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Volumn 29, Issue 1, 2008, Pages 42-49

HIV-1 protease inhibitors: effects on HIV-2 replication and resistance

Author keywords

[No Author keywords available]

Indexed keywords

AMPRENAVIR; AMPRENAVIR PHOSPHATE; ATAZANAVIR; DARUNAVIR; INDINAVIR; ISOLEUCINE; LEUCINE; LOPINAVIR; METHIONINE; NELFINAVIR; PROTEINASE; PROTEINASE INHIBITOR; RITONAVIR; SAQUINAVIR; TIPRANAVIR; VIRUS PROTEIN;

EID: 37549038589     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2007.10.013     Document Type: Review
Times cited : (45)

References (44)
  • 1
    • 0023052240 scopus 로고
    • Isolation of a new retrovirus from West African patients with AIDS
    • Clavel F., et al. Isolation of a new retrovirus from West African patients with AIDS. Science 233 (1986) 343-346
    • (1986) Science , vol.233 , pp. 343-346
    • Clavel, F.1
  • 2
    • 0035663379 scopus 로고    scopus 로고
    • Infection with HIV-2
    • Bock P.J., and Markovitz D.M. Infection with HIV-2. AIDS 15 Suppl. 5 (2001) S35-S45
    • (2001) AIDS , vol.15 , Issue.SUPPL. 5
    • Bock, P.J.1    Markovitz, D.M.2
  • 3
    • 0346881255 scopus 로고    scopus 로고
    • Update on HIV resistance and resistance testing
    • Sebastian J., and Faruki H. Update on HIV resistance and resistance testing. Med. Res. Rev. 24 (2004) 115-125
    • (2004) Med. Res. Rev. , vol.24 , pp. 115-125
    • Sebastian, J.1    Faruki, H.2
  • 4
    • 1542319002 scopus 로고    scopus 로고
    • Susceptibility of HIV-2, SIV and SHIV to various anti-HIV-1 compounds: implications for treatment and postexposure prophylaxis
    • Witvrouw M., et al. Susceptibility of HIV-2, SIV and SHIV to various anti-HIV-1 compounds: implications for treatment and postexposure prophylaxis. Antivir. Ther. 9 (2004) 57-65
    • (2004) Antivir. Ther. , vol.9 , pp. 57-65
    • Witvrouw, M.1
  • 5
    • 2642709177 scopus 로고    scopus 로고
    • Declining morbidity and mortality among patients with advanced human immunodeficiency virus infection
    • Palella Jr. F.J., et al. Declining morbidity and mortality among patients with advanced human immunodeficiency virus infection. N. Engl. J. Med. 338 (1998) 853-860
    • (1998) N. Engl. J. Med. , vol.338 , pp. 853-860
    • Palella Jr., F.J.1
  • 6
    • 0025989978 scopus 로고
    • Comparative analysis of the sequences and structures of HIV-1 and HIV-2 proteases
    • Gustchina A., and Weber I.T. Comparative analysis of the sequences and structures of HIV-1 and HIV-2 proteases. Proteins 10 (1991) 325-339
    • (1991) Proteins , vol.10 , pp. 325-339
    • Gustchina, A.1    Weber, I.T.2
  • 7
    • 34250336893 scopus 로고    scopus 로고
    • HIV-1 protease: Structure dynamics, and inhibition
    • Louis J.M., et al. HIV-1 protease: Structure dynamics, and inhibition. Adv. Pharmacol. 55 (2007) 261-298
    • (2007) Adv. Pharmacol. , vol.55 , pp. 261-298
    • Louis, J.M.1
  • 8
    • 0036369217 scopus 로고    scopus 로고
    • Molecular basis of fidelity of DNA synthesis and nucleotide specificity of retroviral reverse transcriptases
    • Menéndez-Arias L. Molecular basis of fidelity of DNA synthesis and nucleotide specificity of retroviral reverse transcriptases. Prog. Nucleic Acid Res. Mol. Biol. 71 (2002) 91-147
    • (2002) Prog. Nucleic Acid Res. Mol. Biol. , vol.71 , pp. 91-147
    • Menéndez-Arias, L.1
  • 9
    • 1242269308 scopus 로고    scopus 로고
    • Polymorphism and drug selected mutations in the protease gene of human immunodeficiency virus type 2 from patients living in Southern France
    • Colson P., et al. Polymorphism and drug selected mutations in the protease gene of human immunodeficiency virus type 2 from patients living in Southern France. J. Clin. Microbiol. 42 (2004) 570-577
