메뉴 건너뛰기




Volumn 52, Issue 2, 2013, Pages 432-444

Affinity labeling of hepatitis C virus replicase with a nucleotide analogue: Identification of binding site

Author keywords

[No Author keywords available]

Indexed keywords

ATP-BINDING SITE; CONCENTRATION-DEPENDENT; DOUBLE-STRANDED RNA; HEPATITIS C VIRUS; HPLC ANALYSIS; LC/MS/MS; NUCLEOTIDE ANALOGUES; PHOTO-CROSS-LINK; TRYPTIC PEPTIDES;

EID: 84872575070     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301098g     Document Type: Article
Times cited : (7)

References (53)
  • 2
    • 0026448768 scopus 로고
    • Diagnosis of hepatitis C virus (HCV) infection using an immunodominant chimeric polyprotein to capture circulating antibodies: Reevaluation of the role of HCV in liver disease
    • Chien, D. Y., Choo, Q. L., Tabrizi, A., Kuo, C., McFarland, J., Berger, K., Lee, C., Shuster, J. R., Nguyen, T., and Moyer, D. L. 1992, Diagnosis of hepatitis C virus (HCV) infection using an immunodominant chimeric polyprotein to capture circulating antibodies: reevaluation of the role of HCV in liver disease Proc. Natl. Acad. Sci. U.S.A. 89, 10011-10015
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10011-10015
    • Chien, D.Y.1    Choo, Q.L.2    Tabrizi, A.3    Kuo, C.4    McFarland, J.5    Berger, K.6    Lee, C.7    Shuster, J.R.8    Nguyen, T.9    Moyer, D.L.10
  • 3
    • 0035934568 scopus 로고    scopus 로고
    • Peginterferon alfa-2b plus ribavirin compared with interferon alfa-2b plus ribavirin for initial treatment of chronic hepatitis C: A randomised trial
    • Manns, M. P., McHutchison, J. G., Gordon, S. C., Rustgi, V. K., Shiffman, M., Reindollar, R., Goodman, Z. D., Koury, K., Ling, M., and Albrecht, J. K. (2001) Peginterferon alfa-2b plus ribavirin compared with interferon alfa-2b plus ribavirin for initial treatment of chronic hepatitis C: a randomised trial Lancet 358, 958-965
    • (2001) Lancet , vol.358 , pp. 958-965
    • Manns, M.P.1    McHutchison, J.G.2    Gordon, S.C.3    Rustgi, V.K.4    Shiffman, M.5    Reindollar, R.6    Goodman, Z.D.7    Koury, K.8    Ling, M.9    Albrecht, J.K.10
  • 4
    • 23944462641 scopus 로고    scopus 로고
    • Mechanism of action of interferon and ribavirin in treatment of hepatitis C
    • Feld, J. J. and Hoofnagle, J. H. (2005) Mechanism of action of interferon and ribavirin in treatment of hepatitis C Nature 436, 967-972
    • (2005) Nature , vol.436 , pp. 967-972
    • Feld, J.J.1    Hoofnagle, J.H.2
  • 5
    • 79960070664 scopus 로고    scopus 로고
    • Pegylated interferon and ribavirin treatment for hepatitis C virus infection
    • Palumbo, E. (2011) Pegylated interferon and ribavirin treatment for hepatitis C virus infection Ther. Adv. Chronic Dis. 2, 39-45
    • (2011) Ther. Adv. Chronic Dis. , vol.2 , pp. 39-45
    • Palumbo, E.1
  • 7
    • 77953463393 scopus 로고    scopus 로고
    • Nucleoside analog inhibitors of hepatitis C viral replication: Recent advances, challenges and trends
    • Furman, P. A., Lam, A. M., and Murakami, E. (2009) Nucleoside analog inhibitors of hepatitis C viral replication: recent advances, challenges and trends Fut. Med. Chem. 1, 1429-1452
    • (2009) Fut. Med. Chem. , vol.1 , pp. 1429-1452
