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Multifaceted antiviral actions of APOBEC3 cytidine deaminases
Abstract
To defend against external pathogens, metazoan organisms have evolved numerous defenses that generally fall within the innate and adaptive immune responses. Considerable effort continues to focus on developing a vaccine to manipulate the adaptive immune system to protect against or control HIV-1. However, recent advances in our understanding of the innate immune system have revealed that cells have a potent intrinsic antiretroviral defense in the form of APOBEC3G, which is a member of a larger family of cytidine deaminases that are active against HIV-1 and other retroviruses. Insights into how the action of A3G is circumvented by HIV-1 through the action of its Vif protein, and the surprising mechanisms by which A3G is regulated within the cell, offer exciting new opportunities for developing novel anti-HIV-1 therapies that exploit this intrinsic antiretroviral system.
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Cellular RNA polymerase II, along with various viral and host factors, also influences retroviral mutations, particularly in HIV-1.
“However, cellular RNA polymerase II, along with various viral and host factors, also influences retroviral mutations, particularly in HIV-1 (O’Neil et al. 2002, Mangeat et al. 2003, Chiu and Greene 2006, Hughes 2015).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Chiu and Greene 2006
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Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
Mangeat, B., Turelli, P., Caron, G., Friedli, M., Perrin, L., & Trono, D. (2003) · Nature · doi:10.1038/nature01709 · Cited by 1,486
Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G
Sawyer, S. L., Emerman, M., & Malik, H. S. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020275 · Cited by 485
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Research works printed but not linked: 80
- Sheehy, 2002, Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein, Nature, 418, 646, 10.1038/nature00939 · DOI
- Mariani, 2003, Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif, Cell, 114, 21, 10.1016/S0092-8674(03)00515-4 · DOI
- Stopak, 2003, HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability, Mol. Cell, 12, 591, 10.1016/S1097-2765(03)00353-8 · DOI
- Yu, 2004, Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome, Nat. Struct. Mol. Biol., 11, 435, 10.1038/nsmb758 · DOI
- Lecossier, 2003, Hypermutation of HIV-1 DNA in the absence of the Vif protein, Science, 300, 1112, 10.1126/science.1083338 · DOI
- Harris, 2003, DNA deamination mediates innate immunity to retroviral infection, Cell, 113, 803, 10.1016/S0092-8674(03)00423-9 · DOI
- Zhang, 2003, The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA, Nature, 424, 94, 10.1038/nature01707 · DOI
- Schrofelbauer, 2005, Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases, J. Virol., 79, 10978, 10.1128/JVI.79.17.10978-10987.2005 · DOI
- Kaiser, 2006, Uracil DNA glycosylase is dispensable for human immunodeficiency virus type 1 replication and does not contribute to the antiviral effects of the cytidine deaminase Apobec3G, J. Virol., 80, 875, 10.1128/JVI.80.2.875-882.2006 · DOI
- Simon, 1998, Evidence for a newly discovered cellular anti-HIV-1 phenotype, Nat. Med., 4, 1397, 10.1038/3987 · DOI
- Madani, 1998, An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein, J. Virol., 72, 10251, 10.1128/JVI.72.12.10251-10255.1998 · DOI
- Conticello, 2003, The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G, Curr. Biol., 13, 2009, 10.1016/j.cub.2003.10.034 · DOI
- Marin, 2003, HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation, Nat. Med., 9, 1398, 10.1038/nm946 · DOI
