nucleic Acid Res 33:1913–1923
Lecossier D, Bouchonnet F, Clavel F, Hance AJ (2003) Hypermutation of HIV-1 DNA in the absence of the Vif protein. Science 300:1112
Lehmann DM, Galloway CA, Sowden MP, Smith HC (2006) Metabolic regulation of ApoB mRNA editing is associated with phosphorylation of APOBEC-1 complementation factor. Nucleic Acid Res 34:3299–3308
Li L, Li JY, Sui HS, Zhao RY, Liu YJ, Bao ZY, Liu SY, Zhuang DM (2008) HIV-1 Vif protein mediates the degradation of APOBEC3G in fission yeast when over-expressed using codon optimization. Virol Sin 23:255–264
Liu B, Sarkis PTN, Luo K, Yu Y, Yu XF (2005) Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase. J Virol 79:9579–9587
Liu Y, Li J, Kim BO, Pace BS, He JJ (2002) HIV-1 Tat protein-mediated transactivation of the HIV-1 long terminal repeat promoter is potentiated by a novel nuclear Tat-interacting protein of 110 kDa, Tip110. J Biol Chem 28:23854–23863
Lochelt M, Romen F, Bastone P, Muckenfuss H, Kirchner N, Kim YB, Truyen U, Rosler U, Battenberg M, Saib A, Flory E, Cichutek K, Munk C (2005) The antiretroviral activity of APOBEC3 is inhibited by the foamy virus accessory Bet protein. Proc Natl Acad Sci USA 102:7982–7987
Luo K, Wang T, Liu B, Tian C, Xiao Z, Kappes J, Yu XF (2007) Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation. J Virol 81:7238–7248
Lv W, Liu Z, Jin H, Yu X, Zhang L, Zhang L (2007) Three-dimensional structure of HIV-1 Vif constructed by comparative modeling and the function characterization analyzed by molecular dynamics simulation. Org Biomol Chem 5:617–626
MacDuff DA, Harris RS (2006) Directed DNA deamination by AID/APOBEC3 in immunity. Curr Biol 16:R186–R189
Mariani R, Chen D, Schrofelbauer B, Navarro F, Konig R, Bollman B, Munk C, Nymark-McMahon H, Landau NR (2003) Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 114:21–31
Marin M, Golem S, Rose KM, Kozak SL, Kabat D (2007) HIV-1 Vif functionally interacts with diverse APOBEC3 cytidine deaminases and moves with them between cytoplasmic sites of mRNA metabolism. J Virol. doi:10.1128/JVI.01078-01007
Mehle A, Goncalves J, Santa-Marta M, Mcpike M, Gabuzda D (2004) Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif–Cul5 complex that promotes APOBEC3G degradation. Genes Dev 18:2861–2866
Mehle A, Strack B, Ancuta P, Zhang C, McPike M, Gabzda D (2004) Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin–proteasome pathway. J Biol Chem 279:7792–7798
Mehle A, Thomas ER, Rajendran KS, Gabuzda D (2006) A zinc-binding region in Vif binds Cul5 and determines cullin selection. J Biol Chem 281:17259–17265
Mehle A, Wilson H, Zhang C, Brazier AJ, McPike M, Pery E, Gabuzda D (2007) Identification of an APOBEC3G binding site in HIV-1 Vif and inhibitors of Vif APOBEC3G binding. J Virol. doi:10.1128/JVI.00204-00207
Navarro F, Landau NR (2004) Recent insights into HIV-1 Vif. Curr Opin Immunol 16:477–482
Ochsenbauer C, Wilk T, Bosch V (1997) Analysis of vif-defective human immunodeficiency virus type 1 (HIV-1) virions synthesized in ‘non-permissive’ T lymphoid cells stably infected with selectable HIV-1. J Gen Virol 78:627–635
OhAinle M, Kerns JA, Li MMH, Harmit SM, Emerman M (2008) Antiretroelement activity of APOBEC3H was lost twice in recent human evolution. Cell Host Microbe 4:249–259
OhAinle M, Kerns JA, Malik HS, Emerman M (2006) Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H. J Virol 80:3853–3862
Paulous S, Emerman M, Keller R, Montagnier L, Cordonnier A (1992) Functional mapping of the rev-responsive element of human immunodeficiency virus type 2 (HIV-2): influence of HIV-2 envelope-encoding sequences on HIV-1 gpl20 expression in the presence or absence of Rev. J Gen Virol 73:1773–1780
