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Volumn 73, Issue 12, 1999, Pages 9867-9878

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

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; HEPATITIS A; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROCESSING; VIRUS PARTICLE; VIRUS REPLICATION;

EID: 0344240134     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.12.9867-9878.1999     Document Type: Article
Times cited : (31)

References (44)
  • 1
    • 0025036493 scopus 로고
    • Morphogenesis of hepatitis A virus: Isolation and characterisation of subviral particles
    • Anderson, D. A., and B. Ross. 1990. Morphogenesis of hepatitis A virus: isolation and characterisation of subviral particles. J. Virol. 64:5284-5289.
    • (1990) J. Virol. , vol.64 , pp. 5284-5289
    • Anderson, D.A.1    Ross, B.2
  • 3
    • 0030949292 scopus 로고    scopus 로고
    • Site-directed mutagenesis of hepatitis A virus protein 3A: Effects on membrane interaction
    • Beneduce, F., A. Ciervo, and G. Morace. 1997. Site-directed mutagenesis of hepatitis A virus protein 3A: effects on membrane interaction. Biochim. Biophys. Acta 1326:157-165.
    • (1997) Biochim. Biophys. Acta , vol.1326 , pp. 157-165
    • Beneduce, F.1    Ciervo, A.2    Morace, G.3
  • 4
    • 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., S. C. Mosimann, M. M. Chernaia, B. A. Malcolm, and M. N. G. James. 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.G.5
  • 5
    • 0027405544 scopus 로고
    • A cellular cofactor facilitates efficient 3CD cleavage of the poliovirus P1 precursor
    • Blair, W. S., X. Li, and B. L. Semler. 1993. A cellular cofactor facilitates efficient 3CD cleavage of the poliovirus P1 precursor. J. Virol. 67:2336-2343.
    • (1993) J. Virol. , vol.67 , pp. 2336-2343
    • Blair, W.S.1    Li, X.2    Semler, B.L.3
  • 6
    • 0028797162 scopus 로고
    • Mutagenesis of the yellow fever virus NS2B/3 cleavage site: Determinants of cleavage site specificity and effects on polyprotein processing and viral replication
    • Chambers, T. J., A. Nestrorowicz, and C. Rice. 1995. Mutagenesis of the yellow fever virus NS2B/3 cleavage site: determinants of cleavage site specificity and effects on polyprotein processing and viral replication. J. Virol. 69:1600-1605.
    • (1995) J. Virol. , vol.69 , pp. 1600-1605
    • Chambers, T.J.1    Nestrorowicz, A.2    Rice, C.3
  • 7
    • 0032504596 scopus 로고    scopus 로고
    • Polypeptide 3AB of hepatitis A virus is a transmembrane protein
    • Ciervo, A., F. Beneduce, and G. Morace. 1998. Polypeptide 3AB of hepatitis A virus is a transmembrane protein. Biochem. Biophys. Res. Commun. 249:266-274.
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 266-274
    • Ciervo, A.1    Beneduce, F.2    Morace, G.3
  • 8
    • 0030273679 scopus 로고    scopus 로고
    • Effects of P2 cleavage site mutations on poliovirus polyprotein processing
    • Cohen, L., K. M. Kean, M. Girard, and S. van der Werf. 1996. Effects of P2 cleavage site mutations on poliovirus polyprotein processing. Virology 224: 34-42.
    • (1996) Virology , vol.224 , pp. 34-42
    • Cohen, L.1    Kean, K.M.2    Girard, M.3    Van Der Werf, S.4
  • 9
    • 0000233999 scopus 로고
    • Eukaryotic expression system based on a recombinant vaccinia virus that synthesize bacteriophage T7 RNA polymerase
    • Fuerst, T. R., E. G. Niles, F. W. Studier, and B. Moss. 1986. Eukaryotic expression system based on a recombinant vaccinia virus that synthesize bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA 83:8122-8126.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 10
    • 0027183347 scopus 로고
    • Functional and genetic plasticity of the poliovirus genome quasi-infectious RNAs modified in the 5′-untranslated region yield a variety of pseudorevertants
    • Gmyl, A. P., E. V. Pilipenko, S. V. Maslova, G. A. Belov, and V. I. Agol. 1993. Functional and genetic plasticity of the poliovirus genome quasi-infectious RNAs modified in the 5′-untranslated region yield a variety of pseudorevertants. J. Virol. 67:6309-6316.
