메뉴 건너뛰기




Volumn 423, Issue 2, 2012, Pages 125-133

Characterization and inhibition of norovirus proteases of genogroups I and II using a fluorescence resonance energy transfer assay

Author keywords

Antiviral; Chymostatin; Fluorescence resonance energy transfer; MD145 virus; Norwalk virus; Nuclear magnetic resonance spectroscopy; Viral proteases

Indexed keywords

CHYMOSTATIN; PROTEINASE; PROTEINASE INHIBITOR;

EID: 84855787364     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2011.12.002     Document Type: Article
Times cited : (32)

References (53)
  • 1
    • 33746356187 scopus 로고    scopus 로고
    • The epidemiologic and clinical importance of norovirus infection
    • (viii)
    • Atmar R.L., Estes M.K. The epidemiologic and clinical importance of norovirus infection. Gastroenterol. Clin. North Am. 2006, 35(2):275-290. (viii).
    • (2006) Gastroenterol. Clin. North Am. , vol.35 , Issue.2 , pp. 275-290
    • Atmar, R.L.1    Estes, M.K.2
  • 2
    • 0141677707 scopus 로고    scopus 로고
    • In vitro proteolytic processing of the MD145 norovirus ORF1 nonstructural polyprotein yields stable precursors and products similar to those detected in calicivirus-infected cells
    • Belliot G., Sosnovtsev S.V., Mitra T., Hammer C., Garfield M., Green K.Y. In vitro proteolytic processing of the MD145 norovirus ORF1 nonstructural polyprotein yields stable precursors and products similar to those detected in calicivirus-infected cells. J. Virol. 2003, 77(20):10957-10974.
    • (2003) J. Virol. , vol.77 , Issue.20 , pp. 10957-10974
    • Belliot, G.1    Sosnovtsev, S.V.2    Mitra, T.3    Hammer, C.4    Garfield, M.5    Green, K.Y.6
  • 4
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W., Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 1992, 204(2):433-451.
    • (1992) Eur. J. Biochem. , vol.204 , Issue.2 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 6
    • 19944427356 scopus 로고    scopus 로고
    • Enzymatic activity characterization of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer technique
    • Chen S., Chen L.L., Luo H.B., Sun T., Chen J., Ye F., Cai J.H., Shen J.K., Shen X., Jiang H.L. Enzymatic activity characterization of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer technique. Acta Pharmacol. Sin. 2005, 26(1):99-106.
    • (2005) Acta Pharmacol. Sin. , vol.26 , Issue.1 , pp. 99-106
    • Chen, S.1    Chen, L.L.2    Luo, H.B.3    Sun, T.4    Chen, J.5    Ye, F.6    Cai, J.H.7    Shen, J.K.8    Shen, X.9    Jiang, H.L.10
  • 7
    • 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., Madison E.L. Revisiting catalysis by chymotrypsin family serine proteases using peptide substrates and inhibitors with unnatural main chains. J. Biol. Chem. 1999, 274(34):24074-24079.
    • (1999) J. Biol. Chem. , vol.274 , Issue.34 , pp. 24074-24079
    • Coombs, G.S.1    Rao, M.S.2    Olson, A.J.3    Dawson, P.E.4    Madison, E.L.5
  • 8
    • 28844491633 scopus 로고    scopus 로고
    • Determination of peptide substrate specificity for mu-calpain by a peptide library-based approach: the importance of primed side interactions
    • Cuerrier D., Moldoveanu T., Davies P.L. Determination of peptide substrate specificity for mu-calpain by a peptide library-based approach: the importance of primed side interactions. J. Biol. Chem. 2005, 280(49):40632-40641.
    • (2005) J. Biol. Chem. , vol.280 , Issue.49 , pp. 40632-40641
    • Cuerrier, D.1    Moldoveanu, T.2    Davies, P.L.3
  • 9
    • 77955391393 scopus 로고    scopus 로고
    • The HADDOCK web server for data-driven biomolecular docking. Nat. Protoc. 5 (5)
    • de Vries, S.J., van Dijk, M., Bonvin, A.M., 2010. The HADDOCK web server for data-driven biomolecular docking. Nat. Protoc. 5 (5), 883-897.
    • (2010) , pp. 883-897
    • De Vries, S.J.1    Van Dijk, M.2    Bonvin, A.M.3
  • 10
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 1995, 6(3):277-293.
    • (1995) J. Biomol. NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 11
    • 84873068298 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System. DeLano Scientific LLC, San Carlos, CA.
