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Volumn 397, Issue 1, 2006, Pages 203-211

Probing the substrate specificity of the dengue virus type 2 NS3 serine protease by using internally quenched fluorescent peptides

Author keywords

3 nitrotyrosine; Dengue virus; Dengue virus non structural protein 3 (NS3) serine protease; Fluorescence; Polyprotein; Substrate specificity

Indexed keywords

AMINO ACIDS; BIOCHEMICAL ENGINEERING; FLUORESCENCE; POLYPEPTIDES; PROTEINS; QUENCHING; SUBSTRATES;

EID: 33745516142     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051767     Document Type: Article
Times cited : (52)

References (42)
  • 1
    • 0025864149 scopus 로고
    • Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins
    • Falgout, B., Pethel, M., Zhang, Y. M. and Lai, C. J. (1991) Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins. J. Virol. 65, 2467-2475
    • (1991) J. Virol. , vol.65 , pp. 2467-2475
    • Falgout, B.1    Pethel, M.2    Zhang, Y.M.3    Lai, C.J.4
  • 2
    • 0025201350 scopus 로고
    • Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein
    • Chambers, T. J., Weir, R. C., Grakoui, A., McCourt, D. W., Bazan, J. F., Fletterick, R. J. and Rice, C. M. (1990) Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein. Proc. Natl. Acad. Sci. U.S.A. 87, 8898-8902
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 8898-8902
    • Chambers, T.J.1    Weir, R.C.2    Grakoui, A.3    McCourt, D.W.4    Bazan, J.F.5    Fletterick, R.J.6    Rice, C.M.7
  • 3
    • 0025033393 scopus 로고
    • In vitro processing of dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3
    • Preugschat, F., Yao, C. W. and Strauss, J. H. (1990) In vitro processing of dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3. J. Virol. 64, 4364-4374
    • (1990) J. Virol. , vol.64 , pp. 4364-4374
    • Preugschat, F.1    Yao, C.W.2    Strauss, J.H.3
  • 4
    • 0026322815 scopus 로고
    • Processing of nonstructural proteins NS4A and NS4B of dengue 2 virus in vitro and in vivo
    • Preugschat, F. and Strauss, J. H. (1991) Processing of nonstructural proteins NS4A and NS4B of dengue 2 virus in vitro and in vivo. Virology 185, 689-697
    • (1991) Virology , vol.185 , pp. 689-697
    • Preugschat, F.1    Strauss, J.H.2
  • 5
    • 0027285404 scopus 로고
    • Dengue 2 virus NS2B and NS3 form a stable complex that can cleave NS3 within the helicase domain
    • Arias, C. F., Preugschat, F. and Strauss, J. H. (1993) Dengue 2 virus NS2B and NS3 form a stable complex that can cleave NS3 within the helicase domain. Virology 193, 888-899
    • (1993) Virology , vol.193 , pp. 888-899
    • Arias, C.F.1    Preugschat, F.2    Strauss, J.H.3
  • 6
    • 0027475018 scopus 로고
    • Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 proteinase is a prerequisite for processing at the downstream 4A/4B signalase site
    • Lin, C., Amberg, S. M., Chambers, T. J. and Rice, C. M. (1993) Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 proteinase is a prerequisite for processing at the downstream 4A/4B signalase site. J. Virol. 67, 2327-2335
    • (1993) J. Virol. , vol.67 , pp. 2327-2335
    • Lin, C.1    Amberg, S.M.2    Chambers, T.J.3    Rice, C.M.4
  • 7
    • 0027264853 scopus 로고
    • Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3
    • Lobigs, M. (1993) Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3. Proc. Natl. Acad. Sci. U.S.A. 90, 6218-6222
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6218-6222
    • Lobigs, M.1
  • 8
    • 0031020347 scopus 로고    scopus 로고