Pomerantz RJ (2003) The HIV-1 Vif protein: a paradigm for viral: cell interactions. Cell Mol Life Sci 60:2017–2019
Priet S, Gros N, Navarro JM, Boretto J, Canard B, Querat G, Sire J (2005) HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle. Mol Cell 17:479–490
Rogozin IB, Basu MK, Jordan IK, Pavlov YI, Koonin EV (2005) APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy) cytidine deaminases predicted by computational analysis. Cell Cycle 4:1281–1285
Rulli-Jr SJ, Mirro J, Hill SA, Lloyd P, Gorelick RJ, Coffin JM, Derse D, Rein A (2008) Interactions of murine APOBEC3 and human APOBEC3G with murine leukemia viruses. J Virol 82:6566–6575
Sakai H, Shibata R, Sakuragi JI, Sakuragi S, Kawamura M, Adachi A (1993) Cell-dependent requirement of human immunodeficiency virus type 1 Vif protein for maturation of virus particles. J Virol 67:1663–1666
Sakai K, Dimas J, Lenardo MJ (2006) The Vif and Vpr accessory proteins independently cause HIV-1-induced T cell cytopathicity and cell cycle arrest. Proc Natl Acad Sci USA 103:3369–3374
Salemi M, Strimmer K, Hall WW, Duffy M, Delaporte E, Mboup S, Peeters M, Vandamme AM (2001) Dating the common ancestor of SIVcpz and HIV-1 group M and the origin of HIV-1 subtypes using a new method to uncover clock-like molecular evolution. FASEB J 15:276–278
Santa-Marta M, Silva FAD, Fonseca AM, Goncalves J (2004) HIV-1 Vif can directly inhibit apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation. J Bacteriol Chem 280:8765–8775
Schrofelbauer B, Yu Q, Landau NR (2004) New insights into the role of Vif in HIV-1 replication. AIDS Rev 6:34–39
Seelamgari A, Maddukuri A, Berro R, de-la-Fuente C, Kehn K, Deng L, Dadgar S, Bottazzi ME, Ghedin E, Pumfery A, Kashanchi F (2004) Role of viral regulatory and accessory proteins in HIV-1 replication. Front Biosci 1:2388–2413
Sheehy AM, Gaddis NC, Choi JD, Malim MH (2002) Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418:646–650
Simon JHM, Miller DL, Fouchier RAM, Malim MH (1998) Virion incorporation of human immunodeficiency virus type-1 Vif is determined by intracellular expression level and may not be necessary for function. Virology 248:182–187
Soares AER, Soares MA, Schrago CG (2008) Positive selection on HIV accessory proteins and the analysis of molecular adaptation after interspecies transmission. J Mol Evol 66:598–604
Stanley BJ, Ehrlich ES, Short L, Yu Y, Xiao Z, Yu XF, Xiong Y (2008) Structural insight into the HIV Vif SOCS box and its role in human E3 ubiquitin ligase. J Virol 82:8656–8663
Stenglein MD, Harris RS (2006) APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism. J Bacteriol Chem 281:16837–16841
Stopak K, De-Noronha C, Yonemoto W, Greene WC (2003) HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol Cell 12:591–601
Strebel K, Khan MA (2008) APOBEC3G encapsidation into HIV-1 virions: which RNA is it? Retrovirology. doi:10.1186/1742-4690-1185-1155
Sun BJ, Nie P (2004) Molecular cloning of the viperin gene and its promoter region from the mandarin fish Siniperca chuatsi. Vet Immunol Immunopathol 101:161–170
Suspene R, Sommer P, Henry M, Ferris S, Guetard D, Pochet S, Chester A, Navaratnam N, Wain-Hobson S, Vartanian JP (2004) APOBEC3G is a single-stranded DNA cytidine deaminase and functions independently of HIV reverse transcriptase. Nucleic Acids Res 32:2421–2429
Suzuki T, Park H, Lennarz WJ (2002) Cytoplasmic peptide:N-glycanase (PNGase) in eukaryotic cells: occurrence, primary structure, and potential functions. FASEB J 16:635–641