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 570-577
    • Colson, P.1
  • 10
    • 12144290826 scopus 로고    scopus 로고
    • HIV-2 protease sequences of subtypes A and B harbor multiple mutations associated with protease inhibitor resistance in HIV-1
    • Pieniazek D., et al. HIV-2 protease sequences of subtypes A and B harbor multiple mutations associated with protease inhibitor resistance in HIV-1. AIDS 18 (2004) 495-502
    • (2004) AIDS , vol.18 , pp. 495-502
    • Pieniazek, D.1
  • 11
    • 19944429697 scopus 로고    scopus 로고
    • Polymorphism of the human immunodeficiency virus type 2 (HIV-2) protease gene and selection of drug resistance mutations in HIV-2-infected patients treated with protease inhibitors
    • Damond F., et al. Polymorphism of the human immunodeficiency virus type 2 (HIV-2) protease gene and selection of drug resistance mutations in HIV-2-infected patients treated with protease inhibitors. J. Clin. Microbiol. 43 (2005) 484-487
    • (2005) J. Clin. Microbiol. , vol.43 , pp. 484-487
    • Damond, F.1
  • 12
    • 33845458777 scopus 로고    scopus 로고
    • Natural polymorphisms of HIV type 2 pol sequences from drug naive individuals
    • Parreira R., et al. Natural polymorphisms of HIV type 2 pol sequences from drug naive individuals. AIDS Res. Hum. Retroviruses 22 (2006) 1178-1182
    • (2006) AIDS Res. Hum. Retroviruses , vol.22 , pp. 1178-1182
    • Parreira, R.1
  • 13
    • 33846648687 scopus 로고    scopus 로고
    • Natural polymorphisms in the human immunodeficiency virus type 2 protease can accelerate time to development of resistance to protease inhibitors
    • Ntemgwa M., et al. Natural polymorphisms in the human immunodeficiency virus type 2 protease can accelerate time to development of resistance to protease inhibitors. Antimicrob. Agents Chemother. 51 (2007) 604-610
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 604-610
    • Ntemgwa, M.1
  • 14
    • 34848925709 scopus 로고    scopus 로고
    • Genetic polymorphisms and resistance mutations of HIV type 2 in antiretroviral-naïve patients in Burkina Faso
    • Ruelle J., et al. Genetic polymorphisms and resistance mutations of HIV type 2 in antiretroviral-naïve patients in Burkina Faso. AIDS Res. Hum. Retroviruses 23 (2007) 955-964
    • (2007) AIDS Res. Hum. Retroviruses , vol.23 , pp. 955-964
    • Ruelle, J.1
  • 15
    • 4143099182 scopus 로고    scopus 로고
    • Identification of the minimal conserved structure of HIV-1 protease in the presence and absence of drug pressure
    • Ceccherini-Silberstein F., et al. Identification of the minimal conserved structure of HIV-1 protease in the presence and absence of drug pressure. AIDS 18 (2004) F11-F19
    • (2004) AIDS , vol.18
    • Ceccherini-Silberstein, F.1
  • 16
    • 0041488689 scopus 로고    scopus 로고
    • Proteolytic events of HIV-1 replication as targets for therapeutic intervention
    • Tözsér J., and Oroszlan S. Proteolytic events of HIV-1 replication as targets for therapeutic intervention. Curr. Pharm. Des. 9 (2003) 1803-1815
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1803-1815
    • Tözsér, J.1    Oroszlan, S.2
  • 17
    • 0025924419 scopus 로고
    • Studies on the role of the S4 substrate binding site of HIV proteinases
    • Tözsér J., et al. Studies on the role of the S4 substrate binding site of HIV proteinases. FEBS Lett. 279 (1991) 356-360
    • (1991) FEBS Lett. , vol.279 , pp. 356-360
    • Tözsér, J.1
  • 18
    • 0026639427 scopus 로고
    • Kinetic and modeling studies of S3-S3′ subsites of HIV proteinases
