Yellow fever virus NS2B/NS3 protease: Hydrolytic Properties and Substrate Specificity

Biochemical and Biophysical Research Communications

Volumn 407, Issue 4, 2011, Pages 640-644

  Kondo, Marcia Y ^a   Oliveira, Lilian C G ^a   Okamoto, Debora N ^a   de Araujo, Marina R T ^b   Duarte dos Santos, Claudia N ^b   Juliano, Maria A ^a   Juliano, Luiz ^a   Gouvea, Iuri E ^a  

^a FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

^b INSTITUTO CARLOS CHAGAS   (Brazil)

Author keywords

Dengue; Enzyme kinetics; Flavivirus; FRET substrate; Serine proteases

Indexed keywords

ARGININE; LYSINE; UNCLASSIFIED DRUG; VIRUS ENZYME; YELLOW FEVER FLAVIVIRUS NS2A NS2B PROTEASE; YELLOW FEVER FLAVIVIRUS NS2B NS3 PROTEASE; YELLOW FEVER FLAVIVIRUS NS3 NS4 PROTEASE; YELLOW FEVER FLAVIVIRUS NS4A NS4B PROTEASE; YELLOW FEVER FLAVIVIRUS NS4B NS5 PROTEASE;

ARTICLE; CATALYSIS; CIRCULAR DICHROISM; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE RESONANCE ENERGY TRANSFER; HYDROLYSIS; IN VIVO STUDY; IONIC STRENGTH; PH; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE;

AMINO ACID MOTIFS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; PEPTIDES; RECOMBINANT PROTEINS; RNA HELICASES; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY; VIRAL NONSTRUCTURAL PROTEINS; YELLOW FEVER VIRUS;

FLAVIVIRUS; WEST NILE VIRUS; YELLOW FEVER VIRUS;

EID: 79954992689     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.03.054     Document Type: Article

References (27)

