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Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
Open accessAbstract
Viral replication usually requires that innate intracellular lines of defence be overcome, a task usually accomplished by specialized viral gene products. The virion infectivity factor (Vif) protein of human immunodeficiency virus (HIV) is required during the late stages of viral production to counter the antiviral activity of APOBEC3G (apolipoprotein B mRNA-editing enzyme, catalytic polypeptide-like 3G; also known as CEM15), a protein expressed notably in human T lymphocytes. When produced in the presence of APOBEC3G, vif-defective virus is non-infectious. APOBEC3G is closely related to APOBEC1, the central component of an RNA-editing complex that deaminates a cytosine residue in apoB messenger RNA. APOBEC family members also have potent DNA mutator activity through dC deamination; however, whether the editing potential of APOBEC3G has any relevance to HIV inhibition is unknown. Here, we demonstrate that it does, as APOBEC3G exerts its antiviral effect during reverse transcription to trigger G-to-A hypermutation in the nascent retroviral DNA. We also find that APOBEC3G can act on a broad range of retroviruses in addition to HIV, suggesting that hypermutation by editing is a general innate defence mechanism against this important group of pathogens.
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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).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Mangeat et al. 2003
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Cites
Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
Sheehy, A. M., Gaddis, N., Choi, J. D., & Malim, M. H. (2002) · Nature · doi:10.1038/nature00939 · Cited by 2,407
Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo
Zufferey, R., Nagy, D., Mandel, R. J., Naldini, L., & Trono, D. (1997) · Nature Biotechnology · doi:10.1038/nbt0997-871 · Cited by 1,977
Self-citationA novel form of tissue-specific RNA processing produces apolipoprotein-B48 in intestine
Powell, L. M., Wallis, S. C., Pease, R. J., Edwards, Y. H., Knott, T. J., & Scott, J. (1987) · Cell · doi:10.1016/0092-8674(87)90510-1 · Cited by 1,039
Transcription-targeted DNA deamination by the AID antibody diversification enzyme
Chaudhuri, J., Tian, M., Khuong, C., Chua, K. F., Pinaud, E., & Alt, F. W. (2003) · Nature · doi:10.1038/nature01574 · Cited by 746
An Anthropoid-Specific Locus of Orphan C to U RNA-Editing Enzymes on Chromosome 22
Jarmuz, A., Chester, A., Bayliss, J., Gisbourne, J., Dunham, I., Scott, J., & Navaratnam, N. (2002) · Genomics · doi:10.1006/geno.2002.6718 · Cited by 711
A quantitative assay for HIV DNA integration in vivo
Butler, S. L., Hansen, M. S., & Bushman, F. D. (2001) · Nature Medicine · doi:10.1038/87979 · Cited by 695
RNA Editing Enzyme APOBEC1 and Some of Its Homologs Can Act as DNA Mutators
Harris, R. S., Petersen‐Mahrt, S. K., & Neuberger, M. S. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00742-6 · Cited by 609
Molecular Cloning of an Apolipoprotein B Messenger RNA Editing Protein
Teng, B., Burant, C. F., & Davidson, N. O. (1993) · Science · doi:10.1126/science.8511591 · Cited by 536
Role of vif in replication of human immunodeficiency virus type 1 in CD4+ T lymphocytes
Gabuzda, D. H., Lawrence, K., Langhoff, E., Terwilliger, E., Dorfman, T., Haseltine, W. A., & Sodroski, J. (1992) · Journal of Virology · doi:10.1128/jvi.66.11.6489-6495.1992 · Cited by 444
Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells
von Schwedler, U. K., Song, J., Aiken, C., & Trono, D. (1993) · Journal of Virology · doi:10.1128/jvi.67.8.4945-4955.1993 · Cited by 441
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Stopak, K., de Noronha, C. M. C., Yonemoto, W. M., & Greene, W. C. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00353-8 · Cited by 723
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Yu, Q., König, R., Pillai, S. K., Chiles, K., Kearney, M. F., Palmer, S., Richman, D., Coffin, J. M., & Landau, N. R. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb758 · Cited by 596
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Yan, N., & Chen, Z. J. (2012) · Nature Immunology · doi:10.1038/ni.2229 · Cited by 565
Harris, R. S., & Dudley, J. P. (2015) · Virology · doi:10.1016/j.virol.2015.03.012 · Cited by 551
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Engelman, A., & Cherepanov, P. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2747 · Cited by 499
Chiu, Y., & Greene, W. C. (2008) · Annual Review of Immunology · doi:10.1146/annurev.immunol.26.021607.090350 · Cited by 426
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Chen, H., Lilley, C. E., Yu, Q., Lee, D. V., Chou, J., Narvaiza, I., Landau, N. R., & Weitzman, M. D. (2006) · Current Biology · doi:10.1016/j.cub.2006.01.031 · Cited by 385
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Esnault, C., Heidmann, O., Delebecque, F., Dewannieux, M., Ribet, D., Hance, A. J., Heidmann, T., & Schwartz, O. (2005) · Nature · doi:10.1038/nature03238 · Cited by 341
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Evidence for Editing of Human Papillomavirus DNA by APOBEC3 in Benign and Precancerous Lesions
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APOBEC3 proteins mediate the clearance of foreign DNA from human cells
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Deaminase-independent inhibition of HIV-1 reverse transcription by APOBEC3G
