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Volumn 84, Issue 11, 2010, Pages 5741-5750

Identification of 81LGxGxxIxW89 and 171EDRW174 domains from human immunodeficiency virus type 1 Vif that regulate APOBEC3G and APOBEC3F neutralizing activity

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3F; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; NEUTRALIZING ANTIBODY; PEPTIDE DERIVATIVE; VIF PROTEIN; APOBEC3F PROTEIN, HUMAN; APOBEC3G PROTEIN, HUMAN; CYTIDINE DEAMINASE; CYTOSINE DEAMINASE; UBIQUITIN PROTEIN LIGASE; VIF PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 77951993429     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00079-10     Document Type: Article
Times cited : (50)

References (38)
  • 2
    • 69249215357 scopus 로고    scopus 로고
    • A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G
    • Chen, G., Z. He, T. Wang, R. Xu, and X. F. Yu. 2009. A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G. J. Virol. 83:8674-8682.
    • (2009) J. Virol. , vol.83 , pp. 8674-8682
    • Chen, G.1    He, Z.2    Wang, T.3    Xu, R.4    Yu, X.F.5
  • 3
    • 45549100648 scopus 로고    scopus 로고
    • Human cytidine deaminase APOBEC3H restricts HIV-1 replication
    • Dang, Y., L. M. Siew, X. Wang, Y. Han, R. Lampen, and Y. H. Zheng. 2008. Human cytidine deaminase APOBEC3H restricts HIV-1 replication. J. Biol. Chem. 283:11606-11614.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11606-11614
    • Dang, Y.1    Siew, L.M.2    Wang, X.3    Han, Y.4    Lampen, R.5    Zheng, Y.H.6
  • 4
    • 45149106103 scopus 로고    scopus 로고
    • APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated
    • Dang, Y., L. M. Siew, and Y. H. Zheng. 2008. APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated. J. Biol. Chem. 283:13124-13131.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13124-13131
    • Dang, Y.1    Siew, L.M.2    Zheng, Y.H.3
  • 5
    • 33750344250 scopus 로고    scopus 로고
    • Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family
    • DOI 10.1128/JVI.01123-06
    • Dang, Y., X. Wang, W. J. Esselman, and Y. H. Zheng. 2006. Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J. Virol. 80:10522-10533. (Pubitemid 44628899)
    • (2006) Journal of Virology , vol.80 , Issue.21 , pp. 10522-10533
    • Dang, Y.1    Wang, X.2    Esselman, W.J.3    Zheng, Y.-H.4
  • 6
    • 69249220263 scopus 로고    scopus 로고
    • Identification of a novel WXSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization
    • Dang, Y., X. Wang, T. Zhou, I. A. York, and Y. H. Zheng. 2009. Identification of a novel WXSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization. J. Virol. 83:8544-8552.
    • (2009) J. Virol. , vol.83 , pp. 8544-8552
    • Dang, Y.1    Wang, X.2    Zhou, T.3    York, I.A.4    Zheng, Y.H.5
  • 7
    • 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., A. Schafer, and B. R. Cullen. 2005. Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif. Virology 339:281-288.
    • (2005) Virology , vol.339 , pp. 281-288
    • Doehle, B.P.1    Schafer, A.2    Cullen, B.R.3
  • 8
    • 48449104748 scopus 로고    scopus 로고
    • Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction
    • He, Z., W. Zhang, G. Chen, R. Xu, and X. F. Yu. 2008. Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction. J. Mol. Biol. 381:1000-1011.
