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Volumn 73, Issue 8, 1999, Pages 6220-6227

Maturation of the hepatitis A virus capsid protein VP1 is not dependent on processing by the 3C(pro) proteinase

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; PROTEINASE;

EID: 0345643403     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.8.6220-6227.1999     Document Type: Article
Times cited : (34)

References (31)
  • 1
    • 0028328469 scopus 로고
    • Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases
    • Allaire, M., M. M. Chernaia, B. A. Malcolm, and M. N. James. 1994. Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature 369:72-76.
    • (1994) Nature , vol.369 , pp. 72-76
    • Allaire, M.1    Chernaia, M.M.2    Malcolm, B.A.3    James, M.N.4
  • 2
    • 0025036493 scopus 로고
    • Morphogenesis of hepatitis A virus: Isolation and characterization of subviral particles
    • Anderson, D. A., and B. C. Ross. 1990. Morphogenesis of hepatitis A virus: isolation and characterization of subviral particles. J. Virol. 64:5284-5289.
    • (1990) J. Virol. , vol.64 , pp. 5284-5289
    • Anderson, D.A.1    Ross, B.C.2
  • 4
    • 85069140616 scopus 로고    scopus 로고
    • Personal communication
    • Bergmann, E. M. Personal communication.
    • Bergmann, E.M.1
  • 5
    • 0002647817 scopus 로고    scopus 로고
    • Proteolytic enzymes of the viruses of the family Picornaviridae
    • B. Dunn (ed.). Academic Press, San Diego, Calif.
    • Bergmann, E. M., and M. N. G. James. 1999. Proteolytic enzymes of the viruses of the family Picornaviridae, p. 139-163. In B. Dunn (ed.), Proteinases of infectious agents. Academic Press, San Diego, Calif.
    • (1999) Proteinases of Infectious Agents , pp. 139-163
    • Bergmann, E.M.1    James, M.N.G.2
  • 6
    • 0024588088 scopus 로고
    • Mengo virus maturation is accompanied by C-terminal modification of capsid protein VP1
    • Boege, U., and D. G. Scraba. 1989. Mengo virus maturation is accompanied by C-terminal modification of capsid protein VP1. Virology 168:409-412.
    • (1989) Virology , vol.168 , pp. 409-412
    • Boege, U.1    Scraba, D.G.2
  • 7
    • 0027315290 scopus 로고
    • Synthesis and assembly of hepatitis A virus-specific proteins in BS-C-1 cells
    • Borovec, S. V., and D. A. Anderson. 1993. Synthesis and assembly of hepatitis A virus-specific proteins in BS-C-1 cells. J. Virol. 67:3095-3102.
    • (1993) J. Virol. , vol.67 , pp. 3095-3102
    • Borovec, S.V.1    Anderson, D.A.2
  • 9
    • 0023214707 scopus 로고
    • Hepatitis A virus cDNA and its RNA transcripts are infectious in cell culture
    • Cohen, J. I., J. R. Ticehurst, S. M. Feinstone, B. Rosenblum, and R. H. Purcell. 1987. Hepatitis A virus cDNA and its RNA transcripts are infectious in cell culture. J. Virol. 61:3035-3039.
    • (1987) J. Virol. , vol.61 , pp. 3035-3039
    • Cohen, J.I.1    Ticehurst, J.R.2    Feinstone, S.M.3    Rosenblum, B.4    Purcell, R.H.5
  • 10
    • 0031022685 scopus 로고    scopus 로고
    • The cleavage activities of aphthovirus and cardiovirus 2A proteins
    • g. Donnelly, M. L., D. Gani, M. Flint, S. Monaghan, and M. D. Ryan. 1997. The cleavage activities of aphthovirus and cardiovirus 2A proteins. J. Gen. Virol. 78:13-21.
    • (1997) J. Gen. Virol. , vol.78 , pp. 13-21
    • Donnelly, M.L.1    Gani, D.2    Flint, M.3    Monaghan, S.4    Ryan, M.D.5
  • 11
    • 0028874914 scopus 로고
    • The proposed gene for VP1 of HAV encodes for a larger protein than that observed in HAV-infected cells and virions
    • Dotzauer, A., A. Vallbracht, and G. M. Keil. 1995. The proposed gene for VP1 of HAV encodes for a larger protein than that observed in HAV-infected cells and virions. Virology 213:671-675.
    • (1995) Virology , vol.213 , pp. 671-675
    • Dotzauer, A.1    Vallbracht, A.2    Keil, G.M.3
  • 12
    • 0020045092 scopus 로고
    • Complementation and genetic linkage between vaccinia virus temperature-sensitive mutants
    • Drillien, R., D. Spehner, and A. Kirn. 1982. Complementation and genetic linkage between vaccinia virus temperature-sensitive mutants. Virology 119: 372-381.
    • (1982) Virology , vol.119 , pp. 372-381
    • Drillien, R.1    Spehner, D.2    Kirn, A.3
  • 13
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthetizes bacteriophage T7 RNA polymerase
    • Fuerst, T. R., E. G. Niles, F. W. Studier, and B. Moss. 1986. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthetizes 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
  • 14
    • 0022906049 scopus 로고
    • Characterization of hepatitis A virus structural proteins
    • Gauss-Muller, V., F. Lottspeich, and F. Deinhardt. 1986. Characterization of hepatitis A virus structural proteins. Virology 155:732-736.
    • (1986) Virology , vol.155 , pp. 732-736