    • Furman, P.A.1    Lam, A.M.2    Murakami, E.3
  • 13
    • 79953797938 scopus 로고    scopus 로고
    • An overview of HCV molecular biology, replication and immune responses
    • Ashfaq, U. A., Javed, T., Rehman, S., Nawaz, Z., and Riazuddin, S. (2011) An overview of HCV molecular biology, replication and immune responses Virol. J. 8, 161
    • (2011) Virol. J. , vol.8 , pp. 161
    • Ashfaq, U.A.1    Javed, T.2    Rehman, S.3    Nawaz, Z.4    Riazuddin, S.5
  • 14
    • 34547618419 scopus 로고    scopus 로고
    • Non-nucleoside inhibitors of the HCV NS5B polymerase: Progress in the discovery and development of novel agents for the treatment of HCV infections
    • Beaulieu, P. L. (2007) Non-nucleoside inhibitors of the HCV NS5B polymerase: progress in the discovery and development of novel agents for the treatment of HCV infections Curr. Opin. Investig. Drugs 8, 614-634
    • (2007) Curr. Opin. Investig. Drugs , vol.8 , pp. 614-634
    • Beaulieu, P.L.1
  • 16
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
    • Lesburg, C. A., Cable, M. B., Ferrari, E., Hong, Z., Mannarino, A. F., and Weber, P. C. (1999) Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site Nat. Struct. Biol. 6, 937-943
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 937-943
    • Lesburg, C.A.1    Cable, M.B.2    Ferrari, E.3    Hong, Z.4    Mannarino, A.F.5    Weber, P.C.6
  • 18
    • 0036120573 scopus 로고    scopus 로고
    • Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides
    • Bressanelli, S., Tomei, L., Rey, F. A., and De Francesco, R. (2002) Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides J. Virol. 76, 3482-3492
    • (2002) J. Virol. , vol.76 , pp. 3482-3492
    • Bressanelli, S.1    Tomei, L.2    Rey, F.A.3    De Francesco, R.4
  • 19
    • 0037470586 scopus 로고    scopus 로고
    • Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): Structural evidence for nucleotide import and de-novo initiation
    • O'Farrell, D., Trowbridge, R., Rowlands, D., and Jager, J. (2003) Substrate complexes of hepatitis C virus RNA polymerase (HC-J4): structural evidence for nucleotide import and de-novo initiation J. Mol. Biol. 326, 1025-1035
    • (2003) J. Mol. Biol. , vol.326 , pp. 1025-1035
    • O'Farrell, D.1    Trowbridge, R.2    Rowlands, D.3    Jager, J.4
  • 20
    • 23744436747 scopus 로고    scopus 로고
    • Crystal structures of the RNA-dependent RNA polymerase genotype 2a of hepatitis C virus reveal two conformations and suggest mechanisms of inhibition by non-nucleoside inhibitors
    • Biswal, B. K., Cherney, M. M., Wang, M., Chan, L., Yannopoulos, C. G., Bilimoria, D., Nicolas, O., Bedard, J., and James, M. N. (2005) Crystal structures of the RNA-dependent RNA polymerase genotype 2a of hepatitis C virus reveal two conformations and suggest mechanisms of inhibition by non-nucleoside inhibitors J. Biol. Chem. 280, 18202-18210
    • (2005) J. Biol. Chem. , vol.280 , pp. 18202-18210
    • Biswal, B.K.1    Cherney, M.M.2    Wang, M.3    Chan, L.4    Yannopoulos, C.G.5    Bilimoria, D.6    Nicolas, O.7    Bedard, J.8    James, M.N.9
  • 23
    • 31044446937 scopus 로고    scopus 로고
