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Volumn 86, Issue 21, 2012, Pages 11754-11762

Broad-spectrum antivirals against 3C or 3C-like proteases of picornaviruses, noroviruses, and coronaviruses

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA KETOAMIDE; ANTIVIRUS AGENT; DIPEPTIDYL ALDEHYDE; DIPEPTIDYL BISULFITE ADDUCT SALT; GC 373; GC 375; GC 376; PROTEINASE; RUPINTRIVIR; UNCLASSIFIED DRUG;

EID: 84869069227     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01348-12     Document Type: Article
Times cited : (265)

References (46)
  • 1
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: a comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. 2010. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr.66:213-221.
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 2
    • 0036646055 scopus 로고    scopus 로고
    • Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.
    • Anand K, et al. 2002. Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.EMBO J. 21:3213-3224.
    • (2002) EMBO J. , vol.21 , pp. 3213-3224
    • Anand, K.1
  • 3
    • 0038120984 scopus 로고    scopus 로고
    • Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
    • Anand K, Ziebuhr J, Wadhwani P, Mesters JR, Hilgenfeld R. 2003.Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Science 300:1763-1767.
    • (2003) Science , vol.300 , pp. 1763-1767
    • Anand, K.1    Ziebuhr, J.2    Wadhwani, P.3    Mesters, J.R.4    Hilgenfeld, R.5
  • 5
    • 0031047974 scopus 로고    scopus 로고
    • The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition
    • Bergmann EM, Mosimann SC, Chernaia MM, Malcolm BA, James MN.1997. The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition. J. Virol. 71:2436-2448.
    • (1997) J. Virol. , vol.71 , pp. 2436-2448
    • Bergmann, E.M.1    Mosimann, S.C.2    Chernaia, M.M.3    Malcolm, B.A.4    James, M.N.5
  • 6
    • 12944268369 scopus 로고    scopus 로고
    • Conservation of amino acids in human rhinovirus 3C protease correlates with broad-spectrum antiviral activity of rupintrivir,a novel human rhinovirus 3C protease inhibitor
    • Binford SL, et al. 2005. Conservation of amino acids in human rhinovirus 3C protease correlates with broad-spectrum antiviral activity of rupintrivir,a novel human rhinovirus 3C protease inhibitor. Antimicrob. Agents Chemother. 49:619-626.
    • (2005) Antimicrob. Agents Chemother , vol.49 , pp. 619-626
    • Binford, S.L.1
  • 7
    • 15744372994 scopus 로고    scopus 로고
    • Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity
    • Birtley JR, et al. 2005. Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity.J. Biol. Chem. 280:11520 -11527.
    • (2005) J. Biol. Chem. , vol.280
    • Birtley, J.R.1
  • 8
    • 33748853528 scopus 로고    scopus 로고
    • Stable expression of a Norwalk virus RNA replicon in a human hepatoma cell line
    • Chang KO, Sosnovtsev SV, Belliot G, King AD, Green KY. 2006. Stable expression of a Norwalk virus RNA replicon in a human hepatoma cell line. Virology 353:463- 473.
    • (2006) Virology , vol.353
    • Chang, K.O.1    Sosnovtsev, S.V.2    Belliot, G.3    King, A.D.4    Green, K.Y.5
  • 9
    • 84855787364 scopus 로고    scopus 로고
    • Characterization of proteases from norovirus genogroup I and II with the fluorescence resonance energy transfer assay
    • Chang KO, Takahashi D, Prakash O, Kim Y. 2012. Characterization of proteases from norovirus genogroup I and II with the fluorescence resonance energy transfer assay. Virology 423:125-133.
    • (2012) Virology , vol.423 , pp. 125-133
    • Chang, K.O.1    Takahashi, D.2    Prakash, O.3    Kim, Y.4
  • 10
    • 0028103275 scopus 로고    scopus 로고
    • The CCP4 suite:programs for protein crystallography
    • Collaborative Computational Project Number 4. 1994,Acta Crystallogr
    • Collaborative Computational Project Number 4. 1994. The CCP4 suite:programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr.50:760 -763.
