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Volumn 26, Issue 1, 2005, Pages 99-106

Enzymatic activity characterization of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer technique

Author keywords

3C like protease; Enzyme activity; Fluorescence resonance energy transfer; Fluorogenic substrate; Severe acute respiratory coronavirus; Site directed mutagenesis

Indexed keywords

ALANINE; CYSTEINE; HISTIDINE; METHIONINE; SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS 3C LIKE PROTEASE; UNCLASSIFIED DRUG; VIRUS ENZYME;

EID: 19944427356     PISSN: 16714083     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1745-7254.2005.00010.x     Document Type: Article
Times cited : (42)

References (36)
  • 1
    • 0038819069 scopus 로고    scopus 로고
    • SARS coronavirus: A new challenge for prevention and therapy
    • Holmes KV. SARS coronavirus: a new challenge for prevention and therapy. J Clin Invest 2003; 111: 1605-9.
    • (2003) J Clin Invest , vol.111 , pp. 1605-1609
    • Holmes, K.V.1
  • 2
    • 0242717589 scopus 로고    scopus 로고
    • Coronavirus as a possible cause of severe acute respiratory syndrome
    • Peiris JS, Lai ST, Poon LL, Guan Y, Yam LY, Lim W, et al. Coronavirus as a possible cause of severe acute respiratory syndrome. Lancet 2003; 361: 1319-25.
    • (2003) Lancet , vol.361 , pp. 1319-1325
    • Peiris, J.S.1    Lai, S.T.2    Poon, L.L.3    Guan, Y.4    Yam, L.Y.5    Lim, W.6
  • 4
    • 0038326554 scopus 로고    scopus 로고
    • SARS-associated coronavirus
    • Holmes KV. SARS-associated coronavirus. N Engl J Med 2003; 348: 1948-51.
    • (2003) N Engl J Med , vol.348 , pp. 1948-1951
    • Holmes, K.V.1
  • 5
    • 0030970783 scopus 로고    scopus 로고
    • Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase
    • Ziebuhr J, Heusipp G, Siddell SG. Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase. J Virol 1997; 71: 3992-7.
    • (1997) J Virol , vol.71 , pp. 3992-3997
    • Ziebuhr, J.1    Heusipp, G.2    Siddell, S.G.3
  • 6
    • 0027138172 scopus 로고
    • Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes
    • Dougherty WG, Semler BL. Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes. Microbiol Rev 1993; 57: 781-822.
    • (1993) Microbiol Rev , vol.57 , pp. 781-822
    • Dougherty, W.G.1    Semler, B.L.2
  • 7
    • 0028897070 scopus 로고
    • Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus
    • Eleouet JF, Rasschaert D, Lambert P, Levy L, Vende P, Laude H. Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus. Virology 1995; 206: 817-22.
    • (1995) Virology , vol.206 , pp. 817-822
    • Eleouet, J.F.1    Rasschaert, D.2    Lambert, P.3    Levy, L.4    Vende, P.5    Laude, H.6
  • 8
    • 0034990084 scopus 로고    scopus 로고
    • Viral replicase gene products suffice for coronavirus discontinuous transcription
    • Thiel V, Herold J, Schelle B, Siddell SG. Viral replicase gene products suffice for coronavirus discontinuous transcription. J Virol 2001; 75: 6676-81.
    • (2001) J Virol , vol.75 , pp. 6676-6681
    • Thiel, V.1    Herold, J.2    Schelle, B.3    Siddell, S.G.4
  • 9
    • 0027313298 scopus 로고
    • Nucleotide sequence of the human coronavirus 229E RNA polymerase locus
    • Herold J, Raabe T, Schelle-Prinz B, Siddell SG. Nucleotide sequence of the human coronavirus 229E RNA polymerase locus. Virology 1993; 195: 680-91.
    • (1993) Virology , vol.195 , pp. 680-691
    • Herold, J.1    Raabe, T.2    Schelle-Prinz, B.3    Siddell, S.G.4
  • 10
    • 0026074776 scopus 로고
    • The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase
    • Lee HJ, Shieh CK, Gorbalenya AE, Koonin EV, Monica N, Tuler J, et al. The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase. Virology 1991; 180: 567-82.
    • (1991) Virology , vol.180 , pp. 567-582
    • Lee, H.J.1    Shieh, C.K.2    Gorbalenya, A.E.3    Koonin, E.V.4    Monica, N.5    Tuler, J.6
  • 11
    • 0029036797 scopus 로고
    • Characterization and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein
    • Liu DX, Brown TD. Characterization and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein. Virology 1995; 209: 420-7.
    • (1995) Virology , vol.209 , pp. 420-427
    • Liu, D.X.1    Brown, T.D.2
  • 12