    • DeLano, W.L., 2010. The PyMOL Molecular Graphics System. DeLano Scientific LLC, San Carlos, CA.
    • DeLano, W.L.1
  • 12
    • 34548726086 scopus 로고    scopus 로고
    • Noroviruses-challenges to control
    • Dolin R. Noroviruses-challenges to control. N. Engl. J. Med. 2007, 357(11):1072-1073.
    • (2007) N. Engl. J. Med. , vol.357 , Issue.11 , pp. 1072-1073
    • Dolin, R.1
  • 13
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: a protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C., Boelens R., Bonvin A.M. HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 2003, 125(7):1731-1737.
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.7 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 14
    • 0031736983 scopus 로고    scopus 로고
    • Molecular epidemiology of "Norwalk-like viruses" in outbreaks of gastroenteritis in the United States
    • Fankhauser R.L., Noel J.S., Monroe S.S., Ando T., Glass R.I. Molecular epidemiology of "Norwalk-like viruses" in outbreaks of gastroenteritis in the United States. J. Infect. Dis. 1998, 178(6):1571-1578.
    • (1998) J. Infect. Dis. , vol.178 , Issue.6 , pp. 1571-1578
    • Fankhauser, R.L.1    Noel, J.S.2    Monroe, S.S.3    Ando, T.4    Glass, R.I.5
  • 18
    • 34548415971 scopus 로고    scopus 로고
    • Caliciviruses: the noroviruses
    • Lippincott Williams & Wilkins, Philadelphia, D.M. Knipe, P.M. Howley (Eds.)
    • Green K.Y. Caliciviruses: the noroviruses. Fields Virology 2007, 1. Lippincott Williams & Wilkins, Philadelphia. 5th ed. D.M. Knipe, P.M. Howley (Eds.).
    • (2007) Fields Virology , pp. 1
    • Green, K.Y.1
  • 19
    • 0001248233 scopus 로고    scopus 로고
    • Human caliciviruses
    • Lippincott Williams & Wilkins, Philadelphia, D.M. Knipe, P.M. Howley (Eds.)
    • Green K.Y., Chanock R.M., Kapikian A.Z. Human caliciviruses. Fields Virology 2001, Vol. 1:841-874. Lippincott Williams & Wilkins, Philadelphia. 4 ed. D.M. Knipe, P.M. Howley (Eds.).
    • (2001) Fields Virology , vol.1 , pp. 841-874
    • Green, K.Y.1    Chanock, R.M.2    Kapikian, A.Z.3
  • 20
    • 0029881450 scopus 로고    scopus 로고
    • The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase
    • Grzesiek S., Bax A., Clore G.M., Gronenborn A.M., Hu J.S., Kaufman J., Palmer I., Stahl S.J., Wingfield P.T. The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nat. Struct. Biol. 1996, 3(4):340-345.
    • (1996) Nat. Struct. Biol. , vol.3 , Issue.4 , pp. 340-345
    • Grzesiek, S.1    Bax, A.2    Clore, G.M.3    Gronenborn, A.M.4    Hu, J.S.5    Kaufman, J.6    Palmer, I.7    Stahl, S.J.8    Wingfield, P.T.9
  • 21
    • 0036802230 scopus 로고    scopus 로고
    • Substrate specificity of the Norwalk virus 3C-like proteinase
    • Hardy M.E., Crone T.J., Brower J.E., Ettayebi K. Substrate specificity of the Norwalk virus 3C-like proteinase. Virus Res. 2002, 89(1):29-39.
    • (2002) Virus Res. , vol.89 , Issue.1 , pp. 29-39
    • Hardy, M.E.1    Crone, T.J.2    Brower, J.E.3    Ettayebi, K.4
  • 25
    • 84855794528 scopus 로고    scopus 로고
    • Calicivirus protein structures
    • Caister Academic Press, Norfolk, G.S. Hansman, X.J. Jiang, K.Y. Green (Eds.)
    • Ng K., Parra F. Calicivirus protein structures. Caliciviruses: Molecular and Cellular Virology 2010, 95-110. Caister Academic Press, Norfolk. G.S. Hansman, X.J. Jiang, K.Y. Green (Eds.).
    • (2010) Caliciviruses: Molecular and Cellular Virology , pp. 95-110
    • Ng, K.1    Parra, F.2
  • 26
    • 0015423669 scopus 로고
    • Visualization by immune electron microscopy of a 27-nm particle associated with acute infectious nonbacterial gastroenteritis
    • Kapikian A.Z., Wyatt R.G., Dolin R., Thornhill T.S., Kalica A.R., Chanock R.M. Visualization by immune electron microscopy of a 27-nm particle associated with acute infectious nonbacterial gastroenteritis. J. Virol. 1972, 10(5):1075-1081.
    • (1972) J. Virol. , vol.10 , Issue.5 , pp. 1075-1081
    • Kapikian, A.Z.1    Wyatt, R.G.2    Dolin, R.3    Thornhill, T.S.4    Kalica, A.R.5    Chanock, R.M.6