1. Monath T.P. Treatment of yellow fever. Antiviral Res. 2008, 78:116-124.
2. W.H. Organization, Yellow Fever, The Weekly Epidemiological Record (WER), 2009.
3. A.D.T. Barrett, T.P. Monath, V. Barban, M. Niedrig, D.E. Teuwen, 17D yellow fever vaccines: New insights - A report of a workshop held during the World Congress on Medicine and Health in the Tropics, Marseille, France, Monday 12 September 2005, Vaccine 25 (2007) 2758-2765.
4. Chambers T.J., Grakoui A., Rice C.M. Processing of the yellow fever virus nonstructural polyprotein: a catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sites. J. Virol. 1991, 65:6042-6050.
5. Weaver S.C., Barrett A.D. Transmission cycles, host range, evolution and emergence of arboviral disease. Nat. Rev. Microbiol. 2004, 2:789-801.
6. Amberg S.M., Nestorowicz A., McCourt D.W., Rice C.M. NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: in vitro and in vivo studies. J. Virol. 1994, 68:3794-3802.
7. Bessaud M., Pastorino B.A., Peyrefitte C.N., Rolland D., Grandadam M., Tolou H.J. Functional characterization of the NS2B/NS3 protease complex from seven viruses belonging to different groups inside the genus Flavivirus. Virus Res. 2006, 120:79-90.
8. Lescar J., Luo D., Xu T., Sampath A., Lim S.P., Canard B., Vasudevan S.G. Towards the design of antiviral inhibitors against flaviviruses: the case for the multifunctional NS3 protein from Dengue virus as a target. Antiviral Res. 2008, 80:94-101.
9. Sampath A., Padmanabhan R. Molecular targets for flavivirus drug discovery. Antiviral Res. 2009, 81:6-15.
10. Arias C.F., Preugschat F., Strauss J.H. Dengue-2 virus Ns2B and Ns3 form a stable complex that can cleave Ns3 within the helicase domain. Virology 1993, 193:888-899.
11. Erbel P., Schiering N., D'Arcy A., Renatus M., Kroemer M., Lim S.P., Yin Z., Keller T.H., Vasudevan S.G., Hommel U. Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus. Nat. Struct. Mol. Biol. 2006, 13:372-373.
12. Aleshin A.E., Shiryaev S.A., Strongin A.Y., Liddington R.C. Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold. Protein Sci. 2007, 16:795-806.
13. Nall T.A., Chappell K.J., Stoermer M.J., Fang N.X., Tyndall J.D.A., Young P.R., Fairlie D.P. Enzymatic characterization and homology model of a catalytically active recombinant West Nile virus NS3 protease. J. Biol. Chem. 2004, 279:48535-48542.
14. Chanprapaph S., Saparpakorn P., Sangma C., Niyomrattanakit P., Hannongbua S., Angsuthanasombat C., Katzenmeier G. Competitive inhibition of the dengue virus NS3 serine protease by synthetic peptides representing polyprotein cleavage sites. Biochem. Biophys. Res. Commun. 2005, 330:1237-1246.
15. Kelly S.M., Jess T.J., Price N.C. How to study proteins by circular dichroism. Bba-Proteins Proteom. 2005, 1751:119-139.
16. Jan L.R., Yang C.S., Trent D.W., Falgout B., Lai C.J. Processing of Japanese Encephalitis-Virus Nonstructural Proteins - Ns2B-Ns3 Complex and Heterologous Proteases. J. Gen. Virol. 1995, 76:573-580.
17. Amberg S.M., Nestorowicz A., Mccourt D.W., Rice C.M. Ns2B-3 Proteinase-Mediated Processing in the Yellow-Fever Virus Structural Region - in-Vitro and in-Vivo Studies. J. Virol. 1994, 68:3794-3802.
18. Lohr K., Knox J.E., Phong W.Y., Ma N.L., Yin Z., Sampath A., Patel S.J., Wang W.L., Chan W.L., Rao K.R., Wang G., Vasudevan S.G., Keller T.H., Lim S.P. Yellow fever virus NS3 protease: peptide-inhibition studies. J. Gen. Virol. 2007, 88:2223-2227.
19. Pop C., Fitzgerald P., Green D.R., Salvesen G.S. Role of proteolysis in caspase-8 activation and stabilization. Biochemistry-Us 2007, 46:4398-4407.
20. Gouvea I.E., Izidoro M.A., Judice W.A., Cezari M.H., Caliendo G., Santagada V., dos Santos C.N., Queiroz M.H., Juliano M.A., Young P.R., Fairlie D.P., Juliano L. Substrate specificity of recombinant dengue 2 virus NS2B-NS3 protease: influence of natural and unnatural basic amino acids on hydrolysis of synthetic fluorescent substrates. Arch. Biochem. Biophys. 2007, 457:187-196.
21. Li J., Lim S.P., Beer D., Patel V., Wen D.Y., Tumanut C., Tully D.C., Williams J.A., Jiricek J., Priestle J.P., Harris J.L., Vasudevan S.G. Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries. J. Biol. Chem. 2005, 280:28766-28774.
22. Leung D., Schroder K., White H., Fang N.X., Stoermer M.J., Abbenante G., Martin J.L., Young P.R., Fairlie D.P. Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors. J. Biol. Chem. 2001, 276:45762-45771.
23. Niyomrattanakit P., Yahorava S., Mutule I., Mutulis F., Petrovska R., Prusis P., Katzenmeier G., Wikberg J.E.S. Probing the substrate specificity of the dengue virus type 2 NS3 serine protease by using internally quenched fluorescent peptides. Biochem. J. 2006, 397:203-211.
24. Hirata I.Y., Cezari, M.H.S., Nakaie, C., Boschcov, P., Ito, A.S., Juliano, M.A., Juliano, L. Internally quenched fluorogenic protease substrates: solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs. Lett. Pept. Sci. 1994, 1:299-308.
25. Liu Y.Y., Kati W., Chen C.M., Tripathi R., Molla A., Kohlbrenner W. Use of a fluorescence plate reader for measuring kinetic parameters with inner filter effect correction. Anal. Biochem. 1999, 267:331-335.
26. Fan K., Wei P., Feng Q., Chen S., Huang C., Ma L., Lai B., Pei J., Liu Y., Chen J., Lai L., Biosynthesis, purification and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase. J. Biol. Chem. 2004, 279:1637-1642.
27. Condotta S.A., Martin M.M., Boutin M., Jean F. Detection and in-cell selectivity profiling of the full-length West Nile virus NS2B/NS3 serine protease using membrane-anchored fluorescent substrates. Biol. Chem. 2010, 391:549-559.