    • 0034072633 scopus 로고    scopus 로고
    • Virus-encoded proteinases and proteolytic processing in Nidovirales
    • Ziebuhr J, Snijder EJ, Gorbalenya AE. Virus-encoded proteinases and proteolytic processing in Nidovirales. J Gen Virol 2000; 81: 853-79.
    • (2000) J Gen Virol , vol.81 , pp. 853-879
    • Ziebuhr, J.1    Snijder, E.J.2    Gorbalenya, A.E.3
  • 13
    • 0036187709 scopus 로고    scopus 로고
    • Conservation of substrate specificities among coronavirus main proteases
    • Hegyi A, Ziebuhr J. Conservation of substrate specificities among coronavirus main proteases. J Gen Virol 2002; 83: 595-9.
    • (2002) J Gen Virol , vol.83 , pp. 595-599
    • Hegyi, A.1    Ziebuhr, J.2
  • 14
    • 0029017145 scopus 로고
    • Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity
    • Ziebuhr J, Herold J, Siddell SG. Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity. J Virol 1995; 69: 4331-8.
    • (1995) J Virol , vol.69 , pp. 4331-4338
    • Ziebuhr, J.1    Herold, J.2    Siddell, S.G.3
  • 15
    • 0036646055 scopus 로고    scopus 로고
    • Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain
    • Anand K, Plam GJ, Mesters JR, Siddell SG, Ziebuhr J, Higenfeld R. Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain. EMBO J 2002; 21: 3213-24.
    • (2002) EMBO J , vol.21 , pp. 3213-3224
    • Anand, K.1    Plam, G.J.2    Mesters, J.R.3    Siddell, S.G.4    Ziebuhr, J.5    Higenfeld, R.6
  • 16
    • 9144268403 scopus 로고    scopus 로고
    • Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase
    • Fan KQ, Wei P, Feng Q, Chen SD, Huang CK, Ma L, et al. Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase. J Biol Chem 2004; 279: 1637-42.
    • (2004) J Biol Chem , vol.279 , pp. 1637-1642
    • Fan, K.Q.1    Wei, P.2    Feng, Q.3    Chen, S.D.4    Huang, C.K.5    Ma, L.6
  • 18
    • 0345255626 scopus 로고    scopus 로고
    • The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor
    • Yang HT, Yang MJ, Ding Y, Liu YW, Lou ZY, Zhou Z, et al. The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor. Proc Natl Acad Sci USA 2003; 100: 13190-5.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13190-13195
    • Yang, H.T.1    Yang, M.J.2    Ding, Y.3    Liu, Y.W.4    Lou, Z.Y.5    Zhou, Z.6
  • 19
    • 0028907271 scopus 로고
    • Coronavirus protein processing and RNA synthesis is inhibited by the cysteine protease inhibitor E43d
    • Kim JC, Spence RA, Currier PF, Liu X, Denison MR. Coronavirus protein processing and RNA synthesis is inhibited by the cysteine protease inhibitor E43d. Virology 1995; 208: 1-8.
    • (1995) Virology , vol.208 , pp. 1-8
    • Kim, J.C.1    Spence, R.A.2    Currier, P.F.3    Liu, X.4    Denison, M.R.5
  • 20
    • 0036114930 scopus 로고    scopus 로고
    • Identification of active-site amino acid residues in the Chiba virus 3C-like protease
    • Someya Y, Takeda N, Miyamura T. Identification of active-site amino acid residues in the Chiba virus 3C-like protease. J Virol 2002; 76: 5949-58.
    • (2002) J Virol , vol.76 , pp. 5949-5958
    • Someya, Y.1    Takeda, N.2    Miyamura, T.3
  • 21
    • 12444278968 scopus 로고    scopus 로고
    • A 3D model of SARS-CoV 3CL proteinase and its inhibitors design by virtual screening
    • Xiong B, Gui CS, Xu XY, Luo C, Chen J, Luo HB, et al. A 3D model of SARS-CoV 3CL proteinase and its inhibitors design by virtual screening. Acta Pharmacol Sin 2003; 24: 497-504.
    • (2003) Acta Pharmacol Sin , vol.24 , pp. 497-504
    • Xiong, B.1    Gui, C.S.2    Xu, X.Y.3    Luo, C.4    Chen, J.5    Luo, H.B.6
  • 22
    • 9144255691 scopus 로고    scopus 로고
    • Molecular cloning, expression, purification, and mass spectrometric characterization of 3C-like protease of SARS coronavirus
    • Sun HF, Luo HB, Yu CY, Sun T, Chen J, Peng SY, et al. Molecular cloning, expression, purification, and mass spectrometric characterization of 3C-like protease of SARS coronavirus. Protein Exp Purif 2003; 32: 302-8.
    • (2003) Protein Exp Purif , vol.32 , pp. 302-308
    • Sun, H.F.1    Luo, H.B.2    Yu, C.Y.3    Sun, T.4    Chen, J.5    Peng, S.Y.6
  • 23
    • 0026505650 scopus 로고
    • A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases
    • Knight CG, Willenbrock F, Murphy G. A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases. FEBS Lett 1992; 296: 263-6.
    • (1992) FEBS Lett , vol.296 , pp. 263-266
    • Knight, C.G.1    Willenbrock, F.2    Murphy, G.3
  • 25
    • 0038505787 scopus 로고    scopus 로고
    • Synthesis and evaluation of fluorescent probes for the detection of calpain activity
    • Mittoo S, Sundstrom LE, Bradley M. Synthesis and evaluation of fluorescent probes for the detection of calpain activity. Anal Biochem 2003; 319: 234-8.
    • (2003) Anal Biochem , vol.319 , pp. 234-238
    • Mittoo, S.1    Sundstrom, L.E.2    Bradley, M.3
  • 26
    • 2442435903 scopus 로고    scopus 로고
    • Characterization of SARS main protease and inhibitor assay using a fluorogenic substrate
    • Kuo CJ, Chi YH, Hsu JT, Liang PH. Characterization of SARS main protease and inhibitor assay using a fluorogenic substrate. Biochem Biophys Res Commun 2004; 318: 862-7.
    • (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
  • 27
    • 0026503894 scopus 로고
    • New intramolecularly quenched fluorogenic peptide substrates for the study of the kinetic specificity of papain
    • Garcia-Echeverria C, Rich DH. New intramolecularly quenched fluorogenic peptide substrates for the study of the kinetic specificity of papain. FEBS Lett 1992; 297: 100-2.
    • (1992) FEBS Lett , vol.297 , pp. 100-102
    • Garcia-Echeverria, C.1    Rich, D.H.2
  • 28
    • 0025053937 scopus 로고
    • Design and synthesis of new fluorogenic HIV protease substrates based on resonance energy transfer
    • Wang GT, Matayoshi E, Jan Huffaker H, Krafft GA. Design and synthesis of new fluorogenic HIV protease substrates based on resonance energy transfer. Tetrahedron Lett 1990; 31: 6493-6.
    • (1990) Tetrahedron Lett , vol.31 , pp. 6493-6496
    • Wang, G.T.1    Matayoshi, E.2    Jan Huffaker, H.3    Krafft, G.A.4
  • 29
    • 0025099455 scopus 로고
    • Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer
    • Matayoshi ED, Wang GT, Krafft GA, Erickson J. Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer. Science 1990; 247: 954-8.
    • (1990) Science , vol.247 , pp. 954-958
    • Matayoshi, E.D.1    Wang, G.T.2    Krafft, G.A.3    Erickson, J.4
  • 30
    • 0026483377 scopus 로고
    • A general method for the preparation of internally quenched fluorogenic protease substrates using solid-phase peptide synthesis
    • Maggiora LL, Smith CW, Zhang ZY. A general method for the preparation of internally quenched fluorogenic protease substrates using solid-phase peptide synthesis. J Med Chem 1992; 35: 3727-30.
    • (1992) J Med Chem , vol.35 , pp. 3727-3730
    • Maggiora, L.L.1    Smith, C.W.2    Zhang, Z.Y.3
  • 31
    • 3142613358 scopus 로고    scopus 로고
    • 3C-like proteinase from SARS coronavirus catalyzes substrate hydrolysis by a general base mechanism
    • Huang CK, Wei P, Fan KQ, Liu Y, Lai LL. 3C-like proteinase from SARS coronavirus catalyzes substrate hydrolysis by a general base mechanism. Biochemistry 2004; 43: 4568-74.
    • (2004) Biochemistry , vol.43 , pp. 4568-4574
    • Huang, C.K.1    Wei, P.2    Fan, K.Q.3    Liu, Y.4    Lai, L.L.5
  • 33
    • 0024398958 scopus 로고
    • Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis
    • Gorbalenya AE, Koonin EV, Donchenko AP, Blinov VM. Coronavirus genome: prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis. Nucleic Acids Res 1989; 17: 4847-61.
    • (1989) Nucleic Acids Res , vol.17 , pp. 4847-4861
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 35
    • 0030988810 scopus 로고    scopus 로고
    • Determinants of mouse hepatitis virus 3C-like proteinase activity
    • Lu Y, Denison MR. Determinants of mouse hepatitis virus 3C-like proteinase activity. Virology 1997; 230: 335-42.
    • (1997) Virology , vol.230 , pp. 335-342
    • Lu, Y.1    Denison, M.R.2
  • 36
    • 0036190639 scopus 로고    scopus 로고
    • Mutational analysis of the active centre of coronavirus 3C-like proteases
    • Hegyi A, Friebe A, Gorbalenya AE, Ziebuhr J. Mutational analysis of the active centre of coronavirus 3C-like proteases. J Gen Virol 2002; 83: 581-93.
    • (2002) J Gen Virol , vol.83 , pp. 581-593
    • Hegyi, A.1    Friebe, A.2    Gorbalenya, A.E.3    Ziebuhr, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.