    • Tözsér J., et al. Kinetic and modeling studies of S3-S3′ subsites of HIV proteinases. Biochemistry 31 (1992) 4793-4800
    • (1992) Biochemistry , vol.31 , pp. 4793-4800
    • Tözsér, J.1
  • 19
    • 33747479539 scopus 로고    scopus 로고
    • Structure-based design of novel HIV-1 protease inhibitors to combat drug resistance
    • Ghosh A.K., et al. Structure-based design of novel HIV-1 protease inhibitors to combat drug resistance. J. Med. Chem. 49 (2006) 5252-5261
    • (2006) J. Med. Chem. , vol.49 , pp. 5252-5261
    • Ghosh, A.K.1
  • 20
    • 5444247213 scopus 로고    scopus 로고
    • Combating susceptibility to drug resistance: lessons from HIV-1 protease
    • King N.M., et al. Combating susceptibility to drug resistance: lessons from HIV-1 protease. Chem. Biol. 11 (2004) 1333-1338
    • (2004) Chem. Biol. , vol.11 , pp. 1333-1338
    • King, N.M.1
  • 21
    • 0036696712 scopus 로고    scopus 로고
    • Targeting HIV: Antiretroviral therapy and development of drug resistance
    • Menéndez-Arias L. Targeting HIV: Antiretroviral therapy and development of drug resistance. Trends Pharmacol. Sci. 23 (2002) 381-388
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 381-388
    • Menéndez-Arias, L.1
  • 22
    • 35748933494 scopus 로고    scopus 로고
    • Update of the drug resistance mutations in HIV-1: 2007
    • Johnson V.A., et al. Update of the drug resistance mutations in HIV-1: 2007. Top. HIV Med. 15 (2007) 119-125
    • (2007) Top. HIV Med. , vol.15 , pp. 119-125
    • Johnson, V.A.1
  • 23
    • 0036145503 scopus 로고    scopus 로고
    • A potent human immunodeficiency virus type 1 protease inhibitor, UIC-94003 (TMC-126), and selection of a novel (A28S) mutation in the protease active site
    • Yoshimura K., et al. A potent human immunodeficiency virus type 1 protease inhibitor, UIC-94003 (TMC-126), and selection of a novel (A28S) mutation in the protease active site. J. Virol. 76 (2002) 1349-1358
    • (2002) J. Virol. , vol.76 , pp. 1349-1358
    • Yoshimura, K.1
  • 24
    • 10744226241 scopus 로고    scopus 로고
    • Novel bis-tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI) UIC-94017 (TMC114) with potent activity against multi-PI-resistant human immunodeficiency virus in vitro
    • Koh Y., et al. Novel bis-tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI) UIC-94017 (TMC114) with potent activity against multi-PI-resistant human immunodeficiency virus in vitro. Antimicrob. Agents Chemother. 47 (2003) 3123-3129
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 3123-3129
    • Koh, Y.1
  • 25
    • 37549044402 scopus 로고    scopus 로고
    • In vitro phenotypic susceptibility of HIV-2 clinical isolates to protease inhibitors: amprenavir, atazanavir, lopinavir, and tipranavir
    • Descamps D., et al. In vitro phenotypic susceptibility of HIV-2 clinical isolates to protease inhibitors: amprenavir, atazanavir, lopinavir, and tipranavir. Antivir. Ther. 11 (2006) S103
    • (2006) Antivir. Ther. , vol.11
    • Descamps, D.1
  • 26
    • 37549017452 scopus 로고    scopus 로고
    • th Conference on Retroviruses and Opportunistic Infections, February 25-28, Los Angeles, CA, U.S.A. Abstract no. 615 (http://www.retroconference.org/2007/Abstracts/29431.htm)
  • 27
    • 52449105860 scopus 로고    scopus 로고
    • Atazanavir susceptibility spectrum extends to HIV-1 non-B subtypes and HIV-2 viral isolates
    • Gong Y.-F., et al. Atazanavir susceptibility spectrum extends to HIV-1 non-B subtypes and HIV-2 viral isolates. Antivir. Ther. 11 (2006) S100
    • (2006) Antivir. Ther. , vol.11
    • Gong, Y.-F.1
  • 28
    • 33645121140 scopus 로고    scopus 로고