    • D Biol. Crystallogr , vol.50
  • 11
    • 77954686776 scopus 로고    scopus 로고
    • Antiviral therapy: quo vadis? Future Med.
    • De Clercq E. 2010. Antiviral therapy: quo vadis? Future Med. Chem.2:1049 -1053.
    • (2010) Chem. , vol.2
    • De clercq, E.1
  • 12
    • 42049112379 scopus 로고    scopus 로고
    • Potential use of antiviral agents in polio eradication
    • De Palma AM, et al. 2008. Potential use of antiviral agents in polio eradication. Emerg. Infect. Dis. 14:545-551.
    • (2008) Emerg. Infect. Dis. , vol.14 , pp. 545-551
    • De Palma, A.M.1
  • 13
    • 0033535579 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 3.Structure-activity studies of ketomethylene-containing peptidomimetics
    • Dragovich PS, et al. 1999. Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 3.Structure-activity studies of ketomethylene-containing peptidomimetics.J. Med. Chem. 42:1203-1212.
    • (1999) J. Med. Chem. , vol.42 , pp. 1203-1212
    • Dragovich, P.S.1
  • 14
    • 0033535596 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 4.Incorporation of P1 lactam moieties as L-glutamine replacements
    • Dragovich PS, et al. 1999. Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 4.Incorporation of P1 lactam moieties as L-glutamine replacements. J. Med. Chem. 42:1213-1224.
    • (1999) J. Med. Chem. , vol.42 , pp. 1213-1224
    • Dragovich, P.S.1
  • 19
    • 78651355832 scopus 로고    scopus 로고
    • A structural study of norovirus 3C protease specificity: binding of a designed active site-directed peptide inhibitor
    • Hussey RJ, et al. 2011. A structural study of norovirus 3C protease specificity: binding of a designed active site-directed peptide inhibitor. Biochemistry 50:240 -249.
    • (2011) Biochemistry , vol.50
    • Hussey, R.J.1
  • 20
    • 0023910548 scopus 로고
    • New human renin inhibitors containing an unnatural amino acid, norstatine
    • Iizuka K, et al. 1988. New human renin inhibitors containing an unnatural amino acid, norstatine. J. Med. Chem. 31:701-704.
    • (1988) J. Med. Chem. , vol.31 , pp. 701-704
    • Iizuka, K.1
  • 21
    • 77956484939 scopus 로고    scopus 로고
    • Hepatitis A virus seroprevalence by age and world region, 1990 and 2005
    • Jacobsen KH, Wiersma ST. 2010. Hepatitis A virus seroprevalence by age and world region, 1990 and 2005. Vaccine 28:6653- 6657.
    • (2010) Vaccine , vol.28
    • Jacobsen, K.H.1    Wiersma, S.T.2
  • 22
    • 34547584549 scopus 로고    scopus 로고
    • A continuous assay for foot-and-mouth disease virus 3C protease activity
    • Jaulent AM, et al. 2007. A continuous assay for foot-and-mouth disease virus 3C protease activity. Anal. Biochem. 368:130 -137.
    • (2007) Anal. Biochem. , vol.368 , pp. 130-137
    • Jaulent, A.M.1
  • 23
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions.
    • Krissinel E, Henrick K. 2004. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60:2256 -2268.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60
    • Krissinel, E.1    Henrick, K.2
  • 24
    • 2442435903 scopus 로고    scopus 로고
    • Characterization of SARSmain protease and inhibitor assay using a fluorogenic substrate
    • Kuo CJ, Chi YH, Hsu JT, Liang PH. 2004. Characterization of SARSmain protease and inhibitor assay using a fluorogenic substrate. Biochem.Biophys. Res. Commun. 318:862- 867.
