메뉴 건너뛰기




Volumn 385, Issue 2, 2005, Pages 363-370

Hepatitis a virus proteinase 3C binding to viral RNA: Correlation with substrate binding and enzyme dimerization

Author keywords

Dimerization; Hepatitis A virus; NMR; Proteinase 3C; RNA binding; Surface plasmon resonance (SPR)

Indexed keywords

DATA ACQUISITION; DIMERS; GENES; PROTEINS; RNA; SURFACE PLASMON RESONANCE; VIRUSES;

EID: 12844264099     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041153     Document Type: Article
Times cited : (26)

References (35)
  • 1
    • 0344012008 scopus 로고    scopus 로고
    • Phase II, randomized, double-blind, placebo-controlled studies of ruprintrivir nasal spray 2-percent suspension for prevention and treatment of experimentally induced rhinovirus colds in healthy volunteers
    • Hayden, F. G., Turner, R. B., Gwaltney, J. M., Chi-Burris, K., Gersten, M., Hsyu, P., Patick, A. K., Smith, 3rd, G. J. and Zalman, L. S. (2003) Phase II, randomized, double-blind, placebo-controlled studies of ruprintrivir nasal spray 2-percent suspension for prevention and treatment of experimentally induced rhinovirus colds in healthy volunteers. Antimicrob. Agents Chemother. 47, 3907-3916
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 3907-3916
    • Hayden, F.G.1    Turner, R.B.2    Gwaltney, J.M.3    Chi-Burris, K.4    Gersten, M.5    Hsyu, P.6    Patick, A.K.7    Smith III, G.J.8    Zalman, L.S.9
  • 2
    • 0031736007 scopus 로고    scopus 로고
    • Protease inhibitors as antiviral agents
    • Patick, A. K. and Potts, K. E. (1998) Protease inhibitors as antiviral agents. Clin. Microbiol. Rev. 11, 614-627
    • (1998) Clin. Microbiol. Rev. , vol.11 , pp. 614-627
    • Patick, A.K.1    Potts, K.E.2
  • 3
    • 0031685015 scopus 로고    scopus 로고
    • Processing of proteinase precursors and their effect on hepatitis a virus particle formation
    • Probst, C., Jecht, M. and Gauss-Muller, V. (1998) Processing of proteinase precursors and their effect on hepatitis A virus particle formation. J. Virol. 72, 8013-8020
    • (1998) J. Virol. , vol.72 , pp. 8013-8020
    • Probst, C.1    Jecht, M.2    Gauss-Muller, V.3
  • 4
    • 0344240134 scopus 로고    scopus 로고
    • Improving proteolytic cleavage at the 3A/3B site of the hepatitis a virus polyprotein impairs processing and particle formation, and the impairment can be complemented in trans by 3AB and 3ABC
    • Kusov, Y. and Gauss-Muller, V. (1999) Improving proteolytic cleavage at the 3A/3B site of the hepatitis A virus polyprotein impairs processing and particle formation, and the impairment can be complemented in trans by 3AB and 3ABC. J. Virol. 73, 9867-9878
    • (1999) J. Virol. , vol.73 , pp. 9867-9878
    • Kusov, Y.1    Gauss-Muller, V.2
  • 5
    • 0031567786 scopus 로고    scopus 로고
    • Refined X-ray crystallographic structure of the poliovirus 3C gene product
    • Mosimann, S. C., Cherney, M. M., Sia, S., Plotch, S. and James, M. N. (1997) Refined X-ray crystallographic structure of the poliovirus 3C gene product. J. Mol. Biol. 273, 1032-1047
    • (1997) J. Mol. Biol. , vol.273 , pp. 1032-1047
    • Mosimann, S.C.1    Cherney, M.M.2    Sia, S.3    Plotch, S.4    James, M.N.5
  • 6
    • 0031047974 scopus 로고    scopus 로고
    • The refined crystal structure of the 3C gene product from hepatitis a virus: Specific proteinase activity and RNA recognition
    • Bergmann, E. M., Mosimann, S. C., Chernaia, M. M., Malcolm, B. A. and James, M. N. (1997) The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition. J. Virol. 71, 2436-2448
    • (1997) J. Virol. , vol.71 , pp. 2436-2448
    • Bergmann, E.M.1    Mosimann, S.C.2    Chernaia, M.M.3    Malcolm, B.A.4    James, M.N.5
  • 7
    • 0033527893 scopus 로고    scopus 로고
    • Crystal structure of an inhibitor complex of the 3C proteinase from hepatitis a virus (HAV) and implications for the polyprotein processing in HAV