  • 27
    • 33745092046 scopus 로고    scopus 로고
    • Peptide, peptidomimetic and small-molecule drug discovery targeting HIV-1 host-cell attachment and entry through gp120, gp41, CCR5 and CXCR4
    • Kazmierski W.M., Kenakin T.P., Gudmundsson K.S. Peptide, peptidomimetic and small-molecule drug discovery targeting HIV-1 host-cell attachment and entry through gp120, gp41, CCR5 and CXCR4. Chem. Biol. Drug Des. 2006, 67(1):13-26.
    • (2006) Chem. Biol. Drug Des. , vol.67 , Issue.1 , pp. 13-26
    • Kazmierski, W.M.1    Kenakin, T.P.2    Gudmundsson, K.S.3
  • 30
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M., Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 1980, 49:593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 31
    • 0033008413 scopus 로고    scopus 로고
    • Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli
    • Liu B.L., Viljoen G.J., Clarke I.N., Lambden P.R. Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli. J. Gen. Virol. 1999, 80(Pt. 2):291-296.
    • (1999) J. Gen. Virol. , vol.80 , Issue.PART 2 , pp. 291-296
    • Liu, B.L.1    Viljoen, G.J.2    Clarke, I.N.3    Lambden, P.R.4
  • 34
    • 0345167058 scopus 로고    scopus 로고
    • Evolution of human calicivirus RNA in vivo: accumulation of mutations in the protruding P2 domain of the capsid leads to structural changes and possibly a new phenotype
    • Nilsson M., Hedlund K.O., Thorhagen M., Larson G., Johansen K., Ekspong A., Svensson L. Evolution of human calicivirus RNA in vivo: accumulation of mutations in the protruding P2 domain of the capsid leads to structural changes and possibly a new phenotype. J. Virol. 2003, 77(24):13117-13124.
    • (2003) J. Virol. , vol.77 , Issue.24 , pp. 13117-13124
    • Nilsson, M.1    Hedlund, K.O.2    Thorhagen, M.3    Larson, G.4    Johansen, K.5    Ekspong, A.6    Svensson, L.7
  • 36
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Robert Fraczkiewicz W.B. Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comput. Chem. 1998, 19(3):319-333.
    • (1998) J. Comput. Chem. , vol.19 , Issue.3 , pp. 319-333
    • Robert Fraczkiewicz, W.B.1
  • 38
    • 0034823633 scopus 로고    scopus 로고
    • Clinical severity of Norwalk virus and Sapporo virus gastroenteritis in children in Hokkaido, Japan
    • Sakai Y., Nakata S., Honma S., Tatsumi M., Numata-Kinoshita K., Chiba S. Clinical severity of Norwalk virus and Sapporo virus gastroenteritis in children in Hokkaido, Japan. Pediatr. Infect. Dis. J. 2001, 20(9):849-853.
    • (2001) Pediatr. Infect. Dis. J. , vol.20 , Issue.9 , pp. 849-853
    • Sakai, Y.1    Nakata, S.2    Honma, S.3    Tatsumi, M.4    Numata-Kinoshita, K.5    Chiba, S.6
  • 39
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 1967, 27(2):157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , Issue.2 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 40
    • 34347328307 scopus 로고    scopus 로고
    • Differential cleavage of the norovirus polyprotein precursor by two active forms of the viral protease
    • Scheffler U., Rudolph W., Gebhardt J., Rohayem J. Differential cleavage of the norovirus polyprotein precursor by two active forms of the viral protease. J. Gen. Virol. 2007, 88(Pt 7):2013-2018.
    • (2007) J. Gen. Virol. , vol.88 , Issue.PART 7 , pp. 2013-2018
    • Scheffler, U.1    Rudolph, W.2    Gebhardt, J.3    Rohayem, J.4
  • 41
    • 0345102433 scopus 로고    scopus 로고
    • Open reading frame 1 of the Norwalk-like virus Camberwell: completion of sequence and expression in mammalian cells
    • Seah E.L., Marshall J.A., Wright P.J. Open reading frame 1 of the Norwalk-like virus Camberwell: completion of sequence and expression in mammalian cells. J. Virol. 1999, 73(12):10531-10535.
    • (1999) J. Virol. , vol.73 , Issue.12 , pp. 10531-10535
    • Seah, E.L.1    Marshall, J.A.2    Wright, P.J.3
  • 42
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker S.B., Hajduk P.J., Meadows R.P., Fesik S.W. Discovering high-affinity ligands for proteins: SAR by NMR. Science 1996, 274(5292):1531-1534.