    • (2004) Biochem.Biophys. Res. Commun. , vol.318 , pp. 862-867
    • Kuo, C.J.1    Chi, Y.H.2    Hsu, J.T.3    Liang, P.H.4
  • 25
    • 58649118410 scopus 로고    scopus 로고
    • Individual and common inhibitors of coronavirus and picornavirus main proteases
    • Kuo CJ, et al. 2009. Individual and common inhibitors of coronavirus and picornavirus main proteases. FEBS Lett. 583:549-555.
    • (2009) FEBS Lett. , vol.583 , pp. 549-555
    • Kuo, C.J.1
  • 26
    • 65549145945 scopus 로고    scopus 로고
    • Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and peptidomimetic compounds
    • Lee CC, et al. 2009. Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and peptidomimetic compounds.J. Biol. Chem. 284:7646 -7655.
    • (2009) J. Biol. Chem. , vol.284
    • Lee, C.C.1
  • 28
    • 84863425147 scopus 로고    scopus 로고
    • Potent inhibition of Norwalk virus 3C protease by peptidyl α-ketoamides and α-ketoheterocycles
    • Mandadapu SR, et al. Potent inhibition of Norwalk virus 3C protease by peptidyl α-ketoamides and α-ketoheterocycles. Bioorg. Med. Chem. 22: 4820-4826.
    • Bioorg. Med. Chem. , vol.22 , pp. 4820-4826
    • Mandadapu, S.R.1
  • 29
    • 0028235532 scopus 로고
    • Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein
    • Matthews DA, et al. 1994. Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein. Cell 77:761-771.
    • (1994) Cell , vol.77 , pp. 761-771
    • Matthews, D.A.1
  • 30
    • 27144521087 scopus 로고    scopus 로고
    • A norovirus protease structure provides insights into active and substrate binding site integrity
    • Nakamura K, et al. 2005. A norovirus protease structure provides insights into active and substrate binding site integrity. J. Virol. 79:13685-13693.
    • (2005) J. Virol. , vol.79 , pp. 13685-13693
    • Nakamura, K.1
  • 31
    • 0024203938 scopus 로고
    • oliovirus proteinase 3C: large-scale expression, purification, and specific cleavage activity on natural and synthetic substrates in vitro
    • Nicklin MJ, Harris KS, Pallai PV, Wimmer E. 1988. Poliovirus proteinase 3C: large-scale expression, purification, and specific cleavage activity on natural and synthetic substrates in vitro. J. Virol. 62:4586-4593.
    • (1988) J. Virol. , vol.62 , pp. 4586-4593
    • Nicklin, M.J.1    Harris, K.S.2    Pallai, P.V.3    Wimmer, E.4
  • 32
    • 0028857767 scopus 로고
    • α-Hydroxy phosphinyl-based inhibitors of human renin
    • Patel DV, et al. 1995. α-Hydroxy phosphinyl-based inhibitors of human renin. J. Med. Chem. 38:4557- 4569.
    • (1995) J. Med. Chem. , vol.38 , pp. 4557-4569
    • Patel, D.V.1
  • 33
    • 0032870120 scopus 로고    scopus 로고
    • In vitro antiviral activity of AG7088, a potent inhibitor of human rhinovirus 3C protease
    • Patick AK, et al. 1999. In vitro antiviral activity of AG7088, a potent inhibitor of human rhinovirus 3C protease. Antimicrob. Agents Chemother.43:2444-2450.
    • (1999) Antimicrob. Agents Chemother , vol.43 , pp. 2444-2450
    • Patick, A.K.1
  • 34
    • 67349158649 scopus 로고    scopus 로고
    • Coronaviruses post-SARS: update on replication and pathogenesis
    • Perlman S, Netland J. 2009. Coronaviruses post-SARS: update on replication and pathogenesis. Nat. Rev. Microbiol. 7:439-450.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 439-450
    • Perlman, S.1    Netland, J.2
  • 35
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent endpoints
    • Reed LJ, Muench H. 1938. A simple method of estimating fifty percent endpoints. Am. J. Hyg. 27:493-497.
