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Volumn 364, Issue 2, 2007, Pages 486-493

The intrinsic antiretroviral factor APOBEC3B contains two enzymatically active cytidine deaminase domains

Author keywords

APOBEC3G; DNA editing; HIV 1; Intrinsic immunity

Indexed keywords

CYTIDINE DEAMINASE; MUTANT PROTEIN; VIRUS DNA;

EID: 34249892197     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2007.03.019     Document Type: Article
Times cited : (59)

References (44)
  • 1
    • 4544232464 scopus 로고    scopus 로고
    • APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein
    • Alce T.M., and Popik W. APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein. J. Biol. Chem. 279 (2004) 34083-34086
    • (2004) J. Biol. Chem. , vol.279 , pp. 34083-34086
    • Alce, T.M.1    Popik, W.2
  • 2
    • 1542328859 scopus 로고    scopus 로고
    • Comparison of the differential context-dependence of DNA deamination by APOBEC enzymes: correlation with mutation spectra in vivo
    • Beale R.C.L., Petersen-Mahrt S.K., Watt I.N., Harris R.S., Rada C., and Neuberger M.S. Comparison of the differential context-dependence of DNA deamination by APOBEC enzymes: correlation with mutation spectra in vivo. J. Mol. Biol. 337 (2004) 585-596
    • (2004) J. Mol. Biol. , vol.337 , pp. 585-596
    • Beale, R.C.L.1    Petersen-Mahrt, S.K.2    Watt, I.N.3    Harris, R.S.4    Rada, C.5    Neuberger, M.S.6
  • 3
    • 0028057520 scopus 로고
    • Cytidine deaminase. The 2·3 Å crystal structure of an enzyme: transition-state analog complex
    • Betts L., Xiang S., Short S.A., Wolfenden R., and Carter Jr. C.W. Cytidine deaminase. The 2·3 Å crystal structure of an enzyme: transition-state analog complex. J. Mol. Biol. 235 (1994) 635-656
    • (1994) J. Mol. Biol. , vol.235 , pp. 635-656
    • Betts, L.1    Xiang, S.2    Short, S.A.3    Wolfenden, R.4    Carter Jr., C.W.5
  • 5
    • 33748640960 scopus 로고    scopus 로고
    • Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
    • Bishop K.N., Holmes R.K., and Malim M.H. Antiviral potency of APOBEC proteins does not correlate with cytidine deamination. J. Virol. 80 (2006) 8450-8458
    • (2006) J. Virol. , vol.80 , pp. 8450-8458
    • Bishop, K.N.1    Holmes, R.K.2    Malim, M.H.3
  • 6
    • 31644442239 scopus 로고    scopus 로고
    • APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells
    • Bogerd H.P., Wiegand H.L., Doehle B.P., Lueders K.K., and Cullen B.R. APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells. Nucleic Acids Res. 34 (2006) 89-95
    • (2006) Nucleic Acids Res. , vol.34 , pp. 89-95
    • Bogerd, H.P.1    Wiegand, H.L.2    Doehle, B.P.3    Lueders, K.K.4    Cullen, B.R.5
  • 10
    • 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., Wehrly K., Nishio J., and Perryman S. 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 (1992) 6547-6554
    • (1992) J. Virol. , vol.66 , pp. 6547-6554
    • Chesebro, B.1    Wehrly, K.2    Nishio, J.3    Perryman, S.4
  • 11
    • 0242709301 scopus 로고    scopus 로고
    • The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G
    • Conticello S.G., Harris R.S., and Neuberger M.S. The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G. Curr. Biol. 13 (2003) 2009-2013
    • (2003) Curr. Biol. , vol.13 , pp. 2009-2013
    • Conticello, S.G.1    Harris, R.S.2    Neuberger, M.S.3
  • 12
    • 31144469701 scopus 로고    scopus 로고
    • Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors
    • Cullen B.R. Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors. J. Virol. 80 (2006) 1067-1076
    • (2006) J. Virol. , vol.80 , pp. 1067-1076
    • Cullen, B.R.1
  • 13
    • 33750344250 scopus 로고    scopus 로고
    • Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family
    • Dang Y., Wang X., Esselman W.J., and Zheng Y.-H. Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J. Virol. 80 (2006) 10522-10533
    • (2006) J. Virol. , vol.80 , pp. 10522-10533
    • Dang, Y.1    Wang, X.2    Esselman, W.J.3    Zheng, Y.-H.4
  • 14
    • 23844483541 scopus 로고    scopus 로고
    • Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif
    • Doehle B.P., Schäfer A., and Cullen B.R. Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif. Virology 339 (2005) 281-288
    • (2005) Virology , vol.339 , pp. 281-288
    • Doehle, B.P.1    Schäfer, A.2    Cullen, B.R.3
  • 15
    • 15744390742 scopus 로고    scopus 로고
    • The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain
    • Haché G., Liddament M.T., and Harris R.S. The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain. J. Biol. Chem. 280 (2005) 10920-10924
    • (2005) J. Biol. Chem. , vol.280 , pp. 10920-10924
    • Haché, G.1    Liddament, M.T.2    Harris, R.S.3
  • 16
    • 33846031136 scopus 로고    scopus 로고
    • Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains
    • Hakata Y., and Landau N.R. Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains. J. Biol. Chem. 281 (2006) 36624-36631
    • (2006) J. Biol. Chem. , vol.281 , pp. 36624-36631
    • Hakata, Y.1    Landau, N.R.2
  • 18
    • 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., Koning F.A., Bishop K.N., and Malim M.H. APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation: comparisons with APOBEC3G. J. Biol. Chem. 282 (2007) 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
  • 22
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • Liddament M.T., Brown W.L., Schumacher A.J., and Harris R.S. APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo. Curr. Biol. 14 (2004) 1385-1391
    • (2004) Curr. Biol. , vol.14 , pp. 1385-1391