    • Gauss-Muller, V.1    Lottspeich, F.2    Deinhardt, F.3
  • 15
    • 0030045348 scopus 로고    scopus 로고
    • Identification of hepatitis A virus non-structural protein 2B and its release by the major virus protease 3C
    • Gosert, R., P. Cassinotti, G. Siegl, and M. Weitz. 1996. Identification of hepatitis A virus non-structural protein 2B and its release by the major virus protease 3C. J. Gen. Virol. 77:247-255.
    • (1996) J. Gen. Virol. , vol.77 , pp. 247-255
    • Gosert, R.1    Cassinotti, P.2    Siegl, G.3    Weitz, M.4
  • 16
    • 0026646534 scopus 로고
    • Hepatitis A virus 3C proteinase substrate specificity
    • Jewell, D. A., W. Swietnicki, B. M. Dunn, and B. A. Malcom. 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    Malcom, B.A.4
  • 17
    • 0027272084 scopus 로고
    • Primary cleavage of the HAV capsid protein precursor in the middle of the proposed 2A coding region
    • Jia, X. Y., D. F. Summers, and E. Ehrenfeld. 1993. Primary cleavage of the HAV capsid protein precursor in the middle of the proposed 2A coding region. Virology 193:515-519.
    • (1993) Virology , vol.193 , pp. 515-519
    • Jia, X.Y.1    Summers, D.F.2    Ehrenfeld, E.3
  • 18
    • 0020522468 scopus 로고
    • Radioimmunofocus assay for quantitation of hepatitis a virus in cell cultures
    • Lemon, S. M., L. N. Binn, and R. H. Marchwicki. 1983. Radioimmunofocus assay for quantitation of hepatitis A virus in cell cultures. J. Clin. Microbiol. 17:834-839.
    • (1983) J. Clin. Microbiol. , vol.17 , pp. 834-839
    • Lemon, S.M.1    Binn, L.N.2    Marchwicki, R.H.3
  • 19
    • 0026069630 scopus 로고
    • Antigenic and genetic variation in cytopathic hepatitis A virus variants arising during persistent infection: Evidence for genetic recombination
    • Lemon, S. M., P. C. Murphy, P. A. Shields, L. H. Ping, S. M. Feinstone, T. Cromeans, and R. W. Jansen. 1991. Antigenic and genetic variation in cytopathic hepatitis A virus variants arising during persistent infection: evidence for genetic recombination. J. Virol. 65:2056-2065.
    • (1991) J. Virol. , vol.65 , pp. 2056-2065
    • Lemon, S.M.1    Murphy, P.C.2    Shields, P.A.3    Ping, L.H.4    Feinstone, S.M.5    Cromeans, T.6    Jansen, R.W.7
  • 20
    • 0000420959 scopus 로고
    • Current perspectives in the virology and molecular biology of hepatitis A virus
    • Lemon, S. M., and B. H. Robertson. 1993. Current perspectives in the virology and molecular biology of hepatitis A virus. Semin. Virol. 4:285-295.
    • (1993) Semin. Virol. , vol.4 , pp. 285-295
    • Lemon, S.M.1    Robertson, B.H.2
  • 23
    • 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
  • 25
    • 0025011840 scopus 로고
    • Proteolytic processing of picornaviral polyprotein
    • Palmenberg, A. C. 1990. Proteolytic processing of picornaviral polyprotein. Annu. Rev. Microbiol. 44:603-623.
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 603-623
    • Palmenberg, A.C.1
  • 26
    • 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. Jechl, and V. Gauss-Muller. 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    Jechl, M.2    Gauss-Muller, V.3
  • 27
    • 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-Muller. 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-Muller, V.3
  • 28
    • 0028851295 scopus 로고
    • Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates
    • Schultheiss, T., W. Sommergruber, Y. Kusov, and V. Gauss-Muller. 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
  • 29
    • 0026786146 scopus 로고
    • Enzymatic inverse PCR: A restriction site independent, single-fragment method for high-efficiency, site-directed mutagenesis
    • Stemmer, W. P. C., and S. K. Morris. 1992. Enzymatic inverse PCR: a restriction site independent, single-fragment method for high-efficiency, site-directed mutagenesis. BioTechniques 13:215-220.
    • (1992) BioTechniques , vol.13 , pp. 215-220
    • Stemmer, W.P.C.1    Morris, S.K.2
  • 30
    • 0022429789 scopus 로고
    • The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate modified DNA
    • Taylor, J. W., J. Ott, and F. Eckstein. 1985. The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate modified DNA. Nucleic Acids Res. 13:8765-8785.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 8765-8785
    • Taylor, J.W.1    Ott, J.2    Eckstein, F.3
  • 31
    • 0028858326 scopus 로고
    • An infectious cDNA clone of a cytopathic hepatitis A virus: Genomic regions associated with rapid replication and cytopathic effect
    • Zhang, H., S.-F. Chao, L.-M. 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 effect. Virology 212:686-697.
    • (1995) Virology , vol.212 , pp. 686-697
    • Zhang, H.1    Chao, S.-F.2    Ping, L.-M.3    Grace, K.4    Clarke, B.5    Lemon, S.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.