    • Bergmann, E. M., Cherney, M. M., Mckendrick, J., Frormann, S., Luo, C., Malcolm, B. A., Vederas, J. C. and James, M. N. (1999) Crystal structure of an inhibitor complex of the 3C proteinase from hepatitis A virus (HAV) and implications for the polyprotein processing in HAV. Virology 265, 153-163
    • (1999) Virology , vol.265 , pp. 153-163
    • Bergmann, E.M.1    Cherney, M.M.2    Mckendrick, J.3    Frormann, S.4    Luo, C.5    Malcolm, B.A.6    Vederas, J.C.7    James, M.N.8
  • 8
    • 0028328469 scopus 로고
    • Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases
    • Allaire, M., Chernaia, M. M., Malcolm, B. A. and James, M. N. (1994) Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature (London) 369, 72-76
    • (1994) Nature (London) , vol.369 , pp. 72-76
    • Allaire, M.1    Chernaia, M.M.2    Malcolm, B.A.3    James, M.N.4
  • 9
    • 0029086385 scopus 로고
    • The picornaviral 3C proteinases: Cysteine nucleophiles in serine proteinase folds
    • Malcolm, B. A. (1995) The picornaviral 3C proteinases: cysteine nucleophiles in serine proteinase folds. Protein Sci. 4, 1439-1445
    • (1995) Protein Sci. , vol.4 , pp. 1439-1445
    • Malcolm, B.A.1
  • 10
    • 0028235532 scopus 로고
    • Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA binding site, and means for cleaving precursor polyprotein
    • 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. et al. (1994) Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA binding site, and means for cleaving precursor polyprotein. Cell 77, 761-771
    • (1994) Cell , vol.77 , pp. 761-771
    • Matthews, D.A.1    Smith, W.W.2    Ferre, R.A.3    Condon, B.4    Budahazi, G.5    Sisson, W.6    Villafranca, J.E.7    Janson, C.A.8    McElroy, H.E.9    Gribskov, C.L.10
  • 11
    • 0030887314 scopus 로고    scopus 로고
    • Virus-encoded proteinases of the picornavirus super-group
    • Ryan, M. D. and Flint, M. (1997) Virus-encoded proteinases of the picornavirus super-group. J. Gen. Virol. 78, 699-723
    • (1997) J. Gen. Virol. , vol.78 , pp. 699-723
    • Ryan, M.D.1    Flint, M.2
  • 12
    • 0037903343 scopus 로고    scopus 로고
    • Signals in hepatitis a virus P3 region proteins recognized by the ubiquitin-mediated proteolytic system
    • Losick, V. P., Schlax, P. E., Emmons, R. A. and Lawson, T. G. (2003) Signals in hepatitis A virus P3 region proteins recognized by the ubiquitin-mediated proteolytic system. Virology 309, 306-319
    • (2003) Virology , vol.309 , pp. 306-319
    • Losick, V.P.1    Schlax, P.E.2    Emmons, R.A.3    Lawson, T.G.4
  • 13
    • 0027170180 scopus 로고
    • Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA
    • Andino, R., Rieckhof, G. E., Achacoso, P. L. and Baltimore, D. (1993) Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA. EMBO J. 12, 3587-3598
    • (1993) EMBO J. , vol.12 , pp. 3587-3598
    • Andino, R.1    Rieckhof, G.E.2    Achacoso, P.L.3    Baltimore, D.4
  • 14
    • 0025049209 scopus 로고
    • A functional ribonucleoprotein complex forms around the 5′ end of poliovirus RNA
    • Andino, R., Rieckhof, G. E. and Baltimore, D. (1990) A functional ribonucleoprotein complex forms around the 5′ end of poliovirus RNA. Cell 63, 369-380
    • (1990) Cell , vol.63 , pp. 369-380
    • Andino, R.1    Rieckhof, G.E.2    Baltimore, D.3
  • 15
    • 0032146721 scopus 로고    scopus 로고
    • Switch from translation to RNA replication in a positive-stranded RNA virus
    • Gamarnik, A. V. and Andino, R. (1998) Switch from translation to RNA replication in a positive-stranded RNA virus. Genes Dev. 12, 2293-2304
    • (1998) Genes Dev. , vol.12 , pp. 2293-2304
    • Gamarnik, A.V.1    Andino, R.2
  • 16
    • 0030899223 scopus 로고    scopus 로고
    • In vitro RNA binding of the hepatitis a virus proteinase 3C (HAV 3Cpro) to secondary structure elements within the 5′ terminus of the HAV genome