    • Liddament, M.T.1    Brown, W.L.2    Schumacher, A.J.3    Harris, R.S.4
  • 23
    • 22544465590 scopus 로고    scopus 로고
    • Regulation of APOBEC3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase
    • Liu B., Sarkis P.T.N., Luo K., Yu Y., and Yu X.-F. Regulation of APOBEC3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase. J. Virol. 79 (2005) 9579-9587
    • (2005) J. Virol. , vol.79 , pp. 9579-9587
    • Liu, B.1    Sarkis, P.T.N.2    Luo, K.3    Yu, Y.4    Yu, X.-F.5
  • 24
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat B., Turelli P., Caron G., Friedli M., Perrin L., and Trono D. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424 (2003) 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
  • 25
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin M., Rose K.M., Kozak S.L., and Kabat D. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat. Med. 9 (2003) 1398-1403
    • (2003) Nat. Med. , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 26
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle A., Strack B., Ancuta P., Zhang C., McPike M.N., and Gabuzda D. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J. Biol. Chem. 279 (2004) 7792-7798
    • (2004) J. Biol. Chem. , vol.279 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3    Zhang, C.4    McPike, M.N.5    Gabuzda, D.6
  • 30
    • 33645760962 scopus 로고    scopus 로고
    • Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H
    • OhAinle M., Kerns J.A., Malik H.S., and Emerman M. Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H. J. Virol. 80 (2006) 3853-3862
    • (2006) J. Virol. , vol.80 , pp. 3853-3862
    • OhAinle, M.1    Kerns, J.A.2    Malik, H.S.3    Emerman, M.4
  • 31
    • 5344222683 scopus 로고    scopus 로고
    • Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor
    • Schäfer A., Bogerd H.P., and Cullen B.R. Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor. Virology 328 (2004) 163-168
    • (2004) Virology , vol.328 , pp. 163-168
    • Schäfer, A.1    Bogerd, H.P.2    Cullen, B.R.3
  • 32
    • 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., Gaddis N.C., Choi J.D., and Malim M.H. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418 (2002) 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
  • 33
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy A.M., Gaddis N.C., and Malim M.H. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat. Med. 9 (2003) 1404-1407
    • (2003) Nat. Med. , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 34
    • 0242497878 scopus 로고    scopus 로고
    • Shindo, K., Takaori-Kondo, A., Kobayashi, M., Abudu, A., Fukunaga, K., Uchiyama T. 2003, The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity. 278, 44412-44416.
  • 35
    • 33745184896 scopus 로고    scopus 로고
    • APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism
    • Stenglein M.D., and Harris R.S. APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism. J. Biol. Chem. 281 (2006) 16837-16841
    • (2006) J. Biol. Chem. , vol.281 , pp. 16837-16841
    • Stenglein, M.D.1    Harris, R.S.2
  • 36
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • Stopak K., de Noronha C., Yonemoto W., and Greene W.C. HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol. Cell 12 (2003) 591-601
    • (2003) Mol. Cell , vol.12 , pp. 591-601
    • Stopak, K.1    de Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 38
    • 3242712200 scopus 로고    scopus 로고
    • A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
    • Wiegand H.L., Doehle B.P., Bogerd H.P., and Cullen B.R. A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J. 23 (2004) 2451-2458
    • (2004) EMBO J. , vol.23 , pp. 2451-2458
    • Wiegand, H.L.1    Doehle, B.P.2    Bogerd, H.P.3    Cullen, B.R.4
  • 39
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu X., Yu Y., Liu B., Luo K., Kong W., Mao P., and Yu X.-F. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 302 (2003) 1056-1060
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5    Mao, P.6    Yu, X.-F.7
  • 40
    • 11144244647 scopus 로고    scopus 로고
    • APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication
    • Yu Q., Chen D., König R., Mariani R., Unutmaz D., and Landau N.R. APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication. J. Biol. Chem. 279 (2004) 53379-53386
    • (2004) J. Biol. Chem. , vol.279 , pp. 53379-53386
    • Yu, Q.1    Chen, D.2    König, R.3    Mariani, R.4    Unutmaz, D.5    Landau, N.R.6
  • 42
    • 6344294871 scopus 로고    scopus 로고
    • APOBEC3G incorporation into human immunodeficiency virus type 1 particles
    • Zennou V., Perez-Caballero D., Göttlinger H., and Bieniasz P.D. APOBEC3G incorporation into human immunodeficiency virus type 1 particles. J. Virol. 78 (2004) 12058-12061
    • (2004) J. Virol. , vol.78 , pp. 12058-12061
    • Zennou, V.1    Perez-Caballero, D.2    Göttlinger, H.3    Bieniasz, P.D.4
  • 43
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang H., Yang B., Pomerantz R.J., Zhang C., Arunachalam S.C., and Gao L. The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424 (2003) 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
  • 44
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • Zheng Y.-H., Irwin D., Kurosu T., Tokunaga K., Sata T., and Peterlin B.M. Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J. Virol. 78 (2004) 6073-6076
    • (2004) J. Virol. , vol.78 , pp. 6073-6076
    • Zheng, Y.-H.1    Irwin, D.2    Kurosu, T.3    Tokunaga, K.4    Sata, T.5    Peterlin, B.M.6


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