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Research Article

Effectiveness of commercial inhibitors against subtype F HIV-1 protease

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Pages 638-645 | Received 17 Feb 2008, Accepted 23 May 2008, Published online: 01 Jun 2009

References

  • C Kuiken, B Foley, E Freed, B Hahn, P Marx, F McCutchan, L Mellors, B Korber. HIV sequence compendium 2002, Theoretical Biology and Biophysics Group Los Alamos National Laboratory, LA-UR n 03-3564; 2002.
  • S Osmanov, C Pattou, N Walker, B Schwardlander, J Esparza. Estimated global distribution and regional spread of HIV-1 genetic subtypes in the year 2000. J Acquir Immune Defic Syndr 2002; 29:184–190.
  • AD Frankel, JA Young. HIV-1: Fifteen proteins and a RNA. Annu Rev Biochem 1998; 67:1–25.
  • A Wlodawer, M Miller, MK Jaskolski, B Sathyanarayana, ET Baldwin, IM Weber, L Selk, L Clawson, J Schneider, SB Kent. Conserved folding in retroviral proteases: Crystal structure of a synthetic HIV-1 protease. Science 1989; 245:616–621.
  • M Miller, J Schneider, BK Sathyanarayana, MV Toth, GR Marshall, L Clawson, L Selk, SB Kent, A Wlodawer. Structure of complex of synthetic HIV-1 protease with a substrate based inhibitor at 2.3-Å resolution. Science 1989; 246:1149–1152.
  • R Lapatto, T Blundell, A Hemmings, J Overington, A Wilderspin, S Wood, JR Merson, PJ Whittle, DE Danley, KF Geoghegan, SJ Hawrylik, SE Lee, KG Scheld, PM Hobart. X-ray analysis of HIV-1 proteinase at 2.7 Å resolution confirms structural homology among retroviral enzymes. Nature 1989; 342:299–302.
  • R Kantor, DA Katzenstein, B Efron, AP Carvalho, B Wynhoven, P Cane, J Clarke, S Sirivichayakul, MA Soares, J Snoeck, C Pillay, H Rudich, R Rodrigues, A Holguin, K Ariyoshi, MB Bouzas, P Cahn, W Sugiura, V Soriano, LF Brigido, Z Grossman, L Morris, A-M Vandamme, A Tanuri, P Phanuphak, JN Weber, D Pillay, PR Harrigan, R Camacho, JM Schapiro, RW Shafer. Impact of HIV-1 subtype and antiretroviral therapy on protease and reverse transcriptase genotype: Results of a global collaboration. PLoS Med 2005; 2:325–337.
  • SY Rhee, WJ Fessel, AR Zolopa, L Hurley, T Liu, J Taylor, DP Nguyen, S Slome, D Klein, M Horberg, J Flamm, S Follansbee, JM Schapiro, RWJ Shafer. HIV drug resistance database. Infect Dis 2005; 192:456–465.
  • VA Johnson, F Brun-Vézinet, B Clotet, HF Günthard, DR Kuritzkes, D Pillay, JM Schapiro, A Telenti, DD Richman. Update of the drug resistance mutations in HIV-1: 2007. Top HIV Med 2007; 15:119–125.
  • JW Erickson, SK Burt. Structural mechanisms of HIV drug resistance. Annu Rev Pharmacol Toxicol 1996; 36:545–571.
  • ET Baldwin, TN Bhat, B Liu, N Pattabiraman, JW Erickson. Structural basis of drug resistance for the V82A mutant of HIV-1 proteinase. Nat Struct Biol 1995; 2:244–249.
  • S Muzammil, P Ross, E Freire. A major role for a set of non-active site mutations in the development of HIV-1 protease drug resistance. Biochemistry 2003; 42:631–638.
  • HB Schock, VM Garsky, LC Kuo. Mutational anatomy of an HIV-1 protease variant conferring cross-resistance to protease inhibitors in clinical trials. Compensatory modulations of binding and activity. J Biol Chem 1996; 271:31957–31963.
  • DB Olsen, MW Stahlhut, CA Rutkowski, HB Schock, AL van Olden, LC Kuo. Non-active site changes elicit broad-based cross-resistance of the HIV-1 protease to inhibitors. J Biol Chem 1999; 274:23699–23701.
  • CF Perno, A Cozzi-Lepri, C Balotta, F Forbici, M Violin, A Bertoli, G Facchi, P Pezzetti, G Cadeo, G Tositti, S Pasquinucci, S Pauluzzi, A Scalzini, B Salassa, A Vincenti, AN Phillips, F Dianzani, A Apice, G Angarano, L Monno, G Ippolito, M Moroni, AA Monfortethe. Italian Cohort Naive Antiretroviral (I.CO.N.A.) study group. secondary mutations in the protease region of human immunodeficiency virus and virologic failure in drug-naïve patients treated with protease inhibitor-based therapy. J Infect Dis 2001; 184:983–991.
  • A Velázquez-Campoy, S Vega, E Fleming, U Bacha, Y Sayed, HW Dirr, E Freire. Protease inhibition in African subtypes of HIV-1. AIDS Rev 2003; 5:165–171.