    • Kusov, Y. Y. and Gauss-Muller, V. (1997) In vitro RNA binding of the hepatitis A virus proteinase 3C (HAV 3Cpro) to secondary structure elements within the 5′ terminus of the HAV genome. RNA 3, 291-302
    • (1997) RNA , vol.3 , pp. 291-302
    • Kusov, Y.Y.1    Gauss-Muller, V.2
  • 17
    • 0029061499 scopus 로고
    • Sequence and structural determinants of the interaction between the 5′-noncoding region of picornavirus RNA and rhinovirus protease 3C
    • Walker, P. A., Leong, L. E. and Porter, A. G. (1995) Sequence and structural determinants of the interaction between the 5′-noncoding region of picornavirus RNA and rhinovirus protease 3C. J. Biol. Chem. 270, 14510-14516
    • (1995) J. Biol. Chem. , vol.270 , pp. 14510-14516
    • Walker, P.A.1    Leong, L.E.2    Porter, A.G.3
  • 18
    • 0028851295 scopus 로고
    • Cleavage specificity of purified recombinant hepatitis a virus 3C proteinase on natural substrates
    • Schultheiss, T., Sommergruber, W., Kusov, Y. and Gauss-Muller, V. (1995) Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates. J. Virol. 69, 1727-1733
    • (1995) J. Virol. , vol.69 , pp. 1727-1733
    • Schultheiss, T.1    Sommergruber, W.2    Kusov, Y.3    Gauss-Muller, V.4
  • 19
    • 0026646534 scopus 로고
    • Hepatitis a virus 3C proteinase substrate specificity
    • Jewell, D. A., Swietnicki, W., Dunn, B. M. and Malcolm, B. A. (1992) Hepatitis A virus 3C proteinase substrate specificity. Biochemistry 31, 7862-7869
    • (1992) Biochemistry , vol.31 , pp. 7862-7869
    • Jewell, D.A.1    Swietnicki, W.2    Dunn, B.M.3    Malcolm, B.A.4
  • 20
    • 0031259636 scopus 로고    scopus 로고
    • Interaction of hepatitis a virus (HAV) precursor proteins 3AB and 3ABC with the 5′ and 3′ termini of the HAV RNA
    • Kusov, Y. Y., Morace, G., Probst, C. and Gauss-Muller, V. (1997) Interaction of hepatitis A virus (HAV) precursor proteins 3AB and 3ABC with the 5′ and 3′ termini of the HAV RNA. Virus Res. 51, 151-157
    • (1997) Virus Res. , vol.51 , pp. 151-157
    • Kusov, Y.Y.1    Morace, G.2    Probst, C.3    Gauss-Muller, V.4
  • 21
    • 0033955735 scopus 로고    scopus 로고
    • Advances in surface plasmon resonance biosensor analysis
    • Rich, R. L. and Myszka, D. G. (2000) Advances in surface plasmon resonance biosensor analysis. Curr. Opin. Biotechnol. 11, 54-61
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 54-61
    • Rich, R.L.1    Myszka, D.G.2
  • 22
    • 0032321401 scopus 로고    scopus 로고
    • Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors
    • Morton, T. A. and Myszka, D. G. (1998) Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Methods Enzymol. 295, 268-294
    • (1998) Methods Enzymol. , vol.295 , pp. 268-294
    • Morton, T.A.1    Myszka, D.G.2
  • 24
    • 0027138665 scopus 로고
    • Hepatitis a virus 3C proteinase: Some properties, crystallization and preliminary crystallographic characterization
    • Chernaia, M. M., Malcolm, B. A., Allaire, M. and James, M. N. (1993) Hepatitis A virus 3C proteinase: some properties, crystallization and preliminary crystallographic characterization. J. Mol. Biol. 234, 890-893
    • (1993) J. Mol. Biol. , vol.234 , pp. 890-893
    • Chernaia, M.M.1    Malcolm, B.A.2    Allaire, M.3    James, M.N.4
  • 26
    • 0018370106 scopus 로고
    • Modification of the 3′ terminus of tRNA by periodate oxidation and subsequent reaction with hydrazides
    • Hansske, F. and Cramer, F. (1979) Modification of the 3′ terminus of tRNA by periodate oxidation and subsequent reaction with hydrazides. Methods Enzymol. 59, 172-181
    • (1979) Methods Enzymol. , vol.59 , pp. 172-181
    • Hansske, F.1    Cramer, F.2
  • 27
    • 0028929659 scopus 로고
    • Identification of bases in 16S rRNA essential for tRNA binding at the 30S ribosomal P site
