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Volumn 89, Issue 17, 2015, Pages 9068-9079

HIV-1 resistance to the capsid-targeting inhibitor PF74 results in altered dependence on host factors required for virus nuclear entry

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; PF 74; PROTEIN INHIBITOR; UNCLASSIFIED DRUG; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; CHAPERONE; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR; CLEAVAGE FACTOR IM, HUMAN; INDOLE DERIVATIVE; KARYOPHERIN BETA; NUCLEOPORIN; NUP153 PROTEIN, HUMAN; PF-3450074; PHENYLALANINE; PROTEIN BINDING; RAN-BINDING PROTEIN 2; SMALL INTERFERING RNA; TNPO3 PROTEIN, HUMAN;

EID: 84938937756     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00340-15     Document Type: Article
Times cited : (48)

References (57)
  • 2
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys
    • Stremlau M, Owens CM, Perron MJ, Kiessling M, Autissier P, Sodroski J. 2004. The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature 427:848-853. http://dx.doi.org/10.1038/nature02343.
    • (2004) Nature , vol.427 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5    Sodroski, J.6
  • 3
    • 3242876747 scopus 로고    scopus 로고
    • Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1
    • Sayah DM, Sokolskaja E, Berthoux L, Luban J. 2004. Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1. Nature 430:569-573. http://dx.doi.org/10.1038/nature02777.
    • (2004) Nature , vol.430 , pp. 569-573
    • Sayah, D.M.1    Sokolskaja, E.2    Berthoux, L.3    Luban, J.4
  • 4
    • 4444241947 scopus 로고    scopus 로고
    • A Trim5-cyclophilin A fusion protein found in owl monkey kidney cells can restrict HIV-1
    • Nisole S, Lynch C, Stoye JP, Yap MW. 2004. A Trim5-cyclophilin A fusion protein found in owl monkey kidney cells can restrict HIV-1. Proc Natl Acad Sci U S A 101:13324-13328. http://dx.doi.org/10.1073/pnas.0404640101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13324-13328
    • Nisole, S.1    Lynch, C.2    Stoye, J.P.3    Yap, M.W.4
  • 9
    • 78751670547 scopus 로고    scopus 로고
    • Atomic-level modelling of the HIV capsid
    • Pornillos O, Ganser-Pornillos BK, Yeager M. 2011. Atomic-level modelling of the HIV capsid. Nature 469:424-427. http://dx.doi.org/10.1038/nature09640.
    • (2011) Nature , vol.469 , pp. 424-427
    • Pornillos, O.1    Ganser-Pornillos, B.K.2    Yeager, M.3
  • 12
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B
    • Luban J, Bossolt KL, Franke EK, Kalpana GV, Goff SP. 1993. Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B Cell 73:1067-1078.
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 14
    • 72849130164 scopus 로고    scopus 로고
    • The requirement for cellular transportin 3 (TNPO3 or TRN-SR2) during infection maps to human immunodeficiency virus type 1 capsid and not integrase
    • Krishnan L, Matreyek KA, Oztop I, Lee K, Tipper CH, Li X, Dar MJ, Kewalramani VN, Engelman A. 2010. The requirement for cellular transportin 3 (TNPO3 or TRN-SR2) during infection maps to human immunodeficiency virus type 1 capsid and not integrase. J Virol 84:397-406. http://dx.doi.org/10.1128/JVI.01899-09.
    • (2010) J Virol , vol.84 , pp. 397-406
    • Krishnan, L.1    Matreyek, K.A.2    Oztop, I.3    Lee, K.4    Tipper, C.H.5    Li, X.6    Dar, M.J.7    Kewalramani, V.N.8    Engelman, A.9
  • 15
    • 79960415929 scopus 로고    scopus 로고
    • The requirement for nucleoporin NUP153 during human immunodeficiency virus type 1 infection is determined by the viral capsid
    • Matreyek KA, Engelman A. 2011. The requirement for nucleoporin NUP153 during human immunodeficiency virus type 1 infection is determined by the viral capsid. J Virol 85:7818-7827. http://dx.doi.org/10.1128/JVI.00325-11.