- Yu, 2003, Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex, Science, 302, 1056, 10.1126/science.1089591 · DOI
- Mehle, 2004, Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway, J. Biol. Chem., 279, 7792, 10.1074/jbc.M313093200 · DOI
- Mehle, 2004, Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation, Genes Dev., 18, 2861, 10.1101/gad.1249904 · DOI
- Yu, 2004, Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines, Genes Dev., 18, 2867, 10.1101/gad.1250204 · DOI
- Luo, 2005, Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5–E3 ligase through a HCCH motif to suppress APOBEC3G, Proc. Natl. Acad. Sci. U. S. A., 102, 11444, 10.1073/pnas.0502440102 · DOI
- Sheehy, 2003, The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif, Nat. Med., 9, 1404, 10.1038/nm945 · DOI
- Bogerd, 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. U. S. A., 101, 3770, 10.1073/pnas.0307713101 · DOI
- Mangeat, 2004, A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action, J. Biol. Chem., 279, 14481, 10.1074/jbc.C400060200 · DOI
- Schrofelbauer, 2004, A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif), Proc. Natl. Acad. Sci. U. S. A., 101, 3927, 10.1073/pnas.0307132101 · DOI
- Xu, 2004, A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion, Proc. Natl. Acad. Sci. U. S. A., 101, 5652, 10.1073/pnas.0400830101 · DOI
- Gaddis, 2004, Further investigation of simian immunodeficiency virus Vif function in human cells, J. Virol., 78, 12041, 10.1128/JVI.78.21.12041-12046.2004 · DOI
- Delebecque, 2006, Restriction of foamy viruses by APOBEC cytidine deaminases, J. Virol., 80, 605, 10.1128/JVI.80.2.605-614.2006 · DOI
- Lochelt, 2005, The antiretroviral activity of APOBEC3 is inhibited by the foamy virus accessory Bet protein, Proc. Natl. Acad. Sci. U. S. A., 102, 7982, 10.1073/pnas.0501445102 · DOI
- Russell, 2005, Foamy virus Bet proteins function as novel inhibitors of the APOBEC3 family of innate antiretroviral defense factors, J. Virol., 79, 8724, 10.1128/JVI.79.14.8724-8731.2005 · DOI
- Bishop, 2004, Cytidine deamination of retroviral DNA by diverse APOBEC proteins, Curr. Biol., 14, 1392, 10.1016/j.cub.2004.06.057 · DOI
- Liddament, 2004, APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo, Curr. Biol., 14, 1385, 10.1016/j.cub.2004.06.050 · DOI
- Zheng, 2004, Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication, J. Virol., 78, 6073, 10.1128/JVI.78.11.6073-6076.2004 · DOI
- Wiegand, 2004, A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins, EMBO J., 23, 2451, 10.1038/sj.emboj.7600246 · DOI
- Liu, 2005, Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase, J. Virol., 79, 9579, 10.1128/JVI.79.15.9579-9587.2005 · DOI
- Doehle, 2005, Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif, Virology, 339, 281, 10.1016/j.virol.2005.06.005 · DOI
- Jarmuz, 2002, An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22, Genomics, 79, 285, 10.1006/geno.2002.6718 · DOI
- Tian, 2006, Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F, J. Virol., 80, 3112, 10.1128/JVI.80.6.3112-3115.2006 · DOI
- Kao, 2004, Production of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cells, Retrovirology, 1, 27, 10.1186/1742-4690-1-27 · DOI
- Kao, 2003, The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity, J. Virol., 77, 11398, 10.1128/JVI.77.21.11398-11407.2003 · DOI
- Sakai, 2006, The Vif and Vpr accessory proteins independently cause HIV-1-induced T cell cytopathicity and cell cycle arrest, Proc. Natl. Acad. Sci. U. S. A., 103, 3369, 10.1073/pnas.0509417103 · DOI
- Kobayashi, 2004, APOBEC3G targets specific virus species, J. Virol., 78, 8238, 10.1128/JVI.78.15.8238-8244.2004 · DOI
