메뉴 건너뛰기




Volumn 84, Issue 14, 2010, Pages 7396-7404

APOBEC3G contributes to HIV-1 variation through sublethal mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; MUTANT PROTEIN; VIRUS VECTOR;

EID: 77953769689     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00056-10     Document Type: Article
Times cited : (147)

References (45)
  • 1
    • 0024438889 scopus 로고
    • Specificity and mechanism of error-prone replication by human immunodeficiency virus-1 reverse transcriptase
    • Bebenek, K., J. Abbotts, J. D. Roberts, S. H. Wilson, and T. A. Kunkel. 1989. Specificity and mechanism of error-prone replication by human immunodeficiency virus-1 reverse transcriptase. J. Biol. Chem. 264:16948-16956.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16948-16956
    • Bebenek, K.1    Abbotts, J.2    Roberts, J.D.3    Wilson, S.H.4    Kunkel, T.A.5
  • 2
    • 0026714957 scopus 로고
    • The effects of dNTP pool imbalances on frameshift fidelity during DNA replication
    • Bebenek, K., J. D. Roberts, and T. A. Kunkel. 1992. The effects of dNTP pool imbalances on frameshift fidelity during DNA replication. J. Biol. Chem. 267:3589-3596.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3589-3596
    • Bebenek, K.1    Roberts, J.D.2    Kunkel, T.A.3
  • 4
    • 64849104502 scopus 로고    scopus 로고
    • Restriction of HIV-1 by APOBEC3G is cytidine deaminase-dependent
    • Browne, E. P., C. Allers, and N. R. Landau. 2009. Restriction of HIV-1 by APOBEC3G is cytidine deaminase-dependent. Virology 387:313-321.
    • (2009) Virology , vol.387 , pp. 313-321
    • Browne, E.P.1    Allers, C.2    Landau, N.R.3
  • 5
    • 9144256760 scopus 로고    scopus 로고
    • Vif is an auxiliary factor of the HIV-1 reverse transcriptase and facilitates abasic site bypass
    • DOI 10.1042/BJ20040914
    • Cancio, R., S. Spadari, and G. Maga. 2004. Vif is an auxiliary factor of the HIV-1 reverse transcriptase and facilitates abasic site bypass. Biochem. J. 383:475-482. (Pubitemid 39546117)
    • (2004) Biochemical Journal , vol.383 , Issue.3 , pp. 475-482
    • Cancio, R.1    Spadari, S.2    Maga, G.3
  • 6
    • 38949093228 scopus 로고    scopus 로고
    • Human immunodeficiency virus 1 (HIV-1) virion infectivity factor (Vif) is part of reverse transcription complexes and acts as an accessory factor for reverse transcription
    • Carr, J. M., C. Coolen, A. J. Davis, C. J. Burrell, and P. Li. 2008. Human immunodeficiency virus 1 (HIV-1) virion infectivity factor (Vif) is part of reverse transcription complexes and acts as an accessory factor for reverse transcription. Virology 372:147-156.
    • (2008) Virology , vol.372 , pp. 147-156
    • Carr, J.M.1    Coolen, C.2    Davis, A.J.3    Burrell, C.J.4    Li, P.5
  • 8
    • 0026672676 scopus 로고
    • Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: Definition of critical amino acids involved in cell tropism
    • Chesebro, B., K. Wehrly, J. Nishio, and S. Perryman. 1992. Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: definition of critical amino acids involved in cell tropism. J. Virol. 66:6547-6554.
    • (1992) J. Virol. , vol.66 , pp. 6547-6554
    • Chesebro, B.1    Wehrly, K.2    Nishio, J.3    Perryman, S.4
  • 9
    • 42649120310 scopus 로고    scopus 로고
    • The APOBEC3 cytidine deaminases: An innate defensive network opposing exogenous retroviruses and endogenous retroelements
    • Chiu, Y. L., and W. C. Greene. 2008. The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements. Annu. Rev. Immunol. 26:317-353.
    • (2008) Annu. Rev. Immunol. , vol.26 , pp. 317-353
    • Chiu, Y.L.1    Greene, W.C.2
  • 10
    • 0028842207 scopus 로고
    • Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes
    • Connor, R. I., B. K. Chen, S. Choe, and N. R. Landau. 1995. Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes. Virology 206:935-944.
    • (1995) Virology , vol.206 , pp. 935-944
    • Connor, R.I.1    Chen, B.K.2    Choe, S.3    Landau, N.R.4
  • 11
    • 33645232013 scopus 로고    scopus 로고
    • Role of the human T-cell leukemia virus type 1 PTAP motif in Gag targeting and particle release
    • Dorweiler, I. J., S. J. Ruone, H. Wang, R. W. Burry, and L. M. Mansky. 2006. Role of the human T-cell leukemia virus type 1 PTAP motif in Gag targeting and particle release. J. Virol. 80:3634-3643.