    • (2011) J Virol , vol.85 , pp. 7818-7827
    • Matreyek, K.A.1    Engelman, A.2
  • 16
  • 20
    • 80052336130 scopus 로고    scopus 로고
    • Transportin 3 promotes a nuclear maturation step required for efficient HIV-1 integration
    • Zhou L, Sokolskaja E, Jolly C, James W, Cowley SA, Fassati A. 2011. Transportin 3 promotes a nuclear maturation step required for efficient HIV-1 integration. PLoS Pathog 7:e1002194. http://dx.doi.org/10.1371/journal.ppat.1002194.
    • (2011) PLoS Pathog , vol.7
    • Zhou, L.1    Sokolskaja, E.2    Jolly, C.3    James, W.4    Cowley, S.A.5    Fassati, A.6
  • 21
    • 84893716884 scopus 로고    scopus 로고
    • In vivo functions of CPSF6 for HIV-1 as revealed by HIV-1 capsid evolution in HLA-B27-positive subjects
    • Henning MS, Dubose BN, Burse MJ, Aiken C, Yamashita M. 2014. In vivo functions of CPSF6 for HIV-1 as revealed by HIV-1 capsid evolution in HLA-B27-positive subjects. PLoS Pathog 10:e1003868. http://dx.doi.org/10.1371/journal.ppat.1003868.
    • (2014) PLoS Pathog , vol.10
    • Henning, M.S.1    Dubose, B.N.2    Burse, M.J.3    Aiken, C.4    Yamashita, M.5
  • 23
    • 84890215093 scopus 로고    scopus 로고
    • The capsids of HIV-1 and HIV-2 determine immune detection of the viral cDNA by the innate sensor cGAS in dendritic cells
    • Lahaye X, Satoh T, Gentili M, Cerboni S, Conrad C, Hurbain I, El Marjou A, Lacabaratz C, Lelievre JD, Manel N. 2013. The capsids of HIV-1 and HIV-2 determine immune detection of the viral cDNA by the innate sensor cGAS in dendritic cells. Immunity 39:1132-1142. http://dx.doi.org/10.1016/j.immuni.2013.11.002.
    • (2013) Immunity , vol.39 , pp. 1132-1142
    • Lahaye, X.1    Satoh, T.2    Gentili, M.3    Cerboni, S.4    Conrad, C.5    Hurbain, I.6    El Marjou, A.7    Lacabaratz, C.8    Lelievre, J.D.9    Manel, N.10
  • 32
    • 78650064115 scopus 로고    scopus 로고
    • Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization
    • Shi J, Zhou J, Shah VB, Aiken C, Whitby K. 2011. Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization. J Virol 85:542-549. http://dx.doi.org/10.1128/JVI.01406-10.
    • (2011) J Virol , vol.85 , pp. 542-549
    • Shi, J.1    Zhou, J.2    Shah, V.B.3    Aiken, C.4    Whitby, K.5
  • 33
    • 84924194959 scopus 로고    scopus 로고
    • BI-2 destabilizes HIV-1 cores during infection and prevents binding of CPSF6 to the HIV-1 capsid
    • Fricke T, Buffone C, Opp S, Valle-Casuso J, Diaz-Griffero F. 2014. BI-2 destabilizes HIV-1 cores during infection and prevents binding of CPSF6 to the HIV-1 capsid. Retrovirology 11:120. http://dx.doi.org/10.1186/s12977-014-0120-x.
    • (2014) Retrovirology , vol.11 , pp. 120
    • Fricke, T.1    Buffone, C.2    Opp, S.3    Valle-Casuso, J.4    Diaz-Griffero, F.5
  • 34
    • 84919457878 scopus 로고    scopus 로고
    • Compensatory substitutions in the HIV-1 capsid reduce the fitness cost associated with resistance to a capsidtargeting small-molecule inhibitor
    • Shi J, Zhou J, Halambage UD, Shah VB, Burse MJ, Wu H, Blair WS, Butler SL, Aiken C. 2015. Compensatory substitutions in the HIV-1 capsid reduce the fitness cost associated with resistance to a capsidtargeting small-molecule inhibitor. J Virol 89:208-219. http://dx.doi.org/10.1128/JVI.01411-14.
