Allosteric Inhibitors of the NS3 Protease from the Hepatitis C Virus

PLoS ONE

Volumn 8, Issue 7, 2013, Pages

  Abian, Olga ^a,b,c   Vega, Sonia ^a   Sancho, Javier ^a   Velazquez Campoy, Adrian ^a,d  

^a UNIVERSITY OF ZARAGOZA   (Spain)

^b INSTITUTO DE INVESTIGACIÓN SANITARIA ARAGÓN IIS ARAGÓN   (Spain)

^c INSTITUTO DE SALUD CARLOS III   (Spain)

^d FUNDACIÓN ARAID   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC NS3 PROTEASE INHIBITOR; NONSTRUCTURAL PROTEIN 3; NONSTRUCTURAL PROTEIN 4A; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG; ZINC ION;

ALLOSTERISM; ARTICLE; CALORIMETRY; CELL ASSAY; CELL CYCLE ARREST; DRUG DETERMINATION; DRUG EFFICACY; ENZYMATIC ASSAY; ENZYME CONFORMATION; ENZYME INHIBITION; HEPATITIS C VIRUS; LIGAND BINDING; MOLECULAR WEIGHT; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; REPLICON; SUICIDE SUBSTRATE; VIROGENESIS; VIRUS MUTATION; VIRUS RESISTANCE;

ALLOSTERIC REGULATION; ANTIVIRAL AGENTS; CELL LINE; DRUG EVALUATION, PRECLINICAL; DRUG RESISTANCE, VIRAL; ENZYME ACTIVATION; HEPACIVIRUS; HUMANS; LIGANDS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; PROTEASE INHIBITORS; PROTEIN BINDING; VIRAL NONSTRUCTURAL PROTEINS; VIRUS REPLICATION;

EID: 84880845826     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0069773     Document Type: Article

References (31)