    • (1996) Science , vol.274 , Issue.5292 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 44
    • 79960417838 scopus 로고    scopus 로고
    • Norovirus epidemiology
    • Caister Academic Press, Norfolk, G.S. Hansman, X.J. Jians, K.Y. Green (Eds.)
    • Siebenga J.J., Duizer E., Koopmans M.P.G. Norovirus epidemiology. Caliciviruses 2010, 1-24. Caister Academic Press, Norfolk. G.S. Hansman, X.J. Jians, K.Y. Green (Eds.).
    • (2010) Caliciviruses , pp. 1-24
    • Siebenga, J.J.1    Duizer, E.2    Koopmans, M.P.G.3
  • 45
    • 70350045150 scopus 로고    scopus 로고
    • Insights into the enzyme-substrate interaction in the norovirus 3C-like protease
    • Someya Y., Takeda N. Insights into the enzyme-substrate interaction in the norovirus 3C-like protease. J. Biochem. 2009, 146(4):509-521.
    • (2009) J. Biochem. , vol.146 , Issue.4 , pp. 509-521
    • Someya, Y.1    Takeda, N.2
  • 46
    • 57749187792 scopus 로고    scopus 로고
    • Saturation mutagenesis reveals that GLU54 of norovirus 3C-like protease is not essential for the proteolytic activity
    • Someya Y., Takeda N., Wakita T. Saturation mutagenesis reveals that GLU54 of norovirus 3C-like protease is not essential for the proteolytic activity. J. Biochem. 2008, 144(6):771-780.
    • (2008) J. Biochem. , vol.144 , Issue.6 , pp. 771-780
    • Someya, Y.1    Takeda, N.2    Wakita, T.3
  • 48
    • 84858295982 scopus 로고    scopus 로고
    • Backbone and side-chain assignments of Norwalk virus protease
    • Jun 8. doi:10.1007/s12104-011-9316-3
    • Takahashi D., Kim Y., Chang K., Anbanandam A., Prakash O. Backbone and side-chain assignments of Norwalk virus protease. Biomol. NMR Assign. 2011, Jun 8. doi:10.1007/s12104-011-9316-3.
    • (2011) Biomol. NMR Assign.
    • Takahashi, D.1    Kim, Y.2    Chang, K.3    Anbanandam, A.4    Prakash, O.5
  • 49
    • 57349085743 scopus 로고    scopus 로고
    • Peptidomimetic therapeutic agents targeting the protease enzyme of the human immunodeficiency virus and hepatitis C virus
    • Tsantrizos Y.S. Peptidomimetic therapeutic agents targeting the protease enzyme of the human immunodeficiency virus and hepatitis C virus. Acc. Chem. Res. 2008, 41(10):1252-1263.
    • (2008) Acc. Chem. Res. , vol.41 , Issue.10 , pp. 1252-1263
    • Tsantrizos, Y.S.1
  • 50
    • 0038707388 scopus 로고    scopus 로고
    • Hepatitis C virus therapies: current treatments, targets and future perspectives
    • Walker M.P., Appleby T.C., Zhong W., Lau J.Y., Hong Z. Hepatitis C virus therapies: current treatments, targets and future perspectives. Antivir. Chem. Chemother. 2003, 14(1):1-21.
    • (2003) Antivir. Chem. Chemother. , vol.14 , Issue.1 , pp. 1-21
    • Walker, M.P.1    Appleby, T.C.2    Zhong, W.3    Lau, J.Y.4    Hong, Z.5
  • 51
    • 33646458515 scopus 로고    scopus 로고
    • X-ray crystallographic structure of the Norwalk virus protease at 1.5-A resolution
    • Zeitler C.E., Estes M.K., Venkataram Prasad B.V. X-ray crystallographic structure of the Norwalk virus protease at 1.5-A resolution. J. Virol. 2006, 80(10):5050-5058.
    • (2006) J. Virol. , vol.80 , Issue.10 , pp. 5050-5058
    • Zeitler, C.E.1    Estes, M.K.2    Venkataram Prasad, B.V.3
  • 52
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang J.H., Chung T.D., Oldenburg K.R. A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J. Biomol. Screen. 1999, 4(2):67-73.
    • (1999) J. Biomol. Screen. , vol.4 , Issue.2 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 53
    • 73949096807 scopus 로고    scopus 로고
    • Molecular epidemiology of genogroup II-genotype 4 noroviruses in the United States between 1994 and 2006
    • Zheng D.P., Widdowson M.A., Glass R.I., Vinje J. Molecular epidemiology of genogroup II-genotype 4 noroviruses in the United States between 1994 and 2006. J. Clin. Microbiol. 2010, 48(1):168-177.
    • (2010) J. Clin. Microbiol. , vol.48 , Issue.1 , pp. 168-177
    • Zheng, D.P.1    Widdowson, M.A.2    Glass, R.I.3    Vinje, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.