    • Susceptibility to protease inhibitors in HIV-2 primary isolates from patients failing antiretroviral therapy
    • Rodés B., et al. Susceptibility to protease inhibitors in HIV-2 primary isolates from patients failing antiretroviral therapy. J. Antimicrob. Chemother. 57 (2006) 709-713
    • (2006) J. Antimicrob. Chemother. , vol.57 , pp. 709-713
    • Rodés, B.1
  • 29
    • 25144487293 scopus 로고    scopus 로고
    • Selection and characterization of HIV-1 showing reduced susceptibility to the non-peptidic protease inhibitor tipranavir
    • Doyon L., et al. Selection and characterization of HIV-1 showing reduced susceptibility to the non-peptidic protease inhibitor tipranavir. Antiviral Res. 68 (2005) 27-35
    • (2005) Antiviral Res. , vol.68 , pp. 27-35
    • Doyon, L.1
  • 30
    • 13344275873 scopus 로고    scopus 로고
    • Antiviral and resistance studies of AG1343, an orally bioavailable inhibitor of human immunodeficiency virus protease
    • Patick A.K., et al. Antiviral and resistance studies of AG1343, an orally bioavailable inhibitor of human immunodeficiency virus protease. Antimicrob. Agents Chemother. 40 (1996) 292-297
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 292-297
    • Patick, A.K.1
  • 31
    • 35948950183 scopus 로고    scopus 로고
    • In vitro selection and characterization of human immunodeficiency virus type 2 with decreased susceptibility to lopinavir
    • Masse S., et al. In vitro selection and characterization of human immunodeficiency virus type 2 with decreased susceptibility to lopinavir. Antimicrob. Agents Chemother. 51 (2007) 3075-3080
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 3075-3080
    • Masse, S.1
  • 32
    • 29144436631 scopus 로고    scopus 로고
    • High rate of proV47A selection in HIV-2 patients failing lopinavir-based HAART
    • Rodés B., et al. High rate of proV47A selection in HIV-2 patients failing lopinavir-based HAART. AIDS 20 (2006) 127-129
    • (2006) AIDS , vol.20 , pp. 127-129
    • Rodés, B.1
  • 33
    • 0031849665 scopus 로고    scopus 로고
    • In vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor
    • Carrillo A., et al. In vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor. J. Virol. 72 (1998) 7532-7541
    • (1998) J. Virol. , vol.72 , pp. 7532-7541
    • Carrillo, A.1
  • 34
    • 14744283486 scopus 로고    scopus 로고
    • Selection of resistance in protease inhibitor-experienced, human immunodeficiency virus type 1-infected subjects failing lopinavir- and ritonavir-based therapy: mutation patterns and baseline correlates
    • Mo H., et al. Selection of resistance in protease inhibitor-experienced, human immunodeficiency virus type 1-infected subjects failing lopinavir- and ritonavir-based therapy: mutation patterns and baseline correlates. J. Virol. 79 (2005) 3329-3338
    • (2005) J. Virol. , vol.79 , pp. 3329-3338
    • Mo, H.1
  • 35
    • 10344263394 scopus 로고    scopus 로고
    • Genetic correlates of in vivo viral resistance to indinavir, a human immunodeficiency virus type 1 protease inhibitor
    • Condra J.H., et al. Genetic correlates of in vivo viral resistance to indinavir, a human immunodeficiency virus type 1 protease inhibitor. J. Virol. 70 (1996) 8270-8276
    • (1996) J. Virol. , vol.70 , pp. 8270-8276
    • Condra, J.H.1
  • 36
    • 15444377672 scopus 로고    scopus 로고
    • Ordered accumulation of mutations in HIV protease confers resistance to ritonavir
    • Molla A., et al. Ordered accumulation of mutations in HIV protease confers resistance to ritonavir. Nat. Med. 2 (1996) 760-766
    • (1996) Nat. Med. , vol.2 , pp. 760-766
    • Molla, A.1
  • 37