    • (1993) J. Virol. , vol.67 , pp. 6309-6316
    • Gmyl, A.P.1    Pilipenko, E.V.2    Maslova, S.V.3    Belov, G.A.4    Agol, V.I.5
  • 11
    • 0027968278 scopus 로고
    • Mutational events in consecutive passages of hepatitis A virus strain GBM during cell culture adaptation
    • Graf, J., C. Kasang, A. Normann, M. Pfisterer-Hunt, S. M. Feinstone, and B. Flehmig. 1994. Mutational events in consecutive passages of hepatitis A virus strain GBM during cell culture adaptation. Virology 204:60-68.
    • (1994) Virology , vol.204 , pp. 60-68
    • Graf, J.1    Kasang, C.2    Normann, A.3    Pfisterer-Hunt, M.4    Feinstone, S.M.5    Flehmig, B.6
  • 12
    • 0029841215 scopus 로고    scopus 로고
    • Cleavage site mutations in the encephaliomyocarditis virus P3 region lethally abrogate the normal processing cascade
    • Hall, D. J., and A. C. Palmenberg. 1996. Cleavage site mutations in the encephaliomyocarditis virus P3 region lethally abrogate the normal processing cascade. J. Virol. 70:5954-5961.
    • (1996) J. Virol. , vol.70 , pp. 5954-5961
    • Hall, D.J.1    Palmenberg, A.C.2
  • 13
    • 0032488261 scopus 로고    scopus 로고
    • Membrane permeability induced by hepatitis A virus (HAV) proteins 2B and 2BC and proteolytic processing of HAV 2BC
    • Jecht, M., C. Probst, and V. Gauss-Müller. 1998. Membrane permeability induced by hepatitis A virus (HAV) proteins 2B and 2BC and proteolytic processing of HAV 2BC. Virology 252:218-227.
    • (1998) Virology , vol.252 , pp. 218-227
    • Jecht, M.1    Probst, C.2    Gauss-Müller, V.3
  • 14
    • 0026646534 scopus 로고
    • Hepatitis A virus 3C proteinase substrate specificity
    • Jewell, D. A., W. Swietnicki, B. M. Dunn, and B. A. Malcolm. 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
  • 15
    • 0025873585 scopus 로고
    • Proteolytic activity of hepatitis A virus 3C protein
    • Jia, X. Y., E. Ehrenfeld, and D. F. Summers. 1991. Proteolytic activity of hepatitis A virus 3C protein. J. Virol. 65:2595-2600.
    • (1991) J. Virol. , vol.65 , pp. 2595-2600
    • Jia, X.Y.1    Ehrenfeld, E.2    Summers, D.F.3
  • 16
  • 17
    • 0026640791 scopus 로고
    • Intermolecular cleavage of hepatitis A virus (HAV) precursor protein P1-P2 by recombinant HAV proteinase 3C
    • Kusov, Y. Y., W. Sommergruber, M. Schreiber, and V. Gauss-Müller. 1992. Intermolecular cleavage of hepatitis A virus (HAV) precursor protein P1-P2 by recombinant HAV proteinase 3C. J. Virol. 66:6794-6796.
    • (1992) J. Virol. , vol.66 , pp. 6794-6796
    • Kusov, Y.Y.1    Sommergruber, W.2    Schreiber, M.3    Gauss-Müller, V.4
  • 18
    • 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., G. Morace, C. Probst, and V. Gauss-Müller. 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-Müller, V.4
  • 20
    • 0027475009 scopus 로고
    • Roles of nonstructural polyproteins and cleavage products in regulating Sindbis virus RNA replication and transcription
    • Lemm, J. A., and C. Rice. 1993. Roles of nonstructural polyproteins and cleavage products in regulating Sindbis virus RNA replication and transcription. J. Virol. 67:1916-1926.
    • (1993) J. Virol. , vol.67 , pp. 1916-1926
    • Lemm, J.A.1    Rice, C.2
  • 21
    • 0028805715 scopus 로고
    • Identification and site-directed mutagenesis of the primary (2A/2B) cleavage site of the hepatitis A virus polyprotein: Functional impact on the infectivity of HAV RNA transcripts
    • Martin, A., N. Escriou, S. F. Chao, M. Girard, S. M. Lemon, and C. Wychowski. 1995. Identification and site-directed mutagenesis of the primary (2A/2B) cleavage site of the hepatitis A virus polyprotein: functional impact on the infectivity of HAV RNA transcripts. Virology 213:213-222.
    • (1995) Virology , vol.213 , pp. 213-222
    • Martin, A.1    Escriou, N.2    Chao, S.F.3    Girard, M.4    Lemon, S.M.5    Wychowski, C.6
  • 23
    • 0027158749 scopus 로고
    • Mutations in the 3A genomic region of two cytopathic strains of hepatitis A virus isolated in Italy
    • Morace, G., G. Pisani, F. Beneduce, M. Divizia, and A. Pana. 1993. Mutations in the 3A genomic region of two cytopathic strains of hepatitis A virus isolated in Italy. Virus Res. 28:187-194.