    • Recombinant viral RdRps can initiate RNA synthesis from circular templates
    • Ranjith-Kumar, C. T. and Kao, C. C. (2006) Recombinant viral RdRps can initiate RNA synthesis from circular templates RNA 12, 303-312
    • (2006) RNA , vol.12 , pp. 303-312
    • Ranjith-Kumar, C.T.1    Kao, C.C.2
  • 24
    • 0037127306 scopus 로고    scopus 로고
    • Oligomeric interaction of hepatitis C virus NS5B is critical for catalytic activity of RNA-dependent RNA polymerase
    • Qin, W., Luo, H., Nomura, T., Hayashi, N., Yamashita, T., and Murakami, S. (2002) Oligomeric interaction of hepatitis C virus NS5B is critical for catalytic activity of RNA-dependent RNA polymerase J. Biol. Chem. 277, 2132-2137
    • (2002) J. Biol. Chem. , vol.277 , pp. 2132-2137
    • Qin, W.1    Luo, H.2    Nomura, T.3    Hayashi, N.4    Yamashita, T.5    Murakami, S.6
  • 25
    • 0035120615 scopus 로고    scopus 로고
    • Mutational analysis of the structure and functions of hepatitis C virus RNA-dependent RNA polymerase
    • Qin, W., Yamashita, T., Shirota, Y., Lin, Y., Wei, W., and Murakami, S. (2001) Mutational analysis of the structure and functions of hepatitis C virus RNA-dependent RNA polymerase Hepatology 33, 728-737
    • (2001) Hepatology , vol.33 , pp. 728-737
    • Qin, W.1    Yamashita, T.2    Shirota, Y.3    Lin, Y.4    Wei, W.5    Murakami, S.6
  • 27
    • 0037064077 scopus 로고    scopus 로고
    • Modulation of hepatitis C virus RNA-dependent RNA polymerase activity by structure-based site-directed mutagenesis
    • Labonte, P., Axelrod, V., Agarwal, A., Aulabaugh, A., Amin, A., and Mak, P. (2002) Modulation of hepatitis C virus RNA-dependent RNA polymerase activity by structure-based site-directed mutagenesis J. Biol. Chem. 277, 38838-38846
    • (2002) J. Biol. Chem. , vol.277 , pp. 38838-38846
    • Labonte, P.1    Axelrod, V.2    Agarwal, A.3    Aulabaugh, A.4    Amin, A.5    Mak, P.6
  • 28
    • 77952710499 scopus 로고    scopus 로고
    • Regulation of de novo-initiated RNA synthesis in hepatitis C virus RNA-dependent RNA polymerase by intermolecular interactions
    • Chinnaswamy, S., Murali, A., Li, P., Fujisaki, K., and Kao, C. C. (2010) Regulation of de novo-initiated RNA synthesis in hepatitis C virus RNA-dependent RNA polymerase by intermolecular interactions J. Virol. 84, 5923-5935
    • (2010) J. Virol. , vol.84 , pp. 5923-5935
    • Chinnaswamy, S.1    Murali, A.2    Li, P.3    Fujisaki, K.4    Kao, C.C.5
  • 29
    • 77953452896 scopus 로고    scopus 로고
    • Conformations of the monomeric hepatitis C virus RNA dependent RNA polymerase
    • Chinnaswamy, S., Murali, A., and Cai, H. (2010) Conformations of the monomeric hepatitis C virus RNA dependent RNA polymerase Virus Adapt. Treat. 2, 21-39
    • (2010) Virus Adapt. Treat. , vol.2 , pp. 21-39
    • Chinnaswamy, S.1    Murali, A.2    Cai, H.3
  • 30
    • 33645238735 scopus 로고    scopus 로고
    • Biochemical and pre-steady-state kinetic characterization of the hepatitis C virus RNA polymerase (NS5BDelta21, HC-J4)
    • Cramer, J., Jaeger, J., and Restle, T. (2006) Biochemical and pre-steady-state kinetic characterization of the hepatitis C virus RNA polymerase (NS5BDelta21, HC-J4) Biochemistry 45, 3610-3619