    • (2006) J. Virol. , vol.80 , pp. 3634-3643
    • Dorweiler, I.J.1    Ruone, S.J.2    Wang, H.3    Burry, R.W.4    Mansky, L.M.5
  • 13
    • 48949118733 scopus 로고    scopus 로고
    • HIV-1 Vif, APOBEC, and intrinsic immunity
    • Goila-Gaur, R., and K. Strebel. 2008. HIV-1 Vif, APOBEC, and intrinsic immunity. Retrovirology 5:51.
    • (2008) Retrovirology , vol.5 , pp. 51
    • Goila-Gaur, R.1    Strebel, K.2
  • 14
    • 33751206549 scopus 로고    scopus 로고
    • Lys-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication
    • DOI 10.1128/JVI.01038-06
    • Guo, F., S. Cen, M. Niu, J. Saadatmand, and L. Kleiman. 2006. Inhibition of formula-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication. J. Virol. 80:11710-11722. (Pubitemid 44788884)
    • (2006) Journal of Virology , vol.80 , Issue.23 , pp. 11710-11722
    • Guo, F.1    Cen, S.2    Niu, M.3    Saadatmand, J.4    Kleiman, L.5
  • 15
    • 35148824006 scopus 로고    scopus 로고
    • The interaction of APOBEC3G with human immunodeficiency virus type 1 nucleocapsid inhibits tRNA3Lys annealing to viral RNA
    • Guo, F., S. Cen, M. Niu, Y. Yang, R. J. Gorelick, and L. Kleiman. 2007. The interaction of APOBEC3G with human immunodeficiency virus type 1 nucleocapsid inhibits tRNA3Lys annealing to viral RNA. J. Virol. 81:11322-11331.
    • (2007) J. Virol. , vol.81 , pp. 11322-11331
    • Guo, F.1    Cen, S.2    Niu, M.3    Yang, Y.4    Gorelick, R.J.5    Kleiman, L.6
  • 16
    • 33750288097 scopus 로고    scopus 로고
    • Human APOBEC3 proteins, retrovirus restriction, and HIV drug resistance
    • Hache, G., L. M. Mansky, and R. S. Harris. 2006. Human APOBEC3 proteins, retrovirus restriction, and HIV drug resistance. AIDS Rev. 8:148-157.
    • (2006) AIDS Rev. , vol.8 , pp. 148-157
    • Hache, G.1    Mansky, L.M.2    Harris, R.S.3
  • 17
    • 44349179677 scopus 로고    scopus 로고
    • Evolution of HIV-1 isolates that use a novel Vif-independent mechanism to resist restriction by human APOBEC3G
    • Hache, G., K. Shindo, J. S. Albin, and R. S. Harris. 2008. Evolution of HIV-1 isolates that use a novel Vif-independent mechanism to resist restriction by human APOBEC3G. Curr. Biol. 18:819-824.
    • (2008) Curr. Biol. , vol.18 , pp. 819-824
    • Hache, G.1    Shindo, K.2    Albin, J.S.3    Harris, R.S.4
  • 19
    • 33847625391 scopus 로고    scopus 로고
    • APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G
    • Holmes, R. K., F. A. Koning, K. N. Bishop, and M. H. Malim. 2007. APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. J. Biol. Chem. 282:2587-2595.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2587-2595
    • Holmes, R.K.1    Koning, F.A.2    Bishop, K.N.3    Malim, M.H.4
  • 20
    • 0034878971 scopus 로고    scopus 로고
    • 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
    • Janini, M., M. Rogers, D. R. Birx, and F. E. McCutchan. 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. 75:7973-7986.
    • (2001) J. Virol. , vol.75 , pp. 7973-7986
    • Janini, M.1    Rogers, M.2    Birx, D.R.3    McCutchan, F.E.4
  • 21
    • 66349132212 scopus 로고    scopus 로고
    • Likely role of APOBEC3G-mediated G-to-A mutations in HIV-1 evolution and drug resistance
    • Jern, P., R. A. Russell, V. K. Pathak, and J. M. Coffin. 2009. Likely role of APOBEC3G-mediated G-to-A mutations in HIV-1 evolution and drug resistance. PLoS Pathog. 5:e1000367.
    • (2009) PLoS Pathog. , vol.5
    • Jern, P.1    Russell, R.A.2    Pathak, V.K.3    Coffin, J.M.4
  • 23
    • 0031717603 scopus 로고    scopus 로고
    • Deoxyribonucleoside triphosphate pool imbalances in vivo are associated with an increased retroviral mutation rate
    • Julias, J. G., and V. K. Pathak. 1998. Deoxyribonucleoside triphosphate pool imbalances in vivo are associated with an increased retroviral mutation rate. J. Virol. 72:7941-7949.