    • Internal proteolysis of the NS3 protein specified by dengue virus 2
    • Teo, K. F. and Wright, P. J. (1997) Internal proteolysis of the NS3 protein specified by dengue virus 2. J. Gen. Virol. 78, 337-341
    • (1997) J. Gen. Virol. , vol.78 , pp. 337-341
    • Teo, K.F.1    Wright, P.J.2
  • 9
    • 0036388978 scopus 로고    scopus 로고
    • Inhibiting viral proteases: Challenges and opportunities
    • Bianchi, E. and Pessi, A. (2002) Inhibiting viral proteases: challenges and opportunities. Biopolymers 66, 101-114
    • (2002) Biopolymers , vol.66 , pp. 101-114
    • Bianchi, E.1    Pessi, A.2
  • 10
    • 0035112985 scopus 로고    scopus 로고
    • A personal account of the role of peptide research in drug discovery: The case of hepatitis C
    • Pessi, A. (2001) A personal account of the role of peptide research in drug discovery: the case of hepatitis C. J. Pept. Sci. 7, 2-14
    • (2001) J. Pept. Sci. , vol.7 , pp. 2-14
    • Pessi, A.1
  • 11
    • 0031898959 scopus 로고    scopus 로고
    • Virus-encoded proteinases of the Flaviviridae
    • Ryan, M. D., Monaghan, S. and Flint, M. (1998) Virus-encoded proteinases of the Flaviviridae. J. Gen. Virol. 79, 947-959
    • (1998) J. Gen. Virol. , vol.79 , pp. 947-959
    • Ryan, M.D.1    Monaghan, S.2    Flint, M.3
  • 12
    • 0032976077 scopus 로고    scopus 로고
    • The serine protease and RNA-stimulated nucleoside triphosphatase and RNA helicase functional domains of dengue virus type 2 NS3 converge within a region of 20 amino acids
    • Li, H., Clum, S., You, S., Ebner, K. E. and Padmanabhan, R. (1999) The serine protease and RNA-stimulated nucleoside triphosphatase and RNA helicase functional domains of dengue virus type 2 NS3 converge within a region of 20 amino acids. J. Virol. 73, 3108-3116
    • (1999) J. Virol. , vol.73 , pp. 3108-3116
    • Li, H.1    Clum, S.2    You, S.3    Ebner, K.E.4    Padmanabhan, R.5
  • 13
    • 0024341494 scopus 로고
    • N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases
    • Gorbalenya, A. E., Donchenko, A. P., Koonin, E. V. and Blinov, V. M. (1989) N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases. Nucleic Acids Res. 17, 3889-3897
    • (1989) Nucleic Acids Res. , vol.17 , pp. 3889-3897
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Koonin, E.V.3    Blinov, V.M.4
  • 14
    • 0030897821 scopus 로고    scopus 로고
    • Virus-encoded RNA helicases
    • Kadare, G. and Haenni, A. L. (1997) Virus-encoded RNA helicases. J. Virol. 71, 2583-2590
    • (1997) J. Virol. , vol.71 , pp. 2583-2590
    • Kadare, G.1    Haenni, A.L.2
  • 15
    • 0036037499 scopus 로고    scopus 로고
    • Expression, purification, and characterization of the RNA 5′-triphosphatase activity of dengue virus type 2 nonstructural protein 3
    • Bartelma, G. and Padmanabhan, R. (2002) Expression, purification, and characterization of the RNA 5′-triphosphatase activity of dengue virus type 2 nonstructural protein 3. Virology 299, 122-132
    • (2002) Virology , vol.299 , pp. 122-132
    • Bartelma, G.1    Padmanabhan, R.2
  • 16
    • 0026039916 scopus 로고
    • Processing of the yellow fever virus nonstructural polyprotein: A catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sites
    • Chambers, T. J., Grakoui, A. and Rice, C. M. (1991) 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. 65, 6042-6050
    • (1991) J. Virol. , vol.65 , pp. 6042-6050
    • Chambers, T.J.1    Grakoui, A.2    Rice, C.M.3
  • 17
    • 0025865788 scopus 로고
    • In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acids