    • (2008) J. Mol. Biol. , vol.381 , pp. 1000-1011
    • He, Z.1    Zhang, W.2    Chen, G.3    Xu, R.4    Yu, X.F.5
  • 9
    • 34247111953 scopus 로고    scopus 로고
    • Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and virion encapsidation
    • DOI 10.1128/JVI.02795-06
    • Huthoff, H., and M. H. Malim. 2007. Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and virion encapsidation. J. Virol. 81:3807-3815. (Pubitemid 46586878)
    • (2007) Journal of Virology , vol.81 , Issue.8 , pp. 3807-3815
    • Huthoff, H.1    Malim, M.H.2
  • 10
    • 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
    • DOI 10.1128/JVI.77.21.11398-11407.2003
    • 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. (Pubitemid 37271638)
    • (2003) Journal of Virology , vol.77 , Issue.21 , pp. 11398-11407
    • Kao, S.1    Khan, M.A.2    Miyagi, E.3    Plishka, R.4    Buckler-White, A.5    Strebel, K.6
  • 11
    • 18144374907 scopus 로고    scopus 로고
    • Production of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cells
    • DOI 10.1186/1742-4690-1-27
    • Kao, S., E. Miyagi, M. A. Khan, H. Takeuchi, S. Opi, R. Goila-Gaur, and K. Strebel. 2004. Production of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cells. Retrovirology 1:27. (Pubitemid 40617944)
    • (2004) Retrovirology , vol.1 , pp. 27
    • Kao, S.1    Miyagi, E.2    Khan, M.A.3    Takeuchi, H.4    Opi, S.5    Goila-Gaur, R.6    Strebel, K.7
  • 12
    • 34247623286 scopus 로고    scopus 로고
    • Population stratification of a common APOBEC gene deletion polymorphism
    • Kidd, J. M., T. L. Newman, E. Tuzun, R. Kaul, and E. E. Eichler. 2007. Population stratification of a common APOBEC gene deletion polymorphism. PLoS Genet. 3:e63.
    • (2007) PLoS Genet. , vol.3
    • Kidd, J.M.1    Newman, T.L.2    Tuzun, E.3    Kaul, R.4    Eichler, E.E.5
  • 13
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • Liddament, M. T., W. L. Brown, A. J. Schumacher, and R. S. Harris. 2004. APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo. Curr. Biol. 14:1385-1391.
    • (2004) Curr. Biol. , vol.14 , pp. 1385-1391
    • Liddament, M.T.1    Brown, W.L.2    Schumacher, A.J.3    Harris, R.S.4
  • 14
    • 23844473725 scopus 로고    scopus 로고
    • Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G
    • Luo, K., Z. Xiao, E. Ehrlich, Y. Yu, B. Liu, S. Zheng, and X. F. Yu. 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. 102:11444-11449.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 11444-11449
    • Luo, K.1    Xiao, Z.2    Ehrlich, E.3    Yu, Y.4    Liu, B.5    Zheng, S.6    Yu, X.F.7
  • 15
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin, M., K. M. Rose, S. L. Kozak, and D. Kabat. 2003. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat. Med. 9:1398-1403.
    • (2003) Nat. Med. , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 16
    • 10044230343 scopus 로고    scopus 로고
    • Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation
    • DOI 10.1101/gad.1249904
    • Mehle, A., J. Goncalves, M. Santa-Marta, M. McPike, and D. Gabuzda. 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. (Pubitemid 39602304)
    • (2004) Genes and Development , vol.18 , Issue.23 , pp. 2861-2866
    • Mehle, A.1    Goncalves, J.2    Santa-Marta, M.3    McPike, M.4    Gabuzda, D.5
  • 17
    • 33745225450 scopus 로고    scopus 로고
    • A zinc-binding region in Vif binds Cul5 and determines Cullin selection
    • Mehle, A., E. R. Thomas, K. S. Rajendran, and D. Gabuzda. 2006. A zinc-binding region in Vif binds Cul5 and determines Cullin selection. J. Biol. Chem. 281:17259-17265.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17259-17265
    • Mehle, A.1    Thomas, E.R.2    Rajendran, K.S.3    Gabuzda, D.4
  • 18
    • 77950487440 scopus 로고    scopus 로고
    • Host restriction of HIV-1 by APOBEC3 and viral evasion through Vif
    • Niewiadomska, A. M., and X. F. Yu. 2009. Host restriction of HIV-1 by APOBEC3 and viral evasion through Vif. Curr. Top. Microbiol. Immunol. 339:1-25.