- Doehle, 2005, Differential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion, J. Virol., 79, 8201, 10.1128/JVI.79.13.8201-8207.2005 · DOI
- Langlois, 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 Acids Res., 33, 1913, 10.1093/nar/gki343 · DOI
- Hache, 2005, The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain, J. Biol. Chem., 280, 10920, 10.1074/jbc.M500382200 · DOI
- Janini, 2001, Human immunodeficiency virus type 1 DNA sequences genetically damaged by hypermutation are often abundant in patient peripheral blood mononuclear cells and may be generated during near-simultaneous infection and activation of CD4+ T cells, J. Virol., 75, 7973, 10.1128/JVI.75.17.7973-7986.2001 · DOI
- Newman, 2005, Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity, Curr. Biol., 15, 166, 10.1016/j.cub.2004.12.068 · DOI
- Chiu, 2005, Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells, Nature, 435, 108, 10.1038/nature03493 · DOI
- Zack, 1990, HIV-1 entry into quiescent primary lymphocytes: molecular analysis reveals a labile, latent viral structure, Cell, 61, 213, 10.1016/0092-8674(90)90802-L · DOI · Paper page
- Stevenson, 1990, HIV-1 replication is controlled at the level of T cell activation and proviral integration, EMBO J., 9, 1551, 10.1002/j.1460-2075.1990.tb08274.x · DOI
- Neil, 2001, Postentry restriction to human immunodeficiency virus-based vector transduction in human monocytes, J. Virol., 75, 5448, 10.1128/JVI.75.12.5448-5456.2001 · DOI
- Triques, 2004, Characterization of restrictions to human immunodeficiency virus type 1 infection of monocytes, J. Virol., 78, 5523, 10.1128/JVI.78.10.5523-5527.2004 · DOI
- Kreisberg, J.F. et al. Endogenous factors enhance HIV infection of tissue naive CD4 T cells by stimulating high-molecular-mass APOBEC3G complex formation. J. Exp. Med. (in press)
- Turelli, 2004, Response to comment on ‘Inhibition of hepatitis B virus replication by APOBEC3G’, Science, 305, 1403B, 10.1126/science.1100464 · DOI
- Turelli, 2004, Inhibition of hepatitis B virus replication by APOBEC3G, Science, 303, 1829, 10.1126/science.1092066 · DOI
- Rosler, 2004, Comment on ‘Inhibition of hepatitis B virus replication by APOBEC3G’, Science, 305, 1403a, 10.1126/science.1100464 · DOI
- Suspene, 2005, Extensive editing of both hepatitis B virus DNA strands by APOBEC3 cytidine deaminases in vitro and in vivo, Proc. Natl. Acad. Sci. U. S. A., 102, 8321, 10.1073/pnas.0408223102 · DOI
- Noguchi, 2005, G to A hypermutation of hepatitis B virus, Hepatology, 41, 626, 10.1002/hep.20580 · DOI
- Sasada, 2005, APOBEC3G targets human T-cell leukemia virus type 1, Retrovirology, 2, 32, 10.1186/1742-4690-2-32 · DOI
- Mahieux, 2005, Extensive editing of a small fraction of human T-cell leukemia virus type 1 genomes by four APOBEC3 cytidine deaminases, J. Gen. Virol., 86, 2489, 10.1099/vir.0.80973-0 · DOI
- Navarro, 2005, Complementary function of the two catalytic domains of APOBEC3G, Virology, 333, 374, 10.1016/j.virol.2005.01.011 · DOI
- Zhang, 2004, Rapid evolution of primate antiviral enzyme APOBEC3G, Hum. Mol. Genet., 13, 1785, 10.1093/hmg/ddh183 · DOI
- Bogerd, 2006, APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells, Nucleic Acids Res., 34, 89, 10.1093/nar/gkj416 · DOI
- Esnault, 2005, APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses, Nature, 433, 430, 10.1038/nature03238 · DOI
- Dutko, 2005, Inhibition of a yeast LTR retrotransposon by human APOBEC3 cytidine deaminases, Curr. Biol., 15, 661, 10.1016/j.cub.2005.02.051 · DOI
- Schumacher, 2005, APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast, Proc. Natl. Acad. Sci. U. S. A., 102, 9854, 10.1073/pnas.0501694102 · DOI
- Chen, 2006, APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons, Curr. Biol., 16, 480, 10.1016/j.cub.2006.01.031 · DOI