    • (2006) Biochemistry , vol.45 , pp. 3610-3619
    • Cramer, J.1    Jaeger, J.2    Restle, T.3
  • 32
    • 0036631865 scopus 로고    scopus 로고
    • Selection of 3′-template bases and initiating nucleotides by hepatitis C virus NS5B RNA-dependent RNA polymerase
    • Shim, J. H., Larson, G., Wu, J. Z., and Hong, Z. (2002) Selection of 3′-template bases and initiating nucleotides by hepatitis C virus NS5B RNA-dependent RNA polymerase J. Virol. 76, 7030-7039
    • (2002) J. Virol. , vol.76 , pp. 7030-7039
    • Shim, J.H.1    Larson, G.2    Wu, J.Z.3    Hong, Z.4
  • 33
    • 14844283732 scopus 로고    scopus 로고
    • A relaxed discrimination of 2′-O-methyl-GTP relative to GTP between de novo and Elongative RNA synthesis by the hepatitis C RNA-dependent RNA polymerase NS5B
    • Dutartre, H., Boretto, J., Guillemot, J. C., and Canard, B. (2005) A relaxed discrimination of 2′-O-methyl-GTP relative to GTP between de novo and Elongative RNA synthesis by the hepatitis C RNA-dependent RNA polymerase NS5B J. Biol. Chem. 280, 6359-6368
    • (2005) J. Biol. Chem. , vol.280 , pp. 6359-6368
    • Dutartre, H.1    Boretto, J.2    Guillemot, J.C.3    Canard, B.4
  • 35
    • 0025249909 scopus 로고
    • Template primer-dependent binding of 5′-fluorosulfonyl- benzoyldeoxyadenosine by Escherichia coli DNA polymerase I. Identification of arginine 682 as the binding site and its implication in catalysis
    • Pandey, V. N., Kaushik, N. A., Pradhan, D. S., and Modak, M. J. (1990) Template primer-dependent binding of 5′-fluorosulfonyl- benzoyldeoxyadenosine by Escherichia coli DNA polymerase I. Identification of arginine 682 as the binding site and its implication in catalysis J. Biol. Chem. 265, 3679-3684
    • (1990) J. Biol. Chem. , vol.265 , pp. 3679-3684
    • Pandey, V.N.1    Kaushik, N.A.2    Pradhan, D.S.3    Modak, M.J.4
  • 36
    • 0023900101 scopus 로고
    • Affinity labeling of Escherichia coli DNA polymerase i by 5′-fluorosulfonylbenzoyladenosine. Identification of the domain essential for polymerization and Arg-682 as the site of reactivity
    • Pandey, V. N. and Modak, M. J. (1988) Affinity labeling of Escherichia coli DNA polymerase I by 5′-fluorosulfonylbenzoyladenosine. Identification of the domain essential for polymerization and Arg-682 as the site of reactivity J. Biol. Chem. 263, 6068-6073
    • (1988) J. Biol. Chem. , vol.263 , pp. 6068-6073
    • Pandey, V.N.1    Modak, M.J.2
  • 37
    • 0022358884 scopus 로고
    • Affinity labeling of a tyrosine residue in the ATP binding site of the recA protein from Escherichia coli with 5′- p - fluorosulfonylbenzoyladenosine
    • Knight, K. L. and McEntee, K. (1985) Affinity labeling of a tyrosine residue in the ATP binding site of the recA protein from Escherichia coli with 5′- p -fluorosulfonylbenzoyladenosine J. Biol. Chem. 260, 10177-10184
    • (1985) J. Biol. Chem. , vol.260 , pp. 10177-10184
    • Knight, K.L.1    McEntee, K.2
  • 38
    • 0027484027 scopus 로고
    • Affinity labelling of smooth-muscle myosin light-chain kinase with 5′-[p-(fluorosulphonyl)benzoyl]adenosine