    • (2009) Curr. Top. Microbiol. Immunol. , vol.339 , pp. 1-25
    • Niewiadomska, A.M.1    Yu, X.F.2
  • 19
    • 50849100134 scopus 로고    scopus 로고
    • Antiretroelement activity of APOBEC3H was lost twice in recent human evolution
    • OhAinle, M., J. A. Kerns, M. M. Li, H. S. Malik, and M. Emerman. 2008. Antiretroelement activity of APOBEC3H was lost twice in recent human evolution. Cell Host Microbe 4:249-259.
    • (2008) Cell Host Microbe , vol.4 , pp. 249-259
    • Ohainle, M.1    Kerns, J.A.2    Li, M.M.3    Malik, H.S.4    Emerman, M.5
  • 20
    • 33645760962 scopus 로고    scopus 로고
    • Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H
    • OhAinle, M., J. A. Kerns, H. S. Malik, and M. Emerman. 2006. Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H. J. Virol. 80:3853-3862.
    • (2006) J. Virol. , vol.80 , pp. 3853-3862
    • Ohainle, M.1    Kerns, J.A.2    Malik, H.S.3    Emerman, M.4
  • 21
    • 60049098639 scopus 로고    scopus 로고
    • Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif
    • Pery, E., K. S. Rajendran, A. J. Brazier, and D. Gabuzda. 2009. Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif. J. Virol. 83:2374-2381.
    • (2009) J. Virol. , vol.83 , pp. 2374-2381
    • Pery, E.1    Rajendran, K.S.2    Brazier, A.J.3    Gabuzda, D.4
  • 22
    • 34547119261 scopus 로고    scopus 로고
    • Identification of two distinct human immunodeficiency virus type 1 vif determinants critical for interactions with human APOBEC3G and APOBEC3F
    • DOI 10.1128/JVI.00395-07
    • Russell, R. A., and V. K. Pathak. 2007. Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F. J. Virol. 81:8201-8210. (Pubitemid 47101506)
    • (2007) Journal of Virology , vol.81 , Issue.15 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 23
    • 59649118427 scopus 로고    scopus 로고
    • Distinct domains within APOBEC3G and APOBEC3F interact with separate regions of human immunodeficiency virus type 1 Vif
    • Russell, R. A., J. Smith, R. Barr, D. Bhattacharyya, and V. K. Pathak. 2009. Distinct domains within APOBEC3G and APOBEC3F interact with separate regions of human immunodeficiency virus type 1 Vif. J. Virol. 83:1992-2003.
    • (2009) J. Virol. , vol.83 , pp. 1992-2003
    • Russell, R.A.1    Smith, J.2    Barr, R.3    Bhattacharyya, D.4    Pathak, V.K.5
  • 24
    • 15744387175 scopus 로고    scopus 로고
    • 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
    • Santa-Marta, M., F. A. da Silva, A. M. Fonseca, and J. Goncalves. 2005. 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. Biol. Chem. 280:8765-8775.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8765-8775
    • Santa-Marta, M.1    Da Silva, F.A.2    Fonseca, A.M.3    Goncalves, J.4
  • 25
    • 33744939997 scopus 로고    scopus 로고
    • Mutational alteration of human immunodeficiency virus type 1 vif allows for functional interaction with nonhuman primate APOBEC3G
    • DOI 10.1128/JVI.00388-06
    • Schröfelbauer, B., T. Senger, G. Manning, and N. R. Landau. 2006. Mutational alteration of human immunodeficiency virus type 1 Vif allows for functional interaction with nonhuman primate APOBEC3G. J. Virol. 80:5984-5991. (Pubitemid 43849176)
    • (2006) Journal of Virology , vol.80 , Issue.12 , pp. 5984-5991
    • Schrofelbauer, B.1    Senger, T.2    Manning, G.3    Landau, N.R.4
  • 26
    • 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
  • 27
    • 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
  • 29
    • 70449629709 scopus 로고    scopus 로고
    • Multiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development
    • Smith, J. L., W. Bu, R. C. Burdick, and V. K. Pathak. 2009. Multiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development. Trends Pharmacol. Sci. 30:638-646.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 638-646
    • Smith, J.L.1    Bu, W.2    Burdick, R.C.3    Pathak, V.K.4
  • 30
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • DOI 10.1016/S1097-2765(03)00353-8
    • Stopak, K., C. de Noronha, W. Yonemoto, and W. C. Greene. 2003. HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol. Cell 12:591-601. (Pubitemid 37222482)
    • (2003) Molecular Cell , vol.12 , Issue.3 , pp. 591-601
    • Stopak, K.1    De Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 31
    • 70350738592 scopus 로고    scopus 로고
    • Human cellular restriction factors that target HIV-1 replication
    • Strebel, K., J. Luban, and K. T. Jeang. 2009. Human cellular restriction factors that target HIV-1 replication. BMC Med. 7:48.