    • (2015) J Virol , vol.89 , pp. 208-219
    • Shi, J.1    Zhou, J.2    Halambage, U.D.3    Shah, V.B.4    Burse, M.J.5    Wu, H.6    Blair, W.S.7    Butler, S.L.8    Aiken, C.9
  • 35
    • 0030987672 scopus 로고    scopus 로고
    • HIV-1 infection of nondividing cells through the recognition of integrase by the importin/ karyopherin pathway
    • Gallay P, Hope T, Chin D, Trono D. 1997. HIV-1 infection of nondividing cells through the recognition of integrase by the importin/ karyopherin pathway. Proc Natl Acad Sci U S A 94:9825-9830. http://dx.doi.org/10.1073/pnas.94.18.9825.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 9825-9830
    • Gallay, P.1    Hope, T.2    Chin, D.3    Trono, D.4
  • 36
    • 77955557025 scopus 로고    scopus 로고
    • Disulfide bond stabilization of the hexameric capsomer of human immunodeficiency virus
    • Pornillos O, Ganser-Pornillos BK, Banumathi S, Hua Y, Yeager M. 2010. Disulfide bond stabilization of the hexameric capsomer of human immunodeficiency virus. J Mol Biol 401:985-995. http://dx.doi.org/10.1016/j.jmb.2010.06.042.
    • (2010) J Mol Biol , vol.401 , pp. 985-995
    • Pornillos, O.1    Ganser-Pornillos, B.K.2    Banumathi, S.3    Hua, Y.4    Yeager, M.5
  • 38
    • 0030819379 scopus 로고    scopus 로고
    • Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo
    • Zufferey R, Nagy D, Mandel RJ, Naldini L, Trono D. 1997. Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo. Nat Biotechnol 15:871-875. http://dx.doi.org/10.1038/nbt0997-871.
    • (1997) Nat Biotechnol , vol.15 , pp. 871-875
    • Zufferey, R.1    Nagy, D.2    Mandel, R.J.3    Naldini, L.4    Trono, D.5
  • 39
    • 0028705684 scopus 로고
    • Generation of high-titer pseudotyped retroviral with very broad host range
    • Yee JK, Friedmann T, Burns JC. 1994. Generation of high-titer pseudotyped retroviral with very broad host range. Methods Cell Biol 43: 99-112.
    • (1994) Methods Cell Biol , vol.43 , pp. 99-112
    • Yee, J.K.1    Friedmann, T.2    Burns, J.C.3
  • 40
    • 84871947594 scopus 로고    scopus 로고
    • The host proteins transportin SR2/TNPO3 and cyclophilin A exert opposing effects on HIV-1 uncoating
    • Shah VB, Shi J, Hout DR, Oztop I, Krishnan L, Ahn J, Shotwell MS, Engelman A, Aiken C. 2013. The host proteins transportin SR2/TNPO3 and cyclophilin A exert opposing effects on HIV-1 uncoating. J Virol 87:422-432. http://dx.doi.org/10.1128/JVI.07177-11.
    • (2013) J Virol , vol.87 , pp. 422-432
    • Shah, V.B.1    Shi, J.2    Hout, D.R.3    Oztop, I.4    Krishnan, L.5    Ahn, J.6    Shotwell, M.S.7    Engelman, A.8    Aiken, C.9
  • 41
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Anonymous. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50:760-763. http://dx.doi.org/10.1107/S0907444994003112.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 43
    • 84873720427 scopus 로고    scopus 로고
    • TNPO3 protects HIV-1 replication from CPSF6-mediated capsid stabilization in the host cell cytoplasm
    • De Iaco A, Santoni F, Vannier A, Guipponi M, Antonarakis S, Luban J. 2013. TNPO3 protects HIV-1 replication from CPSF6-mediated capsid stabilization in the host cell cytoplasm. Retrovirology 10:20. http://dx.doi.org/10.1186/1742-4690-10-20.