    • von Ahsen, U. and Noller, H. F. (1995) Identification of bases in 16S rRNA essential for tRNA binding at the 30S ribosomal P site. Science 267, 234-237
    • (1995) Science , vol.267 , pp. 234-237
    • Von Ahsen, U.1    Noller, H.F.2
  • 28
    • 0033580814 scopus 로고    scopus 로고
    • Real-time kinetics of HIV-1 Rev-Rev response element interactions. Definition of minimal binding sites on RNA and protein and stoichiometric analysis
    • Van Ryk, D. I. and Venkatesan, S. (1999) Real-time kinetics of HIV-1 Rev-Rev response element interactions. Definition of minimal binding sites on RNA and protein and stoichiometric analysis. J. Biol. Chem. 274, 17452-17463
    • (1999) J. Biol. Chem. , vol.274 , pp. 17452-17463
    • Van Ryk, D.I.1    Venkatesan, S.2
  • 29
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • Mayer, M. and Meyer, B. (1999) Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew. Chem. 38, 1784-1788
    • (1999) Angew. Chem. , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 30
    • 0037463033 scopus 로고    scopus 로고
    • NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors
    • Meyer, B. and Peters, T. (2003) NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors. Angew. Chemie Int. Ed. 42, 864-890
    • (2003) Angew. Chemie Int. Ed. , vol.42 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 31
    • 0031572825 scopus 로고    scopus 로고
    • A continuous colorimetric assay for rhinovirus-14 3C protease using peptide p-nitroanilides as substrates
    • Wang, Q. M., Johnson, R. B., Cox, G. A., Villarreal, E. C. and Loncharich, R. J. (1997) A continuous colorimetric assay for rhinovirus-14 3C protease using peptide p-nitroanilides as substrates. Anal. Biochem. 252, 238-245
    • (1997) Anal. Biochem. , vol.252 , pp. 238-245
    • Wang, Q.M.1    Johnson, R.B.2    Cox, G.A.3    Villarreal, E.C.4    Loncharich, R.J.5
  • 32
    • 0032144281 scopus 로고    scopus 로고
    • Model and simulation of multivalent binding to fixed ligands
    • Müller, K. M., Arndt, K. M. and Plückthun, A. (1998) Model and simulation of multivalent binding to fixed ligands. Anal. Biochem. 261, 149-158
    • (1998) Anal. Biochem. , vol.261 , pp. 149-158
    • Müller, K.M.1    Arndt, K.M.2    Plückthun, A.3
  • 33
    • 0034712884 scopus 로고    scopus 로고
    • Selective binding of hepatitis C virus core protein to synthetic oligonucleotides corresponding to the 5′ untranslated region of the viral genome
    • Tanaka, Y., Shimoike, T., Ishii, K., Suzuki, R., Suzuki, T., Ushijima, H., Matsuura, Y. and Miyamura, T. (2000) Selective binding of hepatitis C virus core protein to synthetic oligonucleotides corresponding to the 5′ untranslated region of the viral genome. Virology 270, 229-236
    • (2000) Virology , vol.270 , pp. 229-236
    • Tanaka, Y.1    Shimoike, T.2    Ishii, K.3    Suzuki, R.4    Suzuki, T.5    Ushijima, H.6    Matsuura, Y.7    Miyamura, T.8
  • 34
    • 0031947053 scopus 로고    scopus 로고
    • Complete protein linkage map of poliovirus P3 proteins: Interaction of polymerase 3Dpol with VPg and with genetic variants of 3AB
    • Xiang, W., Cuconati, A., Hope, D., Kirkegaard, K. and Wimmer, E. (1998) Complete protein linkage map of poliovirus P3 proteins: interaction of polymerase 3Dpol with VPg and with genetic variants of 3AB. J. Virol. 72, 6732-6741
    • (1998) J. Virol. , vol.72 , pp. 6732-6741
    • Xiang, W.1    Cuconati, A.2    Hope, D.3    Kirkegaard, K.4    Wimmer, E.5
  • 35
    • 0034366790 scopus 로고    scopus 로고
    • Low affinity carbohydrate lectin interactions examined with surface plasmon resonance
    • Weimar, T., Haase, B. and Köhli, T. (2000) Low affinity carbohydrate lectin interactions examined with surface plasmon resonance. J. Carbohydr. Chem. 19, 1083-1089
    • (2000) J. Carbohydr. Chem. , vol.19 , pp. 1083-1089
    • Weimar, T.1    Haase, B.2    Köhli, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.