    • Wengler, G., Czaya, G., Farber, P. M. and Hegemann, J. H. (1991) In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acids. J. Gen. Virol. 72, 851-858
    • (1991) J. Gen. Virol. , vol.72 , pp. 851-858
    • Wengler, G.1    Czaya, G.2    Farber, P.M.3    Hegemann, J.H.4
  • 18
    • 0026471347 scopus 로고
    • Processing and localization of dengue virus type 2 polyprotein precursor NS3-NS4A-NS4B-NS5
    • Zhang, L., Mohan, P. M. and Padmanabhan, R. (1992) Processing and localization of dengue virus type 2 polyprotein precursor NS3-NS4A-NS4B-NS5. J. Virol. 66, 7549-7554
    • (1992) J. Virol. , vol.66 , pp. 7549-7554
    • Zhang, L.1    Mohan, P.M.2    Padmanabhan, R.3
  • 19
    • 0027499688 scopus 로고
    • Deletion analysis of dengue virus type 4 nonstructural protein NS2B: Identification of a domain required for NS2B-NS3 protease activity
    • Falgout, B., Miller, R. H. and Lai, C. J. (1993) Deletion analysis of dengue virus type 4 nonstructural protein NS2B: identification of a domain required for NS2B-NS3 protease activity. J. Virol. 67, 2034-2042
    • (1993) J. Virol. , vol.67 , pp. 2034-2042
    • Falgout, B.1    Miller, R.H.2    Lai, C.J.3
  • 21
    • 0033522886 scopus 로고    scopus 로고
    • The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism
    • Barbato, G., Cicero, D. O., Nardi, M. C., Steinkuhler, C., Cortese, R., De Francesco, R. and Bazzo, R. (1999) The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism. J. Mol. Biol. 289, 371-384
    • (1999) J. Mol. Biol. , vol.289 , pp. 371-384
    • Barbato, G.1    Cicero, D.O.2    Nardi, M.C.3    Steinkuhler, C.4    Cortese, R.5    De Francesco, R.6    Bazzo, R.7
  • 23
    • 0030667792 scopus 로고    scopus 로고
    • Cotranslational membrane insertion of the serine proteinase precursor NS2B-NS3(Pro) of dengue virus type 2 is required for efficient in vitro processing and is mediated through the hydrophobic regions of NS2B
    • Clum, S., Ebner, K. E. and Padmanabhan, R. (1997) Cotranslational membrane insertion of the serine proteinase precursor NS2B-NS3(Pro) of dengue virus type 2 is required for efficient in vitro processing and is mediated through the hydrophobic regions of NS2B. J. Biol. Chem. 272, 30715-30723
    • (1997) J. Biol. Chem. , vol.272 , pp. 30715-30723
    • Clum, S.1    Ebner, K.E.2    Padmanabhan, R.3
  • 24
    • 0033605260 scopus 로고    scopus 로고
    • Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects
    • Murthy, H. M., Clum, S. and Padmanabhan, R. (1999) Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects. J. Biol. Chem. 274, 5573-5580
    • (1999) J. Biol. Chem. , vol.274 , pp. 5573-5580
    • Murthy, H.M.1    Clum, S.2    Padmanabhan, R.3
  • 25
    • 0036004555 scopus 로고    scopus 로고
    • In vitro determination of dengue virus type 2 NS2B-NS3 protease activity with fluorescent peptide substrates
    • Khumthong, R., Angsuthanasombat, C., Panyim, S. and Katzenmeier, G. (2002) In vitro determination of dengue virus type 2 NS2B-NS3 protease activity with fluorescent peptide substrates. J. Biochem. Mol. Biol. 35, 206-212
    • (2002) J. Biochem. Mol. Biol. , vol.35 , pp. 206-212
    • Khumthong, R.1    Angsuthanasombat, C.2    Panyim, S.3    Katzenmeier, G.4
  • 27
    • 0035824539 scopus 로고    scopus 로고
    • Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors
    • Leung, D., Schroder, K., White, H., Fang, N. X., Stoermer, M. J., Abbenante, G., Martin, J. L., Young, P. R. and Fairlie, D. P. (2001) 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. 276, 45762-45771
    • (2001) J. Biol. Chem. , vol.276 , pp. 45762-45771
