A continuous assay for foot-and-mouth disease virus 3C protease activity

Analytical Biochemistry

Volumn 368, Issue 2, 2007, Pages 130-137

  Jaulent, Agnès M ^a   Fahy, Aodhnait S ^a   Knox, Stephen R ^a   Birtley, James R ^a   Roqué Rosell, Núria ^a   Curry, Stephen ^a   Leatherbarrow, Robin J ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

3C protease; FMDV; FRET; Peptide; Protease

Indexed keywords

AGRICULTURAL ROBOTS; AGRICULTURE; AMINO ACIDS; ENERGY TRANSFER; FORSTER RESONANCE ENERGY TRANSFER; PEPTIDES; SUBSTRATES; VIRUSES;

3C PROTEASE; CHYMOTRYPSIN INHIBITORS; FLUORESCENCE RESONANCE ENERGY TRANSFER; FMDV; FOOT-AND-MOUTH DISEASE VIRUS; FRET; HIGH-THROUGHPUT ASSAYS; PROTEASE;

ENZYME INHIBITION;

3C PROTEASE; CHYMOTRYPSIN INHIBITOR; CYSTEINE PROTEINASE; PEPTIDE; SERINE PROTEINASE; TOSYLPHENYLALANYL CHLOROMETHYL KETONE; UNCLASSIFIED DRUG; VIRUS ENZYME;

ANALYTIC METHOD; ARTICLE; ENZYME ACTIVITY; FLUORESCENCE RESONANCE ENERGY TRANSFER; FOOT AND MOUTH DISEASE VIRUS; HIGH THROUGHPUT SCREENING; PRIORITY JOURNAL; SEPARATION TECHNIQUE; STOICHIOMETRY; TITRIMETRY;

FOOT-AND-MOUTH DISEASE VIRUS;

EID: 34547584549     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.05.026     Document Type: Article

References (31)

1. Sobrino F., Saiz M., Jimenez-Clavero M.A., Nunez J.I., Rosas M.F., Baranowski E., and Ley V. Foot-and-mouth disease virus: A long known virus, but a current threat. Vet. Res. 32 (2001) 1-30
2. Sutmoller P., Barteling S.S., Olascoaga R.C., and Sumption K.J. Control and eradication of foot-and-mouth disease. Virus Res. 91 (2003) 101-144
3. Grubman M.J., and Baxt B. Foot-and-mouth disease. Clin. Microbiol. Rev. 17 (2004) 465-493
4. Crispin S.M., Roger P.A., O'Hare H., and Binns S.H. The 2001 foot and mouth disease epidemic in the United Kingdom: Animal welfare perspectives. Rev. Sci. Tech. 21 (2002) 877-883
5. Doel T.R. FMD vaccines. Virus Res. 91 (2003) 81-99
6. Sutherland A.D. FMD control strategies. Vet. Rec. 148 (2001) 670-671
7. Moonen P., Jacobs L., Crienen A., and Dekker A. Detection of carriers of foot-and-mouth disease virus among vaccinated cattle. Vet. Microbiol. 103 (2004) 151-160
8. Allaire M., Chernaia M.M., Malcolm B.A., and James M.N. Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature 369 (1994) 72-76
9. Mosimann S.C., Cherney M.M., Sia S., Plotch S., and James M.N. Refined X-ray crystallographic structure of the poliovirus 3C gene product. J. Mol. Biol. 273 (1997) 1032-1047
10. Birtley J.R., Knox S.R., Jaulent A.M., Brick P., Leatherbarrow R.J., and Curry S. Crystal structure of foot-and-mouth disease virus 3C protease: New insights into catalytic mechanism and cleavage specificity. J. Biol. Chem. 280 (2005) 11520-11527
11. Charles C.H., Yelmene M., and Luo G.X. Recent advances in rhinovirus therapeutics. Curr. Drug Targets Infect. Disord. 4 (2004) 331-337
12. Hsu J.T.A., Wang H.C., Chen G.W., and Shih S.R. Antiviral drug discovery targeting to viral proteases. Curr. Pharm. Des. 12 (2006) 1301-1314
13. Wlodawer A., and Vondrasek J. Inhibitors of HIV-1 protease: A major success of structure-assisted drug design. Annu. Rev. Biophys. Biomol. Struct. 27 (1998) 249-284
14. Lamarre D., Anderson P.C., Bailey M., Beaulieu P., Bolger G., Bonneau P., Bos M., Cameron D.R., Cartier M., Cordingley M.G., Faucher A.M., Goudreau N., Kawai S.H., Kukolj G., Lagace L., LaPlante S.R., Narjes H., Poupart M.A., Rancourt J., Sentjens R.E., St George R., Simoneau B., Steinmann G., Thibeault D., Tsantrizos Y.S., Weldon S.M., Yong C.L., and Llinas-Brunet M. An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virus. Nature 426 (2003) 186-189
15. Sweeney T.R., Roque-Rosell N., Birtley J.R., Leatherbarrow R.J., and Curry S. Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the β-ribbon in proteolysis. J. Virol. 81 (2007) 115-124
16. Weidner J.R., and Dunn B.M. Development of synthetic peptide substrates for the poliovirus 3C proteinase. Arch. Biochem. Biophys. 286 (1991) 402-408
17. Jewell D.A., Swietnicki W., Dunn B.M., and Malcolm B.A. Hepatitis A virus 3C proteinase substrate specificity. Biochemistry 31 (1992) 7862-7869
18. Holskin B.P., Bukhtiyarova M., Dunn B.M., Baur P., Dechastonay J., and Pennington M.W. A continuous fluorescence-based assay of human cytomegalovirus protease using a peptide substrate. Anal. Biochem. 227 (1995) 148-155
19. Hata S., Sato T., Sorimachi H., Ishiura S., and Suzuki K. A simple purification and fluorescent assay method of the poliovirus 3C protease searching for specific inhibitors. J. Virol. Methods 84 (2000) 117-126
20. Blanchard J.E., Elowe N.H., Huitema C., Fortin P.D., Cechetto J.D., Eltis L.D., and Brown E.D. High-throughput screening identifies inhibitors of the SARS coronavirus main proteinase. Chem. Biol. 11 (2004) 1445-1453
21. Kao R.Y., To A.P., Ng L.W., Tsui W.H., Lee T.S., Tsoi H.W., and Yuen K.Y. Characterization of SARS-CoV main protease and identification of biologically active small molecule inhibitors using a continuous fluorescence-based assay. FEBS Lett. 576 (2004) 325-330
22. Chen S., Chen L.L., Luo H.B., Sun T., Chen J., Ye F., Cai J.H., Shen J.K., Shen X., and Jiang H.L. Enzymatic activity characterization of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer technique. Acta Pharmacol. Sin. 26 (2005) 99-106
23. Hamill P., Hudson D., Kao R.Y., Chow P., Raj M., Xu H., Richer M.J., and Jean F. Development of a red-shifted fluorescence-based assay for SARS-coronavirus 3CL protease: Identification of a novel class of anti-SARS agents from the tropical marine sponge Axinella corrugata. Biol. Chem. 387 (2006) 1063-1074
24. Matayoshi E.D., Wang G.T., Krafft G.A., and Erickson J. Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer. Science 247 (1990) 954-958
25. Leatherbarrow R.J. GraFit version 5 (2001), Erithacus Software, Horley, UK
26. Taliani M., Bianchi E., Narjes F., Fossatelli M., Urbani A., Steinkuhler C., De Francesco R., and Pessi A. A continuous assay of hepatitis C virus protease based on resonance energy transfer depsipeptide substrates. Anal. Biochem. 240 (1996) 60-67
27. Long A.C., Orr D.C., Cameron J.M., Dunn B.M., and Kay J. A consensus sequence for substrate hydrolysis by rhinovirus 3C proteinase. FEBS Lett. 258 (1989) 75-78
28. Cornish-Bowden A. Fundamentals of Enzyme Kinetics (2004), Portland Press, London
29. Wang Q.M., and Johnson R.B. Activation of human rhinovirus-14 3C protease. Virology 280 (2001) 80-86
30. Kleina L.G., and Grubman M.J. Antiviral effects of a thiol protease inhibitor on foot-and-mouth disease virus. J. Virol. 66 (1992) 7168-7175
31. Hernandez A.A., and Roush W.R. Recent advances in the synthesis, design, and selection of cysteine protease inhibitors. Curr. Opin. Chem. Biol. 6 (2002) 459-465