1. De Francesco R, Urbani A, Nardi MC, Tomei L, Steinkühler C, et al. (1996) A zinc binding site in viral serine proteinases. Biochemistry 35: 13282-13287.
2. Love RA, Parge HE, Wickersham JA, Hostomsky Z, Habuka N, et al. (1996) The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site. Cell 87: 331-342.
3. Kim JL, Morgenstern KA, Lin C, Fox T, Dwyer MD, et al. (1996) Crystal-structure of the hepatitis-C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide. Cell 87: 345-355.
4. Stempniak M, Hostomska Z, Nodes BR, Hostomsky Z, (1997) The NS3 proteinase domain of hepatitis C virus is a zinc-containing enzyme. J Virol 71: 2881-2886.
5. Failla C, Tomei L, De Francesco R, (1994) Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins. J Virol 68: 3753-3760.
6. Lin C, Thomson JA, Rice CM, (1995) A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro. J Virol 69: 4373-4380.
7. Tanji Y, Hijikata M, Satoh S, Kaneko T, Shimotohno K, (1995) Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing. J Virol 69: 1575-1581.
8. Tomei L, Failla C, Vitale RL, Bianchi E, De Francesco R, (1996) A central hydrophobic domain of the hepatitis C virus NS4A protein is necessary and sufficient for the activation of the NS3 protease. J Gen Virol 77: 1065-1070.
9. Kwong AD, Kauffman RS, Hurter P, Mueller P, (2011) Discovery and development of telaprevir: An NS3-4A protease inhibitor for treating genotype 1 chronic hepatitis C virus. Nat Biotechnol 29: 993-1003.
10. Rizza SA, Talwani R, Nehra V, Temesgen Z, (2011) Boceprevir. Drugs Today 47: 743-751.
11. He Y, King MS, Kempf DJ, Lu L, Lim HB, et al. (2008) Relative replication capacity and selective advantage profiles of protease inhibitor-resistant hepatitis c virus (HCV) NS3 protease mutants in the HCV genotype 1b replicon system. Antimicrob Agents Chemother 52: 1101-1110.
12. Courcambeck J, Bouzidi M, Perbost R, Jouirou B, Amrani N, et al. (2004) Resistance of hepatitis C virus to NS3-4A protease inhibitors: Mechanisms of drug resistance induced by R155Q, A156T, D168A and D168V mutations. Antiviral Therapy 11: 847-855.
13. Susser S, Vermehren J, Forestier N, Welker MW, Grigorian N, et al. (2011) Analysis of long-term persistence of resistance mutations within the hepatitis C virus NS3 protease after treatment with telaprevir or boceprevir. J Clin Virol 52: 321-327.
14. Shimizu Y, Yamaji K, Masuho Y, Yokota T, Inoue H, et al. (1996) Identification of the sequence on NS4A required for enhanced cleavage of the NS5A/5B site by hepatitis C virus NS3 protease. J Virol 70: 127-132.
15. Butkiewicz NJ, Wendel M, Zhang R, Jubin R, Pichardo J, et al. (1996) Enhancement of hepatitis C virus NS3 proteinase activity by association with NS4A-specific synthetic peptides: identification of sequence and critical residues of NS4A for the cofactor activity. Virology 225: 328-338.
16. Walker MA, (1999) Hepatitis C virus: an overview of current approaches and progress. Drug Discov Today 4: 518-529.
17. Abian O, Neira JL, Velazquez-Campoy A, (2009) Thermodynamics of zinc binding to hepatitis C virus NS3 protease: A folding by binding event. Proteins 77: 624-636.
18. Abian O, Vega S, Neira JL, Velazquez-Campoy A, (2010) Conformational stability of hepatitis C virus NS3 protease. Biophys J 99: 3811-3820.
19. Colvin R, Holmes WR, Fontaine CP, Maret W, (2010) Cytosolic zinc buffering and muffling: Their role in intracellular zinc homeostasis. Metallomics 2: 306-317.
20. Binet MR, Poole RK, (2000) Cd(II), Pb(II) and Zn(II) ions regulate expression of the metal-transporting P-type ATPase ZntA in Escherichia coli. FEBS Lett 473: 67-70.
21. Brocklehurst KR, Hobman JL, Lawley B, Blank L, Marshall SJ, et al. (1999) ZntR is a Zn(II)-responsive MerR-like transcriptional regulator of zntA in Escherichia coli. Mol Microbiol 31: 893-902.
22. Outten CE, O'Halloran TV, (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292: 2488-2492.
23. Urbani A, Bazzo R, Nardi MC, Cicero DO, De Francesco R, et al. (1998) The metal binding site of the hepatitis C virus NS3 protease. A spectroscopic investigation. J Biol Chem 273: 18760-18769.
24. Thibeault D, Massariol MJ, Zhao S, Welchner E, Goudreau N, et al. (2009) Use of the fused NS4A peptide-NS3 protease domain to study the importance of the helicase domain for protease inhibitor binding to hepatitis C virus NS3-NS4A. Biochemistry 48: 744-753.
25. Vrolijk JM, Kaul A, Hansen BE, Lohmann V, Haagmans BL, et al. (2003) A replicon-based bioassay for the measurement of interferons in patients with chronic hepatitis C. J Virol Methods. 110: 201-209.
26. Lohmann V, Korner F, Dobierzewska A, Bartenschlager R, (2001) Mutations in hepatitis C virus RNAs conferring cell culture adaptation. J Virol 75: 1437-1449.
27. Blight KJ, McKeating JA, Rice CM, (2002) Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication. J Virol 76: 13001-13014.
28. Lohmann V, Korner F, Koch J, Herian U, Theilmann L, et al. (1999) Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line. Science 285: 110-113.
29. Cremades N, Velazquez-Campoy A, Martinez-Julvez M, Neira JL, Perez-Dorado I, et al. (2009) Discovery of specific flavodoxin inhibitors as potential therapeutic agents against Helicobacter pylori infection. ACS Chem Biol 4: 928-938.
30. Pey AL, Ying M, Cremades N, Velazquez-Campoy A, Scherer T, et al. (2008) Identification of pharmacological chaperones as potential therapeutic agents to treat phenylketonuria. J Clin Invest 118: 2858-2867.
31. Taliani M, Bianchi E, Narjes F, Fossatelli M, Urbani A, et al. (1996) A continuous assay of hepatitis C virus protease based on resonance energy transfer depsipeptide substrates. Anal Biochem 240: 60-67.