    • Leung, D.1    Schroder, K.2    White, H.3    Fang, N.X.4    Stoermer, M.J.5    Abbenante, G.6    Martin, J.L.7    Young, P.R.8    Fairlie, D.P.9
  • 28
    • 23344446921 scopus 로고    scopus 로고
    • Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetra- and octa-peptide substrate libraries
    • Li, J., Lim, S. P., Beer, D., Patel, V., Wen, D., Tumanut, C., Tully, D. C., Williams, J. A., Jiricek, J., Priestle, J. P. et al. (2005) Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetra- and octa-peptide substrate libraries. J. Biol. Chem. 280, 28766-28774
    • (2005) J. Biol. Chem. , vol.280 , pp. 28766-28774
    • Li, J.1    Lim, S.P.2    Beer, D.3    Patel, V.4    Wen, D.5    Tumanut, C.6    Tully, D.C.7    Williams, J.A.8    Jiricek, J.9    Priestle, J.P.10
  • 30
    • 0033557480 scopus 로고    scopus 로고
    • Use of a fluorescence plate reader for measuring kinetic parameters with inner filter effect correction
    • Liu, Y., Kati, W., Chen, C. M., Tripathi, R., Molla, A. and Kohlbrenner, W. (1999) Use of a fluorescence plate reader for measuring kinetic parameters with inner filter effect correction. Anal. Biochem. 267, 331-335
    • (1999) Anal. Biochem. , vol.267 , pp. 331-335
    • Liu, Y.1    Kati, W.2    Chen, C.M.3    Tripathi, R.4    Molla, A.5    Kohlbrenner, W.6
  • 31
    • 0036171240 scopus 로고    scopus 로고
    • Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease
    • Kuyumcu-Martinez, N. M., Joachims, M. and Lloyd, R. E. (2002) Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease. J. Virol. 76, 2062-2074
    • (2002) J. Virol. , vol.76 , pp. 2062-2074
    • Kuyumcu-Martinez, N.M.1    Joachims, M.2    Lloyd, R.E.3
  • 32
    • 0035929633 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus leader proteinase: Involvement of C-terminal residues in self-processing and cleavage of eIF4GI
    • Glaser, W., Cencic, R. and Skern, T. (2001) Foot-and-mouth disease virus leader proteinase: involvement of C-terminal residues in self-processing and cleavage of eIF4GI. J. Biol. Chem. 276, 35473-35481
    • (2001) J. Biol. Chem. , vol.276 , pp. 35473-35481
    • Glaser, W.1    Cencic, R.2    Skern, T.3
  • 33
    • 0033588099 scopus 로고    scopus 로고
    • Revisiting catalysis by chymotrypsin family serine proteases using peptide substrates and inhibitors with unnatural main chains
    • Coombs, G. S., Rao, M. S., Olson, A. J., Dawson, P. E. and Madison, E. L. (1999) Revisiting catalysis by chymotrypsin family serine proteases using peptide substrates and inhibitors with unnatural main chains. J. Biol. Chem. 274, 24074-24079
    • (1999) J. Biol. Chem. , vol.274 , pp. 24074-24079
    • Coombs, G.S.1    Rao, M.S.2    Olson, A.J.3    Dawson, P.E.4    Madison, E.L.5
  • 34
    • 0033214037 scopus 로고    scopus 로고
    • The C-terminal sequence encodes function in serine proteases
    • Krem, M. M., Rose, T. and Di Cera, E. (1999) The C-terminal sequence encodes function in serine proteases. J. Biol. Chem. 274, 28063-28066
    • (1999) J. Biol. Chem. , vol.274 , pp. 28063-28066
    • Krem, M.M.1    Rose, T.2    Di Cera, E.3
  • 35
    • 0030729481 scopus 로고    scopus 로고
    • Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold
    • Perona, J. J. and Craik, C. S. (1997) Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. J. Biol. Chem. 272, 29987-29990
    • (1997) J. Biol. Chem. , vol.272 , pp. 29987-29990
    • Perona, J.J.1    Craik, C.S.2
  • 36
    • 0028201374 scopus 로고