  • T Lee, VD Le, D Lim, YC Lin, GM Morris, AL Wong, AJ Olson, JH Elder, C-H Wong. Development of a new type of protease inhibitors, efficacious against FIV and HIV variants. J Am Chem Soc 1999; 121:1145–1155.
  • AM Mildner, DJ Rothrock, JW Leone, CA Bannow, JM Lull, IM Reardon, JL Sarcich, WJ Howe, CS Tomich, CW Smith, RL Heinrikson, AG Tomasselli. The HIV-1 protease as enzyme and substrate: Mutagenesis of autolysis sites and generation of a stable mutant with retained kinetic properties. Biochemistry 1994; 33:9405–9413.
  • PA Brindeiro, RM Brindeiro, C Mortensen, K Hertogs, VD Vroey, NPM Rubini, FS Sion, CAM Sá, DM Machado, RCM Succi, A Tarnuri. Testing genotypic and phenotypic resistance in Human Immunodeficiency Virus type 1 isolates of clade B and other clades from children failing antiretroviral therapy. J Clin Microbiol 2002; 40:4512–4519.
  • M Sanches, NH Martins, A Calazans, RM Brindeiro, A Tanuri, OAC Antunes, I Polikarpov. Crystallization of a non-B and a B mutant HIV protease. Acta Crystallogr 2004; D60:1625–1627.
  • ED Matayoshi, GT Wang, GA Kraft, J Erickson. Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer. Science 1990; 24:954–958.
  • JF Morrison. Kinetics of the reversible inhibition of enzyme catalysed reactions of tight-binding inhibitors. Biochim Biophys Acta 1969; 185:269–285.
  • JG Bieth. Theoretical and practical aspects of proteinase inhibition kinetics. Methods Enzymol 1995; 248:59–84.
  • A Velazquez-Campoy, MJ Todd, S Vega, E Freire. Catalytic efficiency and vitality of HIV-1 proteases from African viral subtypes. Proc Natl Acad Sci USA 2001; 98:6062–6067.
  • D Hoffmann, H Assfalg-Machleidt, H Nitschko, K von der Helm, U Koszinowski, W Machleidt. Rapid enzymatic test for phenotypic HIV protease drug resistance. Biol Chem 2003; 384:1109–1117.
  • Y Lin, X Lin, L Hong, S Foundling, RL Heinrikson, S Thaisrivongs, W Leelamanit, D Raterman, M Shah, BD Dunn, J Tang. Effect of point mutations on the kinetics and the inhibition of human immunodeficiency virus type 1 protease: Relationship to drug resistance. Biochemistry 1995; 34:1143–1152.
  • L Hong, A Treharne, JA Hartsuck, S Foundling, J Tang. Crystal structures of complexes of a peptidic inhibitor with wild-type and two mutant HIV-1 proteases. Biochemistry 1996; 35:10627–10633.
  • A Calazans, R Brindeiro, P Brindeiro, H Verli, MB Arruda, LMF Gonzalez, JA Guimarães, RS Diaz, OAC Antunes, A Tanuri. Low accumulation of L90M in protease from subtype F HIV-1 with resistance to protease inhibitors is caused by the L89M polymorphism. J Infect Dis 2005; 191:1961–1970.
  • M Sanches, S Krauchenco, NH Martins, A Gustchina, A Wlodawer, I Polikarpov. Structural characterization of B and non B subtypes of HIV-protease: Insights into natural susceptibility to drug resistance development. J Mol Biol 2007; 369:1029–1040.
  • S Gulnik, LI Suvorov, B Liu, B Yu, B Anderson, H Mitsuya, JW Erickson. Kinetic characterization and cross-resistance patterns of HIV protease mutants selected under drug pressure. Biochemistry 1995; 34:9282–9287.
  • I Luque, MJ Todd, J Gomez, N Semo, E Freire. Molecular basis of resistance to HIV-1 protease inhibition: A plausible hypothesis. Biochemistry 1998; 37:5791–5797.
  • MJ Todd, I Luque, A Velazquez-Campoy, E Freire. Thermodynamic basis of resistance to HIV-1 protease inhibition: Calorimetric analysis of the V82F/I84V active site resistant mutant. Biochemistry 2000; 39:11876–11883.
  • VA Johnson, F Brun-Vézinet, B Clotet, HF Günthard, DR Kuritzkes, D Pillay, JM Schapiro, DD Richman. Update of the drug resistance mutations in HIV-1: 2007. Top HIV Med 2007; 15:119–125.
  • JC Clemente, RE Moose, R Hemrajani, LR Whitford, L Govindasamy, R Reutzel, R McKenna, M Agbandje-McKenna, MM Goodenow, BM Dunn. Comparing the accumulation of active- and nonactive-site mutations in the HIV-1 protease. Biochemistry 2004; 43:12141–12151.

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