    • Komatsu, H. and Ikebe, M. (1993) Affinity labelling of smooth-muscle myosin light-chain kinase with 5′-[p-(fluorosulphonyl)benzoyl]adenosine Biochem. J. 296 (Pt 1) 53-58
    • (1993) Biochem. J. , vol.296 , Issue.PART 1 , pp. 53-58
    • Komatsu, H.1    Ikebe, M.2
  • 39
    • 0030035137 scopus 로고    scopus 로고
    • ATP and SH3 binding sites in the protein kinase of the large subunit of herpes simplex virus type 2 of ribonucleotide reductase (ICP10)
    • Nelson, J. W., Zhu, J., Smith, C. C., Kulka, M., and Aurelian, L. (1996) ATP and SH3 binding sites in the protein kinase of the large subunit of herpes simplex virus type 2 of ribonucleotide reductase (ICP10) J. Biol. Chem. 271, 17021-17027
    • (1996) J. Biol. Chem. , vol.271 , pp. 17021-17027
    • Nelson, J.W.1    Zhu, J.2    Smith, C.C.3    Kulka, M.4    Aurelian, L.5
  • 40
    • 0032403851 scopus 로고    scopus 로고
    • Inactivation of isocitrate dehydrogenase kinase/phosphatase by 5′-[p-(fluorosulfonyl)benzoyl]adenosine is not due to the labeling of the invariant lysine residue found in the protein kinase family
    • Oudot, C., Jault, J. M., Jaquinod, M., Negre, D., Prost, J. F., Cozzone, A. J., and Cortay, J. C. (1998) Inactivation of isocitrate dehydrogenase kinase/phosphatase by 5′-[p-(fluorosulfonyl)benzoyl]adenosine is not due to the labeling of the invariant lysine residue found in the protein kinase family Eur. J. Biochem. 258, 579-585
    • (1998) Eur. J. Biochem. , vol.258 , pp. 579-585
    • Oudot, C.1    Jault, J.M.2    Jaquinod, M.3    Negre, D.4    Prost, J.F.5    Cozzone, A.J.6    Cortay, J.C.7
  • 41
    • 0035048969 scopus 로고    scopus 로고
    • The ATP-binding site of brain phosphatidylinositol 4-kinase PI4K230 as revealed by 5′-p-fluorosulfonylbenzoyladenosine
    • Vereb, G., Balla, A., Gergely, P., Wymann, M. P., Gulkan, H., Suer, S., and Heilmeyer, L. M., Jr. (2001) The ATP-binding site of brain phosphatidylinositol 4-kinase PI4K230 as revealed by 5′-p- fluorosulfonylbenzoyladenosine Int. J. Biochem. Cell Biol. 33, 249-259
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 249-259
    • Vereb, G.1    Balla, A.2    Gergely, P.3    Wymann, M.P.4    Gulkan, H.5    Suer, S.6    Heilmeyer Jr., L.M.7
  • 43
    • 58149279241 scopus 로고    scopus 로고
    • Mapping of the ATP-binding domain of human fructosamine 3-kinase-related protein by affinity labelling with 5′-[ p -(fluorosulfonyl)benzoyl] adenosine
    • Payne, L. S., Brown, P. M., Middleditch, M., Baker, E., Cooper, G. J., and Loomes, K. M. (2008) Mapping of the ATP-binding domain of human fructosamine 3-kinase-related protein by affinity labelling with 5′-[ p -(fluorosulfonyl)benzoyl]adenosine Biochem. J. 416, 281-288
    • (2008) Biochem. J. , vol.416 , pp. 281-288
    • Payne, L.S.1    Brown, P.M.2    Middleditch, M.3    Baker, E.4    Cooper, G.J.5    Loomes, K.M.6
  • 44
    • 0017344612 scopus 로고
    • Adenosine derivatives for dehydrogenases and kinases
    • Colman, R. F., Pal, P. K., and Wyatt, J. L. (1977) Adenosine derivatives for dehydrogenases and kinases Methods Enzymol. 46, 240-249
    • (1977) Methods Enzymol. , vol.46 , pp. 240-249
    • Colman, R.F.1    Pal, P.K.2    Wyatt, J.L.3
  • 46
    • 0027286502 scopus 로고