    • (2013) Retrovirology , vol.10 , pp. 20
    • De Iaco, A.1    Santoni, F.2    Vannier, A.3    Guipponi, M.4    Antonarakis, S.5    Luban, J.6
  • 44
    • 84874370905 scopus 로고    scopus 로고
    • The V86M mutation in HIV-1 capsid confers resistance to TRIM5alpha by abrogation of cyclophilin A-dependent restriction and enhancement of viral nuclear import
    • Veillette M, Bichel K, Pawlica P, Freund SM, Plourde MB, Pham QT, Reyes-Moreno C, James LC, Berthoux L. 2013. The V86M mutation in HIV-1 capsid confers resistance to TRIM5alpha by abrogation of cyclophilin A-dependent restriction and enhancement of viral nuclear import. Retrovirology 10:25. http://dx.doi.org/10.1186/1742-4690-10-25.
    • (2013) Retrovirology , vol.10 , pp. 25
    • Veillette, M.1    Bichel, K.2    Pawlica, P.3    Freund, S.M.4    Plourde, M.B.5    Pham, Q.T.6    Reyes-Moreno, C.7    James, L.C.8    Berthoux, L.9
  • 45
    • 84928566555 scopus 로고    scopus 로고
    • Quantitative microscopy of functional HIV post-entry complexes reveals association of replication with the viral capsid
    • Peng K, Muranyi W, Glass B, Laketa V, Yant SR, Tsai L, Cihlar T, Muller B, Krausslich HG. 2014. Quantitative microscopy of functional HIV post-entry complexes reveals association of replication with the viral capsid. eLife 3:e04114. http://dx.doi.org/10.7554/eLife.04114.
    • (2014) eLife , vol.3
    • Peng, K.1    Muranyi, W.2    Glass, B.3    Laketa, V.4    Yant, S.R.5    Tsai, L.6    Cihlar, T.7    Muller, B.8    Krausslich, H.G.9
  • 46
    • 78650776859 scopus 로고    scopus 로고
    • Perturbation of host nuclear membrane component RanBP2 impairs the nuclear import of human immunodeficiency virus-1 preintegration complex (DNA)
    • Zhang R, Mehla R, Chauhan A. 2010. Perturbation of host nuclear membrane component RanBP2 impairs the nuclear import of human immunodeficiency virus-1 preintegration complex (DNA). PLoS One 5:e15620. http://dx.doi.org/10.1371/journal.pone.0015620.
    • (2010) PLoS One , vol.5
    • Zhang, R.1    Mehla, R.2    Chauhan, A.3
  • 47
    • 84885090088 scopus 로고    scopus 로고
    • Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity
    • Matreyek KA, Yucel SS, Li X, Engelman A. 2013. Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity. PLoS Pathog 9:e1003693. http://dx.doi.org/10.1371/journal.ppat.1003693.
    • (2013) PLoS Pathog , vol.9
    • Matreyek, K.A.1    Yucel, S.S.2    Li, X.3    Engelman, A.4
  • 48
    • 84859844937 scopus 로고    scopus 로고
    • Identification of second-site suppressors of human immunodeficiency virus type 1 CA mutants: restoration of intracellular activities without correction of intrinsic capsid stability defects
    • Yang R, Shi J, Byeon I-JL, Ahn J, Sheehan JH, Meiler J, Gronenborn AM, Aiken C. 2012. Identification of second-site suppressors of human immunodeficiency virus type 1 CA mutants: restoration of intracellular activities without correction of intrinsic capsid stability defects. Retrovirology 9:30. http://dx.doi.org/10.1186/1742-4690-9-30.