    • (1938) Am. J. Hyg. , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 37
    • 0028851295 scopus 로고
    • Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates
    • Schultheiss T, Sommergruber W, Kusov Y, Gauss-Muller V. 1995.Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates. J. Virol. 69:1727-1733.
    • (1995) J. Virol. , vol.69 , pp. 1727-1733
    • Schultheiss, T.1    Sommergruber, W.2    Kusov, Y.3    Gauss-Muller, V.4
  • 38
    • 57349140230 scopus 로고    scopus 로고
    • Targeting inside-out phosphatidylserine as a therapeutic strategy for viral diseases
    • Soares MM, King SW, Thorpe PE. 2008. Targeting inside-out phosphatidylserine as a therapeutic strategy for viral diseases. Nat. Med. 14:1357-1362.
    • (2008) Nat. Med. , vol.14 , pp. 1357-1362
    • Soares, M.M.1    King, S.W.2    Thorpe, P.E.3
  • 39
    • 84869024522 scopus 로고    scopus 로고
    • ackbone and side-chain (1)H, (15)N, and (13)C resonance assignments of Norwalk virus protease
    • Takahashi D, Kim Y, Chang KO, Anbanandam A, Prakash O. 2012.Backbone and side-chain (1)H, (15)N, and (13)C resonance assignments of Norwalk virus protease. Biomol. NMR Assign. 85:12570 -12577.
    • (2012) Biomol. NMR Assign. , vol.85 , pp. 12570-12577
    • Takahashi, D.1    Kim, Y.2    hang, K.O.3    Anbanandam, A.4    Prakash, O.5
  • 40
    • 80051935019 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of inhibitors of Norwalk virus 3C protease
    • Tiew KC, et al. 2011. Design, synthesis, and evaluation of inhibitors of Norwalk virus 3C protease. Bioorg. Med. Chem. Lett. 21:5315-5319.
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 5315-5319
    • Tiew, K.C.1
  • 41
    • 0036882392 scopus 로고    scopus 로고
    • Viral proteases
    • Tong L. 2002. Viral proteases. Chem. Rev. 102:4609-4626.
    • (2002) Chem. Rev. , vol.102 , pp. 4609-4626
    • Tong, L.1
  • 43
    • 77649246144 scopus 로고    scopus 로고
    • A broad-spectrum antiviral targeting entry of enveloped viruses
    • Wolf MC, et al. 2010. A broad-spectrum antiviral targeting entry of enveloped viruses. Proc. Natl. Acad. Sci. U.S.A. 107:3157-3162.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 3157-3162
    • Wolf, M.C.1
  • 44
    • 26444498493 scopus 로고    scopus 로고
    • Design of wide-spectrum inhibitors targeting coronavirus main proteases.
    • doi:10.1371/journal.pbio.0030324
    • Yang H, et al. 2005. Design of wide-spectrum inhibitors targeting coronavirus main proteases. PLoS Biol. 3:e324. doi:10.1371/journal.pbio.0030324.
    • (2005) PLoS Biol. , vol.3
    • Yang, H.1
  • 45
    • 33746827783 scopus 로고    scopus 로고
    • An episulfide cation (thiiranium ring) trapped in the active site of HAV 3C proteinase inactivated by peptide-based ketone inhibitors
    • Yin J, et al. 2006. An episulfide cation (thiiranium ring) trapped in the active site of HAV 3C proteinase inactivated by peptide-based ketone inhibitors. J. Mol. Biol. 361:673-686.
    • (2006) J. Mol. Biol. , vol.361 , pp. 673-686
    • Yin, J.1
  • 46
    • 33646458515 scopus 로고    scopus 로고
    • X-ray crystallographic structure of the Norwalk virus protease at 1.5-A resolution
    • Zeitler CE, Estes MK, Venkataram Prasad BV. 2006. X-ray crystallographic structure of the Norwalk virus protease at 1.5-A resolution. J.Virol. 80:5050-5058.
    • (2006) J.Virol. , vol.80 , pp. 5050-5058
    • Zeitler, C.E.1    Estes, M.K.2    Venkataram Prasad, B.V.3


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