    • (1998) J. Virol. , vol.72 , pp. 7941-7949
    • Julias, J.G.1    Pathak, V.K.2
  • 24
    • 0142092452 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity
    • Kao, S., M. A. Khan, E. Miyagi, R. Plishka, A. Buckler-White, and K. Strebel. 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. 77:11398-11407.
    • (2003) J. Virol. , vol.77 , pp. 11398-11407
    • Kao, S.1    Khan, M.A.2    Miyagi, E.3    Plishka, R.4    Buckler-White, A.5    Strebel, K.6
  • 25
    • 67649888378 scopus 로고    scopus 로고
    • Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase
    • Kataropoulou, A., C. Bovolenta, A. Belfiore, S. Trabatti, A. Garbelli, S. Porcellini, R. Lupo, and G. Maga. 2009. Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase. Nucleic Acids Res. 37:3660-3669.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3660-3669
    • Kataropoulou, A.1    Bovolenta, C.2    Belfiore, A.3    Trabatti, S.4    Garbelli, A.5    Porcellini, S.6    Lupo, R.7    Maga, G.8
  • 26
    • 49149090397 scopus 로고    scopus 로고
    • Human immunodeficiency virus (HIV) type 1 proviral hypermutation correlates with CD4 count in HIV-infected women from Kenya
    • Land, A. M., T. B. Ball, M. Luo, R. Pilon, P. Sandstrom, J. E. Embree, C. Wachihi, J. Kimani, and F. A. Plummer. 2008. Human immunodeficiency virus (HIV) type 1 proviral hypermutation correlates with CD4 count in HIV-infected women from Kenya. J. Virol. 82:8172-8182.
    • (2008) J. Virol. , vol.82 , pp. 8172-8182
    • Land, A.M.1    Ball, T.B.2    Luo, M.3    Pilon, R.4    Sandstrom, P.5    Embree, J.E.6    Wachihi, C.7    Kimani, J.8    Plummer, F.A.9
  • 27
    • 36148995875 scopus 로고    scopus 로고
    • APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription
    • Li, X. Y., F. Guo, L. Zhang, L. Kleiman, and S. Cen. 2007. APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription. J. Biol. Chem. 282:32065-32074.
    • (2007) J. Biol. Chem. , vol.282 , pp. 32065-32074
    • Li, X.Y.1    Guo, F.2    Zhang, L.3    Kleiman, L.4    Cen, S.5
  • 28
    • 34250857925 scopus 로고    scopus 로고
    • Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation
    • Luo, K., T. Wang, B. Liu, C. Tian, Z. Xiao, J. Kappes, and X. F. Yu. 2007. Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation. J. Virol. 81:7238-7248.
    • (2007) J. Virol. , vol.81 , pp. 7238-7248
    • Luo, K.1    Wang, T.2    Liu, B.3    Tian, C.4    Xiao, Z.5    Kappes, J.6    Yu, X.F.7
  • 29
    • 44649139364 scopus 로고    scopus 로고
    • HIV-1 accessory proteins: Ensuring viral survival in a hostile environment
    • Malim, M. H., and M. Emerman. 2008. HIV-1 accessory proteins: ensuring viral survival in a hostile environment. Cell Host Microbe 3:388-398.
    • (2008) Cell Host Microbe , vol.3 , pp. 388-398
    • Malim, M.H.1    Emerman, M.2
  • 30
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat, B., P. Turelli, G. Caron, M. Friedli, L. Perrin, and D. Trono. 2003. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424:99-103.
    • (2003) Nature , vol.424 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, L.5    Trono, D.6
  • 31
    • 0029075130 scopus 로고
    • Lower in vivo mutation rate of human immunodeficiency virus type 1 than predicted from the fidelity of purified reverse transcriptase
    • Mansky, L. M., and H. M. Temin. 1995. Lower in vivo mutation rate of human immunodeficiency virus type 1 than predicted from the fidelity of purified reverse transcriptase. J. Virol. 69:5087-5094.
    • (1995) J. Virol. , vol.69 , pp. 5087-5094
    • Mansky, L.M.1    Temin, H.M.2
  • 33
    • 37049032574 scopus 로고    scopus 로고
    • Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1
    • Miyagi, E., S. Opi, H. Takeuchi, M. Khan, R. Goila-Gaur, S. Kao, and K. Strebel. 2007. Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1. J. Virol. 81:13346-13353.