    • MASCOT: Multiple alignment system for protein sequences based on three-way dynamic programming
    • Hirosawa, M., Hoshida, M., Ishikawa, M., and Toya, T. (1993) MASCOT: multiple alignment system for protein sequences based on three-way dynamic programming Comput. Appl. Biosci. 9, 161-167
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 161-167
    • Hirosawa, M.1    Hoshida, M.2    Ishikawa, M.3    Toya, T.4
  • 47
    • 0346101769 scopus 로고    scopus 로고
    • Initial binding of the broad spectrum antiviral nucleoside ribavirin to the hepatitis C virus RNA polymerase
    • Bougie, I. and Bisaillon, M. (2003) Initial binding of the broad spectrum antiviral nucleoside ribavirin to the hepatitis C virus RNA polymerase J. Biol. Chem. 278, 52471-52478
    • (2003) J. Biol. Chem. , vol.278 , pp. 52471-52478
    • Bougie, I.1    Bisaillon, M.2
  • 48
    • 0037423270 scopus 로고    scopus 로고
    • Characterization of the metal ion binding properties of the hepatitis C virus RNA polymerase
    • Bougie, I., Charpentier, S., and Bisaillon, M. (2003) Characterization of the metal ion binding properties of the hepatitis C virus RNA polymerase J. Biol. Chem. 278, 3868-3875
    • (2003) J. Biol. Chem. , vol.278 , pp. 3868-3875
    • Bougie, I.1    Charpentier, S.2    Bisaillon, M.3
  • 49
    • 0032530621 scopus 로고    scopus 로고
    • Biochemical and kinetic analyses of NS5B RNA-dependent RNA polymerase of the hepatitis C virus
    • Lohmann, V., Roos, A., Korner, F., Koch, J. O., and Bartenschlager, R. (1998) Biochemical and kinetic analyses of NS5B RNA-dependent RNA polymerase of the hepatitis C virus Virology 249, 108-118
    • (1998) Virology , vol.249 , pp. 108-118
    • Lohmann, V.1    Roos, A.2    Korner, F.3    Koch, J.O.4    Bartenschlager, R.5
  • 51
    • 0015959804 scopus 로고
    • The involvement of serine and carboxyl groups in the activity of bovine pancreatic deoxyribonuclease A
    • Poulos, T. L. and Price, P. A. (1974) The involvement of serine and carboxyl groups in the activity of bovine pancreatic deoxyribonuclease A J. Biol. Chem. 249, 1453-1457
    • (1974) J. Biol. Chem. , vol.249 , pp. 1453-1457
    • Poulos, T.L.1    Price, P.A.2
  • 52
    • 0019888671 scopus 로고
    • Lysine and tyrosine in the NADH inhibitory site of bovine liver glutamate dehydrogenase
    • Saradambal, K. V., Bednar, R. A., and Colman, R. F. (1981) Lysine and tyrosine in the NADH inhibitory site of bovine liver glutamate dehydrogenase J. Biol. Chem. 256, 11866-11872
    • (1981) J. Biol. Chem. , vol.256 , pp. 11866-11872
    • Saradambal, K.V.1    Bednar, R.A.2    Colman, R.F.3
  • 53
    • 0035919073 scopus 로고    scopus 로고
    • A novel mechanism to ensure terminal initiation by hepatitis C virus NS5B polymerase
    • Hong, Z., Cameron, C. E., Walker, M. P., Castro, C., Yao, N., Lau, J. Y., and Zhong, W. (2001) A novel mechanism to ensure terminal initiation by hepatitis C virus NS5B polymerase Virology 285, 6-11
    • (2001) Virology , vol.285 , pp. 6-11
    • Hong, Z.1    Cameron, C.E.2    Walker, M.P.3    Castro, C.4    Yao, N.5    Lau, J.Y.6    Zhong, W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.