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Volumn 55, Issue 3, 2011, Pages 1106-1113

Three residues in HIV-1 matrix contribute to protease inhibitor susceptibility and replication capacity

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE INHIBITOR; MATRIX PROTEIN;

EID: 79952327508     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01228-10     Document Type: Article
Times cited : (31)

References (35)
  • 1
    • 0035182556 scopus 로고    scopus 로고
    • In vivo gene transfer to the mouse eye using an HIV-based lentiviral vector; efficient long-term transduction of corneal endothelium and retinal pigment epithelium
    • Bainbridge, J. W., et al. 2001. In vivo gene transfer to the mouse eye using an HIV-based lentiviral vector; efficient long-term transduction of corneal endothelium and retinal pigment epithelium. Gene Ther. 8:1665-1668.
    • (2001) Gene Ther. , vol.8 , pp. 1665-1668
    • Bainbridge, J.W.1
  • 2
    • 0030065565 scopus 로고    scopus 로고
    • Resistance of human immunodeficiency virus type 1 to protease inhibitors: Selection of resistance mutations in the presence and absence of the drug
    • Borman, A. M., S. Paulous, and F. Clavel. 1996. Resistance of human immunodeficiency virus type 1 to protease inhibitors: selection of resistance mutations in the presence and absence of the drug. J. Gen. Virol. 77:419-426.
    • (1996) J. Gen. Virol. , vol.77 , pp. 419-426
    • Borman, A.M.1    Paulous, S.2    Clavel, F.3
  • 4
    • 0028943992 scopus 로고
    • In vivo emergence of HIV-1 variants resistant to multiple protease inhibitors
    • Condra, J. H., et al. 1995. In vivo emergence of HIV-1 variants resistant to multiple protease inhibitors. Nature 374:569-571.
    • (1995) Nature , vol.374 , pp. 569-571
    • Condra, J.H.1
  • 5
    • 0031015475 scopus 로고    scopus 로고
    • Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors
    • Croteau, G., et al. 1997. Impaired fitness of human immunodeficiency virus type 1 variants with high-level resistance to protease inhibitors. J. Virol. 71:1089-1096. (Pubitemid 27030280)
    • (1997) Journal of Virology , vol.71 , Issue.2 , pp. 1089-1096
    • Croteau, G.1    Doyon, L.2    Thibeault, D.3    Mckercher, G.4    Pilote, L.5    Lamarre, D.6
  • 6
    • 63449110982 scopus 로고    scopus 로고
    • Gag mutations strongly contribute to HIV-1 resistance to protease inhibitors in highly drug-experienced patients besides compensating for fitness loss
    • Dam, E., et al. 2009. Gag mutations strongly contribute to HIV-1 resistance to protease inhibitors in highly drug-experienced patients besides compensating for fitness loss. PLoS Pathog. 5:e1000345.
    • (2009) PLoS Pathog. , vol.5
    • Dam, E.1
  • 8
    • 67649910479 scopus 로고    scopus 로고
    • Protease inhibitor resistance analysis in the MONARK trial comparing first-line lopinavir-ritonavir monotherapy to lopinavir-ritonavir plus zidovudine and lamivudine triple therapy
    • Delaugerre, C., et al. 2009. Protease inhibitor resistance analysis in the MONARK trial comparing first-line lopinavir-ritonavir monotherapy to lopinavir-ritonavir plus zidovudine and lamivudine triple therapy. Antimicrob. Agents Chemother. 53:2934-2939.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 2934-2939
    • Delaugerre, C.1
  • 10
    • 0037155193 scopus 로고    scopus 로고
    • Amino acid substitutions in Gag protein at non-cleavage sites are indispensable for the development of a high multitude of HIV-1 resistance against protease inhibitors
    • Gatanaga, H., et al. 2002. Amino acid substitutions in Gag protein at non-cleavage sites are indispensable for the development of a high multitude of HIV-1 resistance against protease inhibitors. J. Biol. Chem. 277:5952-5961.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5952-5961
    • Gatanaga, H.1
  • 11
    • 52749083531 scopus 로고    scopus 로고
    • British HIV Association guidelines for the treatment of HIV-1-infected adults with antiretroviral therapy 2008
    • Gazzard, B. G., et al. 2008. British HIV Association guidelines for the treatment of HIV-1-infected adults with antiretroviral therapy 2008. HIV Med. 9:563-608.
    • (2008) HIV Med. , vol.9 , pp. 563-608
    • Gazzard, B.G.1
  • 12
    • 77954324656 scopus 로고    scopus 로고
    • Full-length HIV-1 Gag determines protease inhibitor susceptibility within in-vitro assays
    • Gupta, R. K., et al. 2010. Full-length HIV-1 Gag determines protease inhibitor susceptibility within in-vitro assays. AIDS 24:1651-1655.
    • (2010) AIDS , vol.24 , pp. 1651-1655
    • Gupta, R.K.1
  • 13
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: Implications for membrane association and assembly
    • Hill, C. P., D. Worthylake, D. P. Bancroft, A. M. Christensen, and W. I. Sundquist. 1996. Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly. Proc. Natl. Acad. Sci. U. S. A. 93:3099-3104.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 14
    • 0002294347 scopus 로고
    • A simple sequentially rejective multiple test procedure
    • Holm, S. 1979. A simple sequentially rejective multiple test procedure. Scand. J. Stat. 6:65-70.
    • (1979) Scand. J. Stat. , vol.6 , pp. 65-70
    • Holm, S.1
  • 15
    • 70350536652 scopus 로고    scopus 로고
    • Impact of amino acid variations in Gag and protease of HIV type 1 CRF01-AE strains on drug susceptibility of virus to protease inhibitors
    • Jinnopat, P., et al. 2009. Impact of amino acid variations in Gag and protease of HIV type 1 CRF01-AE strains on drug susceptibility of virus to protease inhibitors. J. Acquir. Immune. Defic. Syndr. 52:320-328.
    • (2009) J. Acquir. Immune. Defic. Syndr. , vol.52 , pp. 320-328
    • Jinnopat, P.1
  • 16
    • 77955509880 scopus 로고    scopus 로고
    • The role of lysine residue at amino acid position 165 of human immunodeficiency virus type 1 CRF01-AE Gag in reducing viral drug susceptibility to protease inhibitors
    • Kameoka, M., et al. 2010. The role of lysine residue at amino acid position 165 of human immunodeficiency virus type 1 CRF01-AE Gag in reducing viral drug susceptibility to protease inhibitors. Virology 405:129-138.
    • (2010) Virology , vol.405 , pp. 129-138
    • Kameoka, M.1
  • 17
    • 77953789703 scopus 로고    scopus 로고
    • Gag mutations can impact virological response to dual-boosted protease inhibitor combinations in antiretroviral-naive HIV-infected patients
    • Larrouy, L., et al. 2010. Gag mutations can impact virological response to dual-boosted protease inhibitor combinations in antiretroviral-naive HIV-infected patients. Antimicrob. Agents Chemother. 54:2910-2919.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 2910-2919
    • Larrouy, L.1
  • 18
    • 69249216636 scopus 로고    scopus 로고
    • A strongly transdominant mutation in the human immunodeficiency virus type 1 gag gene defines an Achilles heel in the virus life cycle
    • Lee, S. K., J. Harris, and R. Swanstrom. 2009. A strongly transdominant mutation in the human immunodeficiency virus type 1 gag gene defines an Achilles heel in the virus life cycle. J. Virol. 83:8536-8543.
    • (2009) J. Virol. , vol.83 , pp. 8536-8543
    • Lee, S.K.1    Harris, J.2    Swanstrom, R.3
  • 19
    • 21144431528 scopus 로고    scopus 로고
    • Los Alamos National Laboratory, Los Alamos, NM
    • Leitner, T., et al. 2005. HIV sequence compendium 2005. Los Alamos National Laboratory, Los Alamos, NM.
    • (2005) HIV Sequence Compendium 2005
    • Leitner, T.1
  • 20
    • 0032928065 scopus 로고    scopus 로고
    • Replicative fitness of protease inhibitor-resistant mutants of human immunodeficiency virus type 1
    • Martinez-Picado, J., A. V. Savara, L. Sutton, and R. T. D'Aquila. 1999. Replicative fitness of protease inhibitor-resistant mutants of human immunodeficiency virus type 1. J. Virol. 73:3744-3752.
    • (1999) J. Virol. , vol.73 , pp. 3744-3752
    • Martinez-Picado, J.1    Savara, A.V.2    Sutton, L.3    D'Aquila, R.T.4
  • 21
    • 0027987979 scopus 로고
    • Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein
    • Massiah, M. A., et al. 1994. Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein. J. Mol. Biol. 244:198-223.
    • (1994) J. Mol. Biol. , vol.244 , pp. 198-223
    • Massiah, M.A.1
  • 22
    • 15444377672 scopus 로고    scopus 로고
    • Ordered accumulation of mutations in HIV protease confers resistance to ritonavir
    • Molla, A., et al. 1996. Ordered accumulation of mutations in HIV protease confers resistance to ritonavir. Nat. Med. 2:760-766.
    • (1996) Nat. Med. , vol.2 , pp. 760-766
    • Molla, A.1
  • 23
    • 70350366737 scopus 로고    scopus 로고
    • HIV-1 Gag processing intermediates trans-dominantly interfere with HIV-1 infectivity
    • Muller, B., et al. 2009. HIV-1 Gag processing intermediates trans-dominantly interfere with HIV-1 infectivity. J. Biol. Chem. 284:29692-29703.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29692-29703
    • Muller, B.1
  • 24
    • 0942290560 scopus 로고    scopus 로고
    • Gag non-cleavage site mutations contribute to full recovery of viral fitness in protease inhibitor-resistant human immunodeficiency virus type 1
    • Myint, L., et al. 2004. Gag non-cleavage site mutations contribute to full recovery of viral fitness in protease inhibitor-resistant human immunodeficiency virus type 1. Antimicrob. Agents Chemother. 48:444-452.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 444-452
    • Myint, L.1
  • 25
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini, L., et al. 1996. In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272:263-267.
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1
  • 26
    • 0032804864 scopus 로고    scopus 로고
    • Increased fitness of drug resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy
    • Nijhuis, M., et al. 1999. Increased fitness of drug resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy. AIDS 13:2349-2359.
    • (1999) AIDS , vol.13 , pp. 2349-2359
    • Nijhuis, M.1
  • 27
    • 33846702679 scopus 로고    scopus 로고
    • A novel substrate-based HIV-1 protease inhibitor drug resistance mechanism
    • Nijhuis, M., et al. 2007. A novel substrate-based HIV-1 protease inhibitor drug resistance mechanism. PLoS Med. 4:e36.
    • (2007) PLoS Med. , vol.4
    • Nijhuis, M.1
  • 28
    • 69449097224 scopus 로고    scopus 로고
    • Gag determinants of fitness and drug susceptibility in protease inhibitor-resistant human immunodeficiency virus type 1
    • Parry, C. M., et al. 2009. Gag determinants of fitness and drug susceptibility in protease inhibitor-resistant human immunodeficiency virus type 1. J. Virol. 83:9094-9101.
    • (2009) J. Virol. , vol.83 , pp. 9094-9101
    • Parry, C.M.1
  • 29
    • 7644230388 scopus 로고    scopus 로고
    • Structural basis for coevolution of a human immunodeficiency virus type 1 nucleocapsid-p1 cleavage site with a V82A drug-resistant mutation in viral protease
    • Prabu-Jeyabalan, M., E. A. Nalivaika, N. M. King, and C. A. Schiffer. 2004. Structural basis for coevolution of a human immunodeficiency virus type 1 nucleocapsid-p1 cleavage site with a V82A drug-resistant mutation in viral protease. J. Virol. 78:12446-12454.
    • (2004) J. Virol. , vol.78 , pp. 12446-12454
    • Prabu-Jeyabalan, M.1    Nalivaika, E.A.2    King, N.M.3    Schiffer, C.A.4
  • 30
    • 34249660534 scopus 로고    scopus 로고
    • HIV-1 subtype B protease and reverse transcriptase amino acid covariation
    • Rhee, S. Y., T. F. Liu, S. P. Holmes, and R. W. Shafer. 2007. HIV-1 subtype B protease and reverse transcriptase amino acid covariation. PLoS Comput. Biol. 3:e87.
    • (2007) PLoS Comput. Biol. , vol.3
    • Rhee, S.Y.1    Liu, T.F.2    Holmes, S.P.3    Shafer, R.W.4
  • 31
    • 6344249119 scopus 로고    scopus 로고
    • Amino acid insertions near gag cleavage sites restore the otherwise compromised replication of human immunodeficiency virus type 1 variants resistant to protease inhibitors
    • DOI 10.1128/JVI.78.21.12030-12040.2004
    • Tamiya, S., S. Mardy, M. F. Kavlick, K. Yoshimura, and H. Mistuya. 2004. Amino acid insertions near Gag cleavage sites restore the otherwise compromised replication of human immunodeficiency virus type 1 variants resistant to protease inhibitors. J. Virol. 78:12030-12040. (Pubitemid 39390787)
    • (2004) Journal of Virology , vol.78 , Issue.21 , pp. 12030-12040
    • Tamiya, S.1    Mardy, S.2    Kavlick, M.F.3    Yoshimura, K.4    Mistuya, H.5
  • 32
    • 0036294666 scopus 로고    scopus 로고
    • Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
    • Tang, C., Y. Ndassa, and M. F. Summers. 2002. Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nat. Struct. Biol. 9:537-543.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 537-543
    • Tang, C.1    Ndassa, Y.2    Summers, M.F.3
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 52649104801 scopus 로고    scopus 로고
    • Investigating antibody neutralization of lyssaviruses using lentiviral pseudotypes: A cross-species comparison
    • Wright, E., et al. 2008. Investigating antibody neutralization of lyssaviruses using lentiviral pseudotypes: a cross-species comparison. J. Gen. Virol. 89:2204-2213.
    • (2008) J. Gen. Virol. , vol.89 , pp. 2204-2213
    • Wright, E.1
  • 35
    • 0031946007 scopus 로고    scopus 로고
    • Loss of viral fitness associated with multiple Gag and Gag-Pol processing defects in human immunodeficiency virus type 1 variants selected for resistance to protease inhibitors in vivo
    • Zennou, V., F. Mammano, S. Paulous, D. Mathez, and F. Clavel. 1998. Loss of viral fitness associated with multiple Gag and Gag-Pol processing defects in human immunodeficiency virus type 1 variants selected for resistance to protease inhibitors in vivo. J. Virol. 72:3300-3306. (Pubitemid 28175575)
    • (1998) Journal of Virology , vol.72 , Issue.4 , pp. 3300-3306
    • Zennou, V.1    Mammano, F.2    Paulous, S.3    Mathez, D.4    Clavel, F.5


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