    • (2012) Retrovirology , vol.9 , pp. 30
    • Yang, R.1    Shi, J.2    Byeon, I.-J.L.3    Ahn, J.4    Sheehan, J.H.5    Meiler, J.6    Gronenborn, A.M.7    Aiken, C.8
  • 50
    • 84855654765 scopus 로고    scopus 로고
    • Mechanism of HIV antiretroviral drugs progress toward drug resistance
    • Ammaranond P, Sanguansittianan S. 2012. Mechanism of HIV antiretroviral drugs progress toward drug resistance. Fundam Clin Pharmacol 26:146-161. http://dx.doi.org/10.1111/j.1472-8206.2011.01009.x.
    • (2012) Fundam Clin Pharmacol , vol.26 , pp. 146-161
    • Ammaranond, P.1    Sanguansittianan, S.2
  • 51
    • 84865375176 scopus 로고    scopus 로고
    • HIV-1 antiretroviral drug therapy
    • Arts EJ, Hazuda DJ. 2012. HIV-1 antiretroviral drug therapy. Cold Spring Harb Perspect Med 2:a007161. http://dx.doi.org/10.1101/cshperspect.a007161.
    • (2012) Cold Spring Harb Perspect Med , vol.2
    • Arts, E.J.1    Hazuda, D.J.2
  • 52
    • 84887394848 scopus 로고    scopus 로고
    • Functional conservation of HIV-1 Gag: implications for rational drug design
    • Li G, Verheyen J, Rhee SY, Voet A, Vandamme AM, Theys K. 2013. Functional conservation of HIV-1 Gag: implications for rational drug design. Retrovirology 10:126. http://dx.doi.org/10.1186/1742-4690-10-126.
    • (2013) Retrovirology , vol.10 , pp. 126
    • Li, G.1    Verheyen, J.2    Rhee, S.Y.3    Voet, A.4    Vandamme, A.M.5    Theys, K.6
  • 54
    • 0028109679 scopus 로고
    • Distribution of drug resistance mutations in type 3 poliovirus identifies three regions involved in uncoating functions
    • Mosser AG, Sgro JY, Rueckert RR. 1994. Distribution of drug resistance mutations in type 3 poliovirus identifies three regions involved in uncoating functions. J Virol 68:8193-8201.
    • (1994) J Virol , vol.68 , pp. 8193-8201
    • Mosser, A.G.1    Sgro, J.Y.2    Rueckert, R.R.3
  • 55
    • 0027410407 scopus 로고
    • WIN 51711-dependent mutants of poliovirus type 3: evidence that virions decay after release from cells unless drug is present
    • Mosser AG, Rueckert RR. 1993. WIN 51711-dependent mutants of poliovirus type 3: evidence that virions decay after release from cells unless drug is present. J Virol 67:1246-1254.
    • (1993) J Virol , vol.67 , pp. 1246-1254
    • Mosser, A.G.1    Rueckert, R.R.2
  • 56
    • 0030011638 scopus 로고    scopus 로고
    • Spontaneous mutations in the human immunodeficiency virus type 1 gag gene that affect viral replication in the presence of cyclosporins
    • Aberham C, Weber S, Phares W. 1996. Spontaneous mutations in the human immunodeficiency virus type 1 gag gene that affect viral replication in the presence of cyclosporins. J Virol 70:3536-3544.
    • (1996) J Virol , vol.70 , pp. 3536-3544
    • Aberham, C.1    Weber, S.2    Phares, W.3
  • 57
    • 0029895725 scopus 로고    scopus 로고
    • Cyclosporine A-resistant human immunodeficiency virus type 1 mutants demonstrate that Gag encodes the functional target of cyclophilin
    • Braaten D, Aberham C, Franke EK, Yin L, Phares W, Luban J. 1996. Cyclosporine A-resistant human immunodeficiency virus type 1 mutants demonstrate that Gag encodes the functional target of cyclophilin A J Virol 70:5170-5176.
    • (1996) A J Virol , vol.70 , pp. 5170-5176
    • Braaten, D.1    Aberham, C.2    Franke, E.K.3    Yin, L.4    Phares, W.5    Luban, J.6


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