    • (1993) Virus Res. , vol.28 , pp. 187-194
    • Morace, G.1    Pisani, G.2    Beneduce, F.3    Divizia, M.4    Pana, A.5
  • 24
    • 0032505602 scopus 로고    scopus 로고
    • Internal ribosomal entry site scanning of the poliovirus polyprotein: Implications for proteolytic processing
    • Paul, A. V., J. Mugavero, A. Molla, and E. Wimmer. 1998. Internal ribosomal entry site scanning of the poliovirus polyprotein: implications for proteolytic processing. Virology 250:241-253.
    • (1998) Virology , vol.250 , pp. 241-253
    • Paul, A.V.1    Mugavero, J.2    Molla, A.3    Wimmer, E.4
  • 25
    • 0026597150 scopus 로고
    • Antigenic structure of human hepatitis A virus defined by analysis of escape mutants selected against murine monoclonal antibodies
    • Ping, L.-H., and S. M. Lemon. 1992. Antigenic structure of human hepatitis A virus defined by analysis of escape mutants selected against murine monoclonal antibodies. J. Virol. 66:2208-2216.
    • (1992) J. Virol. , vol.66 , pp. 2208-2216
    • Ping, L.-H.1    Lemon, S.M.2
  • 26
    • 0029036173 scopus 로고
    • Recombinant expression of hepatitis A virus protein 3A: Interaction with membranes
    • Pisani, G., F. Beneduce, V. Gauss-Müller, and G. Morace. 1995. Recombinant expression of hepatitis A virus protein 3A: interaction with membranes. Biochem. Biophys. Res. Commun. 211:627-638.
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 627-638
    • Pisani, G.1    Beneduce, F.2    Gauss-Müller, V.3    Morace, G.4
  • 28
    • 0030969340 scopus 로고    scopus 로고
    • Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus strains: In vivo evidence for cleavage at amino acid position 273/274 of VP1
    • Probst, C., M. Jecht, and V. Gauss-Müller. 1997. Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus strains: in vivo evidence for cleavage at amino acid position 273/274 of VP1. J. Virol. 71:3288-3292.
    • (1997) J. Virol. , vol.71 , pp. 3288-3292
    • Probst, C.1    Jecht, M.2    Gauss-Müller, V.3
  • 29
    • 0031685015 scopus 로고    scopus 로고
    • Processing of proteinase precursors and their effect on hepatitis A virus particle formation
    • Probst, C., M. Jecht, and V. Gauss-Müller. 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-Müller, V.3
  • 30
    • 0033582489 scopus 로고    scopus 로고
    • Intrinsic signals for the assembly of hepatitis A virus particles - Role of structural proteins VP4 and 2A
    • Probst, C., M. Jecht, and V. Gauss-Müller. 1999. Intrinsic signals for the assembly of hepatitis A virus particles - role of structural proteins VP4 and 2A. J. Biol. Chem. 274:4527-4531.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4527-4531
    • Probst, C.1    Jecht, M.2    Gauss-Müller, V.3
  • 31
    • 0028364693 scopus 로고
    • Proteinase 3C of hepatitis A virus (HAV) cleaves the HAV polyprotein P2-P3 at all sites including VP1/2A and 2A/2B
    • Schultheiß, T., Y. Y. Kusov, and V. Gauss-Müller. 1994. Proteinase 3C of hepatitis A virus (HAV) cleaves the HAV polyprotein P2-P3 at all sites including VP1/2A and 2A/2B. Virology 198:275-281.
    • (1994) Virology , vol.198 , pp. 275-281
    • Schultheiß, T.1    Kusov, Y.Y.2    Gauss-Müller, V.3
  • 32
    • 0028851295 scopus 로고
    • Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates
    • Schultheiß, T., T. W. Sommergruber, Y. Y. Kusov, and V. Gauss-Müller. 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, T.W.2    Kusov, Y.Y.3    Gauss-Müller, V.4
  • 33
    • 0028831056 scopus 로고
    • Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing
    • Tanji, Y., M. Hijikata, T. Kaneko, and K. Shimotohno. 1995. Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing. J. Virol. 69:1575-1581.
    • (1995) J. Virol. , vol.69 , pp. 1575-1581
    • Tanji, Y.1    Hijikata, M.2    Kaneko, T.3    Shimotohno, K.4
  • 34
    • 0028332806 scopus 로고
    • Expression of hepatitis A virus precursor protein P3 in vivo and in vitro: Polyprotein processing of the 3CD cleavage site
    • Tesar, M., I. Pak, X. Y. Jia, O. C. Richards, D. F. Summers, and E. Ehrenfeld. 1994. Expression of hepatitis A virus precursor protein P3 in vivo and in vitro: polyprotein processing of the 3CD cleavage site. Virology 198:524-533.
    • (1994) Virology , vol.198 , pp. 524-533
    • Tesar, M.1    Pak, I.2    Jia, X.Y.3    Richards, O.C.4    Summers, D.F.5    Ehrenfeld, E.6
  • 35
    • 0029998594 scopus 로고    scopus 로고
    • Determinants of membrane association for poliovirus protein 3AB
    • Towner, J. S., T. V. Ho, and B. L. Semler. 1996. Determinants of membrane association for poliovirus protein 3AB. J. Biol. Chem. 271:26810-26818.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26810-26818
    • Towner, J.S.1    Ho, T.V.2    Semler, B.L.3
  • 36
    • 0031816873 scopus 로고    scopus 로고
    • Rescue of defective poliovirus RNA replication by 3AB-containing precursor polyproteins
    • Towner, J. S., M. M. Mazanet, and B. L. Semler. 1998. Rescue of defective poliovirus RNA replication by 3AB-containing precursor polyproteins. J. Virol. 72:7191-7200.
    • (1998) J. Virol. , vol.72 , pp. 7191-7200
    • Towner, J.S.1    Mazanet, M.M.2    Semler, B.L.3
  • 38
    • 0029821259 scopus 로고    scopus 로고
    • Mutagenesis of the coxsackie B3 virus 2B/2C cleavage site: Determinants of processing efficiency and effects on viral replications
    • van Kuppefeld, F. J. M., P. J. J. van den Hurk, J. Zoll, J. M. D. Galama, and W. J. G. Melcher. 1996. Mutagenesis of the coxsackie B3 virus 2B/2C cleavage site: determinants of processing efficiency and effects on viral replications. J. Virol. 70:7632-7640.
    • (1996) J. Virol. , vol.70 , pp. 7632-7640
    • Van Kuppefeld, F.J.M.1    Van Den Hurk, P.J.J.2    Zoll, J.3    Galama, J.M.D.4    Melcher, W.J.G.5
  • 39
    • 0030856299 scopus 로고    scopus 로고
    • Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: Evidence that NSP2 acts as a cofactor for the NSP4 serine protease
    • Wassenaar, A. L. M., W. J. M. Spaan, A. E. Gorbalenya, and E. J. Snijder. 1997. Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: evidence that NSP2 acts as a cofactor for the NSP4 serine protease. J. Virol. 71:9313-9322.
    • (1997) J. Virol. , vol.71 , pp. 9313-9322
    • Wassenaar, A.L.M.1    Spaan, W.J.M.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 40
    • 0029398842 scopus 로고
    • Molecular dissection of the multifunctional poliovirus RNA-binding protein 3AB
    • Xiang, W., A. Cuconati, A. P. Paul, W. Cao, and E. Wimmer. 1995. Molecular dissection of the multifunctional poliovirus RNA-binding protein 3AB. RNA 1:892-904.
    • (1995) RNA , vol.1 , pp. 892-904
    • Xiang, W.1    Cuconati, A.2    Paul, A.P.3    Cao, W.4    Wimmer, E.5
  • 43
    • 0024077061 scopus 로고
    • Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor
    • Ypma-Wong, M. F., P. G. Dewalt, V. H. Johnson, J. G. Lamb, and B. L. Semler. 1988. Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor. Virology 166:265-270.
    • (1988) Virology , vol.166 , pp. 265-270
    • Ypma-Wong, M.F.1    Dewalt, P.G.2    Johnson, V.H.3    Lamb, J.G.4    Semler, B.L.5
  • 44
    • 0028858326 scopus 로고
    • An infectious cDNA clone of a cytopathic hepatitis A virus: Genomic regions associated with rapid replication and cytopathic effects
    • Zhang, H., S. F. Chao, L. H. Ping, K. Grace, B. Clarke, and S. M. Lemon. 1995. An infectious cDNA clone of a cytopathic hepatitis A virus: genomic regions associated with rapid replication and cytopathic effects. Virology 212:686-697.
    • (1995) Virology , vol.212 , pp. 686-697
    • Zhang, H.1    Chao, S.F.2    Ping, L.H.3    Grace, K.4    Clarke, B.5    Lemon, S.M.6


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