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Volumn 72, Issue 3, 1998, Pages 2141-2149

Signal peptidase cleavage at the flavivirus C-prM junction: Dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; PROTEINASE; SIGNAL PEPTIDASE; SIGNAL PEPTIDE; VIRUS ENVELOPE PROTEIN;

EID: 0031935890     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.3.2141-2149.1998     Document Type: Article
Times cited : (131)

References (44)
  • 1
    • 0028304762 scopus 로고
    • NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: In vitro and in vivo studies
    • Amberg, S. M., A. Nestorowicz, D. W. McCourt, and C. M. Rice. 1994. NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: in vitro and in vivo studies. J. Virol. 68:3794-3802.
    • (1994) J. Virol. , vol.68 , pp. 3794-3802
    • Amberg, S.M.1    Nestorowicz, A.2    McCourt, D.W.3    Rice, C.M.4
  • 2
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., D. Finley, and A. Varshavsky. 1986. In vivo half-life of a protein is a function of its amino-terminal residue. Science 234:179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 3
    • 0028142992 scopus 로고
    • Protein expression using cotranslational fusion and cleavage of ubiquitin
    • Baker, R. T., S. A. Smith, R. Marano, J. McKee, and P. G. Board. 1994. Protein expression using cotranslational fusion and cleavage of ubiquitin. J. Biol. Chem. 269:25381-25386.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25381-25386
    • Baker, R.T.1    Smith, S.A.2    Marano, R.3    McKee, J.4    Board, P.G.5
  • 4
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel, G., and B. Dobberstein. 1975. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67:835-851.
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 5
    • 85047669331 scopus 로고    scopus 로고
    • Post-translational protein translocation: Not all hsc70s are created equal
    • Brodsky, J. L. 1996. Post-translational protein translocation: not all hsc70s are created equal. Trends Biochem. Sci. 21:122-126.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 122-126
    • Brodsky, J.L.1
  • 6
    • 0022255160 scopus 로고
    • Sequence analysis of the viral core protein and the membrane-associated proteins V1 and NV2 of the flavivirus West Nile virus and of the genome sequence for these proteins
    • Castle, E., T. Nowak, U. Leidner, G. Wengler, and G. Wengler. 1985. Sequence analysis of the viral core protein and the membrane-associated proteins V1 and NV2 of the flavivirus West Nile virus and of the genome sequence for these proteins. Virology 145:227-236.
    • (1985) Virology , vol.145 , pp. 227-236
    • Castle, E.1    Nowak, T.2    Leidner, U.3    Wengler, G.4    Wengler, G.5
  • 7
    • 0023854242 scopus 로고
    • Nucleotide and complete amino acid sequences of Kunjin virus: Definitive gene order and characteristics of the virus-specified proteins
    • Coia, G., M. D. Parker, G. Speight, M. E. Byrne, and E. G. Westaway. 1988. Nucleotide and complete amino acid sequences of Kunjin virus: definitive gene order and characteristics of the virus-specified proteins. J. Gen. Virol. 69:1-21.
    • (1988) J. Gen. Virol. , vol.69 , pp. 1-21
    • Coia, G.1    Parker, M.D.2    Speight, G.3    Byrne, M.E.4    Westaway, E.G.5
  • 8
    • 0022486530 scopus 로고
    • Partial nucleotide sequence of the Murray Valley encephalitis virus genome. Comparison of the encoded polypeptides with yellow fever virus structural and non-structural proteins
    • Dalgarno, L., D. W. Trent, J. H. Strauss, and C. M. Rice. 1986. Partial nucleotide sequence of the Murray Valley encephalitis virus genome. Comparison of the encoded polypeptides with yellow fever virus structural and non-structural proteins. J. Mol. Biol. 187:309-323.
    • (1986) J. Mol. Biol. , vol.187 , pp. 309-323
    • Dalgarno, L.1    Trent, D.W.2    Strauss, J.H.3    Rice, C.M.4
  • 9
    • 0025352629 scopus 로고
    • Cleavage-site preferences of Sindbis virus polyproteins containing the non-structural proteinase. Evidence for temporal regulation of polyprotein processing in vivo
    • de Groot, R. J., W. R. Hardy, Y. Shirako, and J. H. Strauss. 1990. Cleavage-site preferences of Sindbis virus polyproteins containing the non-structural proteinase. Evidence for temporal regulation of polyprotein processing in vivo. EMBO J. 9:2631-2638.
    • (1990) EMBO J. , vol.9 , pp. 2631-2638
    • De Groot, R.J.1    Hardy, W.R.2    Shirako, Y.3    Strauss, J.H.4
  • 10
    • 0023805562 scopus 로고
    • Dengue 2 virus envelope protein expressed by a recombinant vaccinia virus fails to protect monkeys against dengue
    • Deubel, V., R. M. Kinney, J. J. Esposito, C. B. Cropp, A. V. Vorndam, T. P. Monatb, and D. W. Trent. 1988. Dengue 2 virus envelope protein expressed by a recombinant vaccinia virus fails to protect monkeys against dengue. J. Gen. Virol. 69:1921-1929.
    • (1988) J. Gen. Virol. , vol.69 , pp. 1921-1929
    • Deubel, V.1    Kinney, R.M.2    Esposito, J.J.3    Cropp, C.B.4    Vorndam, A.V.5    Monatb, T.P.6    Trent, D.W.7
  • 11
    • 0028039833 scopus 로고
    • Recombinant vaccinia viruses co-expressing dengue-1 glycoproteins prM and E induce neutralizing antibodies in mice
    • Fonseca, B. A., S. Pincus, R. E. Shