A simple purification and fluorescent assay method of the poliovirus 3C protease searching for specific inhibitors

Journal of Virological Methods

Volumn 84, Issue 2, 2000, Pages 117-126

  Hata, Shoji ^a   Sato, Taisuke ^a   Sorimachi, Hiroyuki ^a,b   Ishiura, Shoichi ^a   Suzuki, Koichi ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

3C Protease; Fluorogenic substrate; Ni2+ Affinity chromatography; Poliovirus; Protease inhibitor

Indexed keywords

2,2' DITHIODIPYRIDINE; APROTININ; BENZYLSULFONYL FLUORIDE; BROMELAIN; CALPASTATIN; CHYMOSTATIN; CYSTATIN; IODOACETIC ACID; LEUPEPTIN; MAGNESIUM CHLORIDE; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; ORYZACYSTATIN; PROTEINASE; PROTEINASE INHIBITOR; TOSYLLYSYL CHLOROMETHYL KETONE; TOSYLPHENYLALANYL CHLOROMETHYL KETONE; VIRUS PROTEIN; ZINC CHLORIDE;

ARTICLE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME INHIBITION; ENZYME PURIFICATION; ESCHERICHIA COLI; FLUORESCENCE ANALYSIS; IN VITRO STUDY; MOLECULAR CLONING; POLIOMYELITIS VIRUS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION;

CYSTEINE ENDOPEPTIDASES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; FLUORESCENCE; FLUORESCENT DYES; GLUCURONIDASE; HELA CELLS; HISTIDINE; HUMANS; KINETICS; POLIOVIRUS; POLYPROTEINS; PROTEASE INHIBITORS; RECOMBINANT PROTEINS; VIRAL PROTEINS;

EID: 0033959458     PISSN: 01660934     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-0934(99)00138-X     Document Type: Article

References (20)

1. Bazan J.F., Fletterick R.J. Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications. Proc. Natl. Acad. Sci. U.S.A. 85:1988;7872-7876.
2. Blair W.S., Semler B.L. Role for the P4 amino acid residue in substrate utilization by the poliovirus 3CD proteinase. J. Virol. 65:1991;6111-6123.
3. Cordingley M.J., Register R.B., Callahan P.L., Garsky V.M., Colonno R.J. Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli. J. Virol. 63:1989;5037-5045.
4. Hanecak R., Semler B.L., Anderson C.W., Wimmer E. Proteolytic processing of poliovirus polypeptides: antibodies to polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs. Proc. Natl. Acad. Sci. U.S.A. 79:1982;3973-3977.
5. Hanecak R., Semler B.L., Ariga H., Anderson C.W., Wimmer E. Expression of a cloned gene segment of poliovirus in E. coli: evidence for autocatalytic production of the viral proteinase. Cell. 37:1984;1063-1073.
6. Jore J., Geus B.D., Jackson R.J., Pouwels P.H., Enger-Vark B.E. Poliovirus protein 3CD is active protease for processing of the precursor protein P1 in vitro. J. Gen. Virol. 69:1988;1627-1636.
7. Kitamura N., Semler B.L., Rothberg P.G., Larsen G.R., Adler C.J., Dorner A.J., Emini E.A., Hanecak R., Lee J.J., Werf S., Anderson C.W., Wimmer E. Primary structure, gene organization and polypeptide expression of poliovirus RNA. Nature. 291:1981;547-553.
8. Kondo H., Ijiri S., Abe K., Maeda H., Arai S. Inhibitory effect of oryzacystatin and a truncation mutant on the replication of poliovirus in infected Vero cells. FEBS Lett. 299:1992;48-50.
9. Korant B.D., Brzin J., Turk V. Cystatin, a protein inhibitor of cysteine proteases alters viral protein cleavages in infected human cells. Biochem. Biophys. Res. Commun. 127:1985;1072-1076.
10. Kräusslich H.G., Nicklin M.J.H., Toyoda H., Etchison D., Wimmer E. Poliovirus proteinase 2A induces cleavage of eucaryotic initiation factor 4F polypeptide p220. J. Virol. 61:1987;2711-2718.
11. Laemmli U.K. Cleavage of structual proteins during the assembly of the head of bcteriophage T4. Nature. 227:1970;680-685.
12. Lawson M.A., Semler B.L. Poliovirus thiol proteinase 3C can utilize a serine nucleophile within the putative catalytic triad. Proc. Natl. Acad. Sci. U.S.A. 88:1991;9919-9923.
13. Matthews D.A., Smith W.W., Ferre R.A., Condon B., Budahazi G., Sisson W., Villafranca J.E., Janson C.A., McElroy H.E., Gribskov C.L., Worland S. Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein. Cell. 77:1994;761-771.
14. Nagase H., Fields C.G., Fields G.B. Design and characterization of a fluorogenic substrate selectively hydrolyzed by stromelysin 1 (matrix metalloprotease-3). J. Biol. Chem. 269:1994;20952-20957.
15. Nicklin M.J.H., Harris K.S., Pallai P.V., Wimmer E. Poliovirus proteinase 3C: large-scale expression, purification, and specific cleavage activity on natural and synthetic substrates in vitro. J. Virol. 62:1988;4586-4593.
16. Orr D.C., Long A.C., Kay J., Dunn B.M., Cameron J.M. Hydrolysis of a series of synthetic peptide substrates by the human rhinovirus 14 3C proteinase, cloned and expressed in Escherichia coli. J. Gen. Virol. 70:1989;2931-2942.
17. Pallai P.V., Burkhardt F., Skoog M., Schreiner K., Bax P., Cohen K.A., Hansen G., Palladino D.E.H., Harris K.S., Nicklin M.J., Wimmer E. Cleavage of synthetic peptides by purified poliovirus 3C proteinase. J. Biol. Chem. 264:1989;9738-9741.
18. Racaniello V.R., Baltimore D. Molecular cloning of poliovirus cDNA and determination of the complete nucleotide sequence of the viral genome. Proc. Natl. Acad. Sci. U.S.A. 78:1981;4887-4891.
19. Sablina E.P., Antonov V.K. Recombinant poliovirus 3C protease. FEBS Lett. 283:1991;291-294.
20. Weidner J.R., Dunn B.M. Development of synthetic peptide substrates for the poliovirus 3C proteinase. Arch. Biochem. Biophys. 286:1991;402-408.