    • (2007) J. Virol. , vol.81 , pp. 13346-13353
    • Miyagi, E.1    Opi, S.2    Takeuchi, H.3    Khan, M.4    Goila-Gaur, R.5    Kao, S.6    Strebel, K.7
  • 35
    • 0037064085 scopus 로고    scopus 로고
    • Mutational analysis of HIV-1 long terminal repeats to explore the relative contribution of reverse transcriptase and RNA polymerase II to viral mutagenesis
    • O'Neil, P. K., G. Sun, H. Yu, Y. Ron, J. P. Dougherty, and B. D. Preston. 2002. Mutational analysis of HIV-1 long terminal repeats to explore the relative contribution of reverse transcriptase and RNA polymerase II to viral mutagenesis. J. Biol. Chem. 277:38053-38061.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38053-38061
    • O'Neil, P.K.1    Sun, G.2    Yu, H.3    Ron, Y.4    Dougherty, J.P.5    Preston, B.D.6
  • 36
    • 63049108063 scopus 로고    scopus 로고
    • APOBEC3G induces a hypermutation gradient: Purifying selection at multiple steps during HIV-1 replication results in levels of G-to-A mutations that are high in DNA, intermediate in cellular viral RNA, and low in virion RNA
    • Russell, R. A., M. D. Moore, W. S. Hu, and V. K. Pathak. 2009. APOBEC3G induces a hypermutation gradient: purifying selection at multiple steps during HIV-1 replication results in levels of G-to-A mutations that are high in DNA, intermediate in cellular viral RNA, and low in virion RNA. Retrovirology 6:16.
    • (2009) Retrovirology , vol.6 , pp. 16
    • Russell, R.A.1    Moore, M.D.2    Hu, W.S.3    Pathak, V.K.4
  • 37
    • 40149102165 scopus 로고    scopus 로고
    • The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction
    • Schumacher, A. J., G. Hache, D. A. Macduff, W. L. Brown, and R. S. Harris. 2008. The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction. J. Virol. 82:2652-2660.
    • (2008) J. Virol. , vol.82 , pp. 2652-2660
    • Schumacher, A.J.1    Hache, G.2    Macduff, D.A.3    Brown, W.L.4    Harris, R.S.5
  • 38
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy, A. M., N. C. Gaddis, J. D. Choi, and M. H. Malim. 2002. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418:646-650.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 39
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy, A. M., N. C. Gaddis, and M. H. Malim. 2003. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat. Med. 9:1404-1407.
    • (2003) Nat. Med. , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 40
    • 0028866919 scopus 로고
    • Human immunodeficiency virus envelope V1 and V2 regions influence replication efficiency in macrophages by affecting virus spread
    • Toohey, K., K. Wehrly, J. Nishio, S. Perryman, and B. Chesebro. 1995. Human immunodeficiency virus envelope V1 and V2 regions influence replication efficiency in macrophages by affecting virus spread. Virology 213:70-79.
    • (1995) Virology , vol.213 , pp. 70-79
    • Toohey, K.1    Wehrly, K.2    Nishio, J.3    Perryman, S.4    Chesebro, B.5
  • 41
    • 0028180510 scopus 로고
    • G-A hypermutation of the human immunodeficiency virus type 1 genome: Evidence for dCTP pool imbalance during reverse transcription
    • Vartanian, J.-P., A. Meyerhans, M. Sala, and S. Wain-Hobson. 1994. G-A hypermutation of the human immunodeficiency virus type 1 genome: evidence for dCTP pool imbalance during reverse transcription. Proc. Natl. Acad. Sci. U. S. A. 91:3092-3096.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 3092-3096
    • Vartanian, J.-P.1    Meyerhans, A.2    Sala, M.3    Wain-Hobson, S.4
  • 42
    • 0031214430 scopus 로고    scopus 로고
    • P24 antigen capture assay for quantification of human immunodeficiency virus using readily available inexpensive reagents
    • Wehrly, K., and B. Chesebro. 1997. p24 antigen capture assay for quantification of human immunodeficiency virus using readily available inexpensive reagents. Methods 12:288-293.
    • (1997) Methods , vol.12 , pp. 288-293
    • Wehrly, K.1    Chesebro, B.2
  • 44
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang, H., B. Yang, R. J. Pomerantz, C. Zhang, S. C. Arunachalam, and L. Gao. 2003. The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424:94-98.
    • (2003) Nature , vol.424 , pp. 94-98
    • Zhang, H.1    Yang, B.2    Pomerantz, R.J.3    Zhang, C.4    Arunachalam, S.C.5    Gao, L.6
  • 45
    • 4444290423 scopus 로고    scopus 로고
    • Rapid evolution of primate antiviral enzyme APOBEC3G
    • Zhang, J., and D. M. Webb. 2004. Rapid evolution of primate antiviral enzyme APOBEC3G. Hum. Mol. Genet. 13:1785-1791.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1785-1791
    • Zhang, J.1    Webb, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.