    • 0031692748 scopus 로고    scopus 로고
    • Genotypic and phenotypic characterization of human immunodeficiency virus type 1 variants isolated from patients treated with the protease inhibitor nelfinavir
    • Patick A.K., et al. Genotypic and phenotypic characterization of human immunodeficiency virus type 1 variants isolated from patients treated with the protease inhibitor nelfinavir. Antimicrob. Agents Chemother. 42 (1998) 2637-2644
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2637-2644
    • Patick, A.K.1
  • 38
    • 0036720761 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 genotypic and pharmacokinetic determinants of the virological response to lopinavir-ritonavir-containing therapy in protease inhibitor-experienced patients
    • Masquelier B., et al. Human immunodeficiency virus type 1 genotypic and pharmacokinetic determinants of the virological response to lopinavir-ritonavir-containing therapy in protease inhibitor-experienced patients. Antimicrob. Agents Chemother. 46 (2002) 2926-2932
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2926-2932
    • Masquelier, B.1
  • 39
    • 0033999842 scopus 로고    scopus 로고
    • Emergence of drug resistance mutations in human immunodeficiency virus type 2-infected subjects undergoing antiretroviral therapy
    • Rodés B., et al. Emergence of drug resistance mutations in human immunodeficiency virus type 2-infected subjects undergoing antiretroviral therapy. J. Clin. Microbiol. 38 (2000) 1370-1374
    • (2000) J. Clin. Microbiol. , vol.38 , pp. 1370-1374
    • Rodés, B.1
  • 40
    • 0043033106 scopus 로고    scopus 로고
    • Clinical, immunological and virological response to different antiretroviral regimens in a cohort of HIV-2-infected patients
    • Van der Ende M.E., et al. Clinical, immunological and virological response to different antiretroviral regimens in a cohort of HIV-2-infected patients. AIDS 17 Suppl. 3 (2003) S55-S61
    • (2003) AIDS , vol.17 , Issue.SUPPL. 3
    • Van der Ende, M.E.1
  • 41
    • 37549049114 scopus 로고    scopus 로고
    • Mutations in HIV-2 protease selected by protease-inhibitor therapy
    • Cavaco Silva J., et al. Mutations in HIV-2 protease selected by protease-inhibitor therapy. Antivir. Ther. 12 (2007) S87
    • (2007) Antivir. Ther. , vol.12
    • Cavaco Silva, J.1
  • 42
    • 0035902902 scopus 로고    scopus 로고
    • Genotypic variation of HIV-1 reverse transcriptase and protease: comparative analysis of clade C and clade B
    • Grossman Z., et al. Genotypic variation of HIV-1 reverse transcriptase and protease: comparative analysis of clade C and clade B. AIDS 15 (2001) 1453-1460
    • (2001) AIDS , vol.15 , pp. 1453-1460
    • Grossman, Z.1
  • 43
    • 34748818983 scopus 로고    scopus 로고
    • Mutational patterns and correlated amino acid substitutions in the HIV-1 protease after virological failure to nelfinavir- and lopinavir/ritonavir-based treatments
    • Garriga C., et al. Mutational patterns and correlated amino acid substitutions in the HIV-1 protease after virological failure to nelfinavir- and lopinavir/ritonavir-based treatments. J. Med. Virol. 79 (2007) 1617-1628
    • (2007) J. Med. Virol. , vol.79 , pp. 1617-1628
    • Garriga, C.1
  • 44
    • 0041366926 scopus 로고    scopus 로고
    • pol gene sequence variation in Swedish HIV-2 patients failing antiretroviral therapy
    • Brandin E., et al. pol gene sequence variation in Swedish HIV-2 patients failing antiretroviral therapy. AIDS Res. Hum. Retroviruses 19 (2003) 543-550
    • (2003) AIDS Res. Hum. Retroviruses , vol.19 , pp. 543-550
    • Brandin, E.1


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