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Schröfelbauer, B., Chen, D., & Landau, N. R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307132101 · Cited by 309
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Blankson, J. N., Bailey, J. R., Thayil, S. M., Yang, H., Lassen, K. G., Lai, J., Gandhi, S. K., Siliciano, J. D., Williams, T. M., & Siliciano, R. F. (2006) · Journal of Virology · doi:10.1128/jvi.02165-06 · Cited by 288
Understanding HIV-1 latency provides clues for the eradication of long-term reservoirs
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Malim, M. H. (2008) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2008.0185 · Cited by 276
Gallois‐Montbrun, S., Kramer, B., Swanson, C. M., Byers, H. L., Lynham, S., Ward, M. A., & Malim, M. H. (2006) · Journal of Virology · doi:10.1128/jvi.02287-06 · Cited by 279
Mbisa, J. L., Barr, R., Thomas, J. A., Vandegraaff, N., Dorweiler, I. J., Svarovskaia, E. S., Brown, W. L., Mansky, L. M., Gorelick, R. J., Harris, R. S., et al. (2007) · Journal of Virology · doi:10.1128/jvi.00272-07 · Cited by 273
Simmonds, P. (2020) · mSphere · doi:10.1128/msphere.00408-20 · Cited by 245
Barreto, V. M., Reina‐San‐Martin, B., Ramiro, A. R., McBride, K. M., & Nussenzweig, M. C. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00309-5 · Cited by 270
APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells
Bogerd, H. P. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj416 · Cited by 270
Svarovskaia, E. S., Xu, H., Mbisa, J. L., Barr, R., Gorelick, R. J., Ono, A., Freed, E. O., Hu, W.-S., & Pathak, V. K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405761200 · Cited by 267
Nature, Position, and Frequency of Mutations Made in a Single Cycle of HIV-1 Replication
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VandeWoude, S., & Apetrei, C. (2006) · Clinical Microbiology Reviews · doi:10.1128/cmr.00009-06 · Cited by 262
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Identification of APOBEC3DE as Another Antiretroviral Factor from the Human APOBEC Family
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Bonvin, M., Achermann, F., Greeve, I., Stroka, D., Keogh, A., Inderbitzin, D., Candinas, D., Sommer, P., Wain–Hobson, S., Vartanian, J., et al. (2006) · Hepatology · doi:10.1002/hep.21187 · Cited by 252
High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition
Chiu, Y., Witkowska, H. E., Hall, S. C., Santiago, M. L., Soros, V. B., Esnault, C., Heidmann, T., & Greene, W. C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604524103 · Cited by 244
Human Tripartite Motif 5α Domains Responsible for Retrovirus Restriction Activity and Specificity
Pérez-Caballero, D., Hatziioannou, T., Yang, A., Cowan, S., & Bieniasz, P. D. (2005) · Journal of Virology · doi:10.1128/jvi.79.14.8969-8978.2005 · Cited by 244
The Interaction between HIV-1 Gag and APOBEC3G
Cen, S., Guo, F., Niu, M., Saadatmand, J., Deflassieux, J., & Kleiman, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402062200 · Cited by 242
Alce, T. M., & Popik, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400235200 · Cited by 239
氏家, 和., 石丸, 健., Barr, R., Zhang, Y., Khan, M. A., Strebel, K., & Pathak, V. K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400830101 · Cited by 238
A Single Amino Acid Determinant Governs the Species-specific Sensitivity of APOBEC3G to Vif Action
Mangeat, B., Turelli, P., Liao, S., & Trono, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400060200 · Cited by 237
Self-citationHuman APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif
Doehle, B., Schäfer, A., & Cullen, B. R. (2005) · Virology · doi:10.1016/j.virol.2005.06.005 · Cited by 227
Luo, K., Wang, T., Liu, B., Tian, C., Xiao, Z., Kappes, J. C., & Yu, X.-F. (2007) · Journal of Virology · doi:10.1128/jvi.02584-06 · Cited by 224
Schäfer, A., Bogerd, H. P., & Cullen, B. R. (2004) · Virology · doi:10.1016/j.virol.2004.08.006 · Cited by 223
Bárbaro, G., Scozzafava, A., Mastrolorenzo, A., & Supuran, C. T. (2005) · Current Pharmaceutical Design · doi:10.2174/1381612053764869 · Cited by 222
Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G
Chen, K., Harjes, E., Gross, P. J., Fahmy, A., Lu, Y., Shindo, K., Harris, R. S., & Matsuo, H. (2008) · Nature · doi:10.1038/nature06638 · Cited by 218
Metadata
- Authors
- Mangeat, B., Turelli, P., Caron, G., Friedli, M., Perrin, L., & Trono, D.
- Affiliations
- University of Geneva (CH)
- Corresponding author
- Trono, Didier
- Venue
- Nature
- Published
- 2003-05-28
- Volume
- 424
- Issue
- 6944
- Pages
- 99-103
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1966343819
- Cited by
- 1,486
- References
- 28
- Citations by year
- 2026: 20 · 2025: 29 · 2024: 23 · 2023: 28 · 2022: 25 · 2021: 43 · 2020: 37 · 2019: 53 · 2018: 49 · 2017: 56 · 2016: 58 · 2015: 58 · 2014: 79 · 2013: 87 · 2012: 97
- FWCI
- 36.98
- Type
- journal article
- Language
- en
- Open access
- green
- infoscience.epfl.ch
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- APOBEC3G, HIV-1 Vif, APOBEC1, cytosine deamination, reverse transcription, G-to-A hypermutation, retrovirus restriction, T cells, RNA editing
- MeSH terms
- APOBEC-3G Deaminase, Antiviral Agents, Base Sequence, Cell Line, Cytidine Deaminase, DNA, Viral, Humans, Molecular Sequence Data, Nucleoside Deaminases, Proteins, Repressor Proteins, RNA, Messenger, Transcription, Genetic, Virus Replication, HIV-1, Mutagenesis, Gene Products, vif, Point Mutation, RNA Editing, Viral Load, vif Gene Products, Human Immunodeficiency Virus
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