- An, 2004, APOBEC3G genetic variants and their influence on the progression to AIDS, J. Virol., 78, 11070, 10.1128/JVI.78.20.11070-11076.2004 · DOI
- Do, 2005, Exhaustive genotyping of the CEM15 (APOBEC3G) gene and absence of association with AIDS progression in a French cohort, J. Infect. Dis., 191, 159, 10.1086/426826 · DOI
- Simon, 2005, Natural variation in Vif: differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification, PLoS Pathog., 1, e6, 10.1371/journal.ppat.0010006 · DOI
- Rose, 2004, Transcriptional regulation of APOBEC3G, a cytidine deaminase that hypermutates human immunodeficiency virus, J. Biol. Chem., 279, 41744, 10.1074/jbc.M406760200 · DOI
- Peng, 2006, Induction of APOBEC3 family proteins, a defensive maneuver underlying interferon-induced anti-HIV-1 activity, J. Exp. Med., 203, 41, 10.1084/jem.20051512 · DOI
- Tanaka, 2006, Anti-viral protein APOBEC3G is induced by interferon-α stimulation in human hepatocytes, Biochem. Biophys. Res. Commun., 341, 314, 10.1016/j.bbrc.2005.12.192 · DOI
- Cen, 2004, The interaction between HIV-1 Gag and APOBEC3G, J. Biol. Chem., 279, 33177, 10.1074/jbc.M402062200 · DOI
- Luo, 2004, Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging, J. Virol., 78, 11841, 10.1128/JVI.78.21.11841-11852.2004 · DOI
- Yu, 2004, APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication, J. Biol. Chem., 279, 53379, 10.1074/jbc.M408802200 · DOI
- Cullen, 2006, Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors, J. Virol., 80, 1067, 10.1128/JVI.80.3.1067-1076.2006 · DOI
- Mangeat, 2005, Lentiviral vectors and antiretroviral intrinsic immunity, Hum. Gene Ther., 16, 913, 10.1089/hum.2005.16.913 · DOI
- Turelli, 2005, Editing at the crossroad of innate and adaptive immunity, Science, 307, 1061, 10.1126/science.1105964 · DOI
- Huthoff, 2005, Cytidine deamination and resistance to retroviral infection: towards a structural understanding of the APOBEC proteins, Virology, 334, 147, 10.1016/j.virol.2005.01.038 · DOI
- Stopak, 2005, Protecting APOBEC3G: a potential new target for HIV drug discovery, Curr. Opin. Investig. Drugs, 6, 141
- Harris, 2004, Retroviral restriction by APOBEC proteins, Nat. Rev. Immunol., 4, 868, 10.1038/nri1489 · DOI
- Chiu, 2006, APOBEC3 cytidine deaminases: distinct antiviral actions along the retroviral life cycle, J. Biol. Chem., 281, 8309, 10.1074/jbc.R500021200 · DOI
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Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication
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“However, cellular RNA polymerase II, along with various viral and host factors, also influences retroviral mutations, particularly in HIV-1 (O’Neil et al. 2002 , Mangeat et al. 2003 , Chiu and Greene 2006 , Hughes 2015 ).”
Metadata
- Authors
- Chiu, Y.-L., & Greene, W. C.
- Affiliations
- University of California, San Francisco (US)
- ORCID
- Greene, Warner C.
- Venue
- Trends in Immunology
- Publisher
- Elsevier BV
- Published
- 2006-06
- Volume
- 27
- Issue
- 6
- Pages
- 291-297
- ISSN
- 1471-4906 (ISSN-L)
- OpenAlex
- W2071103917
- Cited by
- 72
- References
- 2
- Citations by year
- 2025: 5 · 2023: 2 · 2022: 1 · 2020: 2 · 2019: 1 · 2018: 4 · 2017: 2 · 2016: 2 · 2015: 2 · 2014: 1 · 2013: 1 · 2012: 7
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Immunology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (R01AI065329)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Keywords
- APOBEC3G, cytidine deaminase, HIV-1, innate immunity, Vif protein, retroviral restriction factors, HIV-1 vaccine
- MeSH terms
- APOBEC-3G Deaminase, Animals, Cytidine Deaminase, Humans, Nucleoside Deaminases, Repressor Proteins, HIV-1, Mice
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