    • (2009) BMC Med. , vol.7 , pp. 48
    • Strebel, K.1    Luban, J.2    Jeang, K.T.3
  • 32
    • 33847261162 scopus 로고    scopus 로고
    • Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycle
    • Wang, X., P. T. Dolan, Y. Dang, and Y. H. Zheng. 2007. Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycle. J. Biol. Chem. 282:1585-1594.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1585-1594
    • Wang, X.1    Dolan, P.T.2    Dang, Y.3    Zheng, Y.H.4
  • 33
    • 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., B. P. Doehle, H. P. Bogerd, and B. R. Cullen. 2004. A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J. 23:2451-2458.
    • (2004) EMBO J. , vol.23 , pp. 2451-2458
    • Wiegand, H.L.1    Doehle, B.P.2    Bogerd, H.P.3    Cullen, B.R.4
  • 34
    • 33646866382 scopus 로고    scopus 로고
    • Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif
    • Xiao, Z., E. Ehrlich, Y. Yu, K. Luo, T. Wang, C. Tian, and X. F. Yu. 2006. Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif. Virology 349:290-299.
    • (2006) Virology , vol.349 , pp. 290-299
    • Xiao, Z.1    Ehrlich, E.2    Yu, Y.3    Luo, K.4    Wang, T.5    Tian, C.6    Yu, X.F.7
  • 35
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu, X., Y. Yu, B. Liu, K. Luo, W. Kong, P. Mao, and X. F. Yu. 2003. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 302:1056-1060.
    • (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
  • 36
    • 10044228286 scopus 로고    scopus 로고
    • Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines
    • Yu, Y., Z. Xiao, E. S. Ehrlich, X. Yu, and X. F. 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. 18:2867-2872.
    • (2004) Genes Dev. , vol.18 , pp. 2867-2872
    • Yu, Y.1    Xiao, Z.2    Ehrlich, E.S.3    Yu, X.4    Yu, X.F.5
  • 37
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • Zheng, Y. H., D. Irwin, T. Kurosu, K. Tokunaga, T. Sata, and B. M. Peterlin. 2004. Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J. Virol. 78:6073-6076.
    • (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
  • 38
    • 65749106717 scopus 로고    scopus 로고
    • A novel HIV-1 restriction factor that is biologically distinct from APOBEC3 cytidine deaminases in a human T cell line CEM.NKR
    • Zhou, T., Y. Han, Y. Dang, X. Wang, and Y. H. Zheng. 2009. A novel HIV-1 restriction factor that is biologically distinct from APOBEC3 cytidine deaminases in a human T cell line CEM.NKR. Retrovirology 6:31.
    • (2009) Retrovirology , vol.6 , pp. 31
    • Zhou, T.1    Han, Y.2    Dang, Y.3    Wang, X.4    Zheng, Y.H.5


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