    • Role of the S′ subsites in serine protease catalysis. Active-site mapping of rat chymotrypsin, rat trypsin, alpha-lytic protease, and cercarial protease from Schistosoma mansoni
    • Schellenberger, V., Turck, C. W. and Rutter, W. J. (1994) Role of the S′ subsites in serine protease catalysis. Active-site mapping of rat chymotrypsin, rat trypsin, alpha-lytic protease, and cercarial protease from Schistosoma mansoni. Biochemistry 33, 4251-4257
    • (1994) Biochemistry , vol.33 , pp. 4251-4257
    • Schellenberger, V.1    Turck, C.W.2    Rutter, W.J.3
  • 37
    • 0034714111 scopus 로고    scopus 로고
    • Crystal structure of Dengue virus NS3 protease in complex with a Bowman-Birk inhibitor: Implications for flaviviral polyprotein processing and drug design
    • Murthy, H. M., Judge, K., DeLucas, L. and Padmanabhan, R. (2000) Crystal structure of Dengue virus NS3 protease in complex with a Bowman-Birk inhibitor: implications for flaviviral polyprotein processing and drug design. J. Mol. Biol. 301, 759-767
    • (2000) J. Mol. Biol. , vol.301 , pp. 759-767
    • Murthy, H.M.1    Judge, K.2    DeLucas, L.3    Padmanabhan, R.4
  • 38
    • 0034616194 scopus 로고    scopus 로고
    • Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro
    • Yusof, R., Clum, S., Wetzel, M., Murthy, H. M. and Padmanabhan, R. (2000) Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro. J. Biol. Chem. 275, 9963-9969
    • (2000) J. Biol. Chem. , vol.275 , pp. 9963-9969
    • Yusof, R.1    Clum, S.2    Wetzel, M.3    Murthy, H.M.4    Padmanabhan, R.5
  • 39
    • 0037184036 scopus 로고    scopus 로고
    • The interdomain region of dengue NS5 protein that binds to the viral helicase NS3 contains independently functional importin beta 1 and importin alpha/beta-recognized nuclear localization signals
    • Brooks, A. J., Johansson, M., John, A. V., Xu, Y., Jans, D. A. and Vasudevan, S. G. (2002) The interdomain region of dengue NS5 protein that binds to the viral helicase NS3 contains independently functional importin beta 1 and importin alpha/beta-recognized nuclear localization signals. J. Biol. Chem. 277, 36399-36407
    • (2002) J. Biol. Chem. , vol.277 , pp. 36399-36407
    • Brooks, A.J.1    Johansson, M.2    John, A.V.3    Xu, Y.4    Jans, D.A.5    Vasudevan, S.G.6
  • 40
    • 22844443626 scopus 로고    scopus 로고
    • Modulation of the nucleoside triphosphatase/RNA helicase and 5′-RNA triphosphatase activities of dengue virus type 2 nonstructural protein 3 (NS3) by interaction with NS5, the RNA-dependent RNA polymerase
    • Yon, C., Teramoto, T., Mueller, N., Phelan, J., Ganesh, V. K., Murthy, K. H. and Padmanabhan, R. (2005) Modulation of the nucleoside triphosphatase/RNA helicase and 5′-RNA triphosphatase activities of dengue virus type 2 nonstructural protein 3 (NS3) by interaction with NS5, the RNA-dependent RNA polymerase. J. Biol. Chem. 280, 27412-27419
    • (2005) J. Biol. Chem. , vol.280 , pp. 27412-27419
    • Yon, C.1    Teramoto, T.2    Mueller, N.3    Phelan, J.4    Ganesh, V.K.5    Murthy, K.H.6    Padmanabhan, R.7
  • 41
    • 0033818886 scopus 로고    scopus 로고
    • The structure of the pro-apoptotic protease granzyme B reveals the molecular determinants of its specificity
    • Waugh, S. M., Harris, J. L., Fletterick, R. and Craik, C. S. (2000) The structure of the pro-apoptotic protease granzyme B reveals the molecular determinants of its specificity. Nat. Struct. Biol. 7, 762-765
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 762-765
    • Waugh, S.M.1    Harris, J.L.2    Fletterick, R.3    Craik, C.S.4


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