Svarovskaia ES, Xu H, Mbisa JL, Barr R, Gorelick RJ, Ono A, Freed EO, Hu WS, Pathak VK (2004) Human APOBEC3G is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs. J Bacteriol Chem 279:35822–35828
Tenno T, Fujiwara K, Tochio H, Lawi K, Morita EH, Hayashi H, Murata S, Hiroaki H, Sato M, Tanaka K, Shirakawa M (2004) Structural basis for distinct roles of Lys63- and Lys48-linked polyubiquitin chains. Genes Cells 9:865–875
Turelli P, Jost S, Mangeat B, Trono D (2004) Response to comment on “inhibition of hepatitis B virus replication by APOBEC3G’’. Science 305:1403b
Turelli P, Mangeat B, Jost S, Vianin S, Trono D (2004) Inhibition of hepatitis B virus replication by APOBEC3G. Science 303:1829
Turelli P, Trono D (2005) Editing at the crossroad of innate and adaptive immunity. Science 307:1061–1065
Ulenga NK, Sarr AD, Hamel D, Sankale JL, Sankale JL, Mboup S, Kanki PJ (2008) The level of APOBEC3G (hA3G)-related G-to-A mutations does not correlate with viral load in HIV type 1-infected individuals. AIDS Res Hum Retroviruses 24:1285–1290
Virgen CA, Hatziioannou T (2007) Antiretroviral activity and Vif sensitivity of rhesus macaque APOBEC3 Proteins. J Virol 81:13932–13937
Wang J, Shackelford JM, Selliah N, Shivers DK, O’neill E, Garcia JV, Muthumani K, Weiner D, Yu XF, Gabuzda D, Finkel TH (2008) The HIV-1 Vif protein mediates degradation of Vpr and reduces Vpr-induced cell cycle arrest. DNA Cell Biol 27:267–277
Wang T, Tian C, Zhang W, Luo K, Sarkis PTN, Yu L, Liu B, Yu Y, Yu XF (2007) 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G. J Virol 81:13112–13124
Wang X, Dolan PT, Dang Y, Zheng YH (2007) Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycle. J Biol Chem 282:1585–1594
Wiegand HL, Doehle BP, Bogerd HP, Cullen BR (2004) A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J 23:2451–2458
Xiao-xia WU, Yi-cai MA (2005) Antiviral warrior-APOBEC3G. J Electron Sci Technol China 3:372–376
Xiao Z, Ehrlich E, Luo K, Xiong Y, Yu XF (2007) Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G. FASEB J 21:217–222
Yap MW, Nisole S, Lynch C, Stoye JP (2004) Trim5α protein restricts both HIV-1 and murine leukemia virus. Proc Natl Acad Sci USA 101:10786–10791
Yu Q, Konig R, Pillai S, Chiles K, Kearney M, Palmer S, Richman D, Coffin JM, Landau NR (2004) Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome. Nat Struct Mol Biol 11:435–442
Yu Y, Xiao Z, Ehrlich ES, Yu X, Yu XF (2004) Selective assembly of HIV-1Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev 18:2867–2872
Zennou V, Perez-Caballero D, Gottlinger H, Bieniasz PD (2004) APOBEC3G incorporation into human immunodeficiency virus type 1 particles. J Virol 78:12058–12061
Zhang H, Pomerantz RJ, Dornadula G, Sun Y (2000) Human immunodeficiency virus type 1 Vif protein is an integral component of an mRNP complex of viral RNA and could be involved in the viral RNA folding and packaging process. J Virol 74:8252–8261
Zhang H, Yang B, Pomerantz RJ, Zhang C, Arunachalam SC, Gao L (2003) The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424:94–98
Zheng YH, Irwin D, Kurosu T, Tokunaga K, Sata T, Peterlin BM (2004) Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J Virol 78:6073–6076
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Romani, B., Engelbrecht, S. & Glashoff, R.H. Antiviral roles of APOBEC proteins against HIV-1 and suppression by Vif. Arch Virol 154, 1579–1588 (2009). https://doi.org/10.1007/s00705-009-0481-y
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DOI: https://doi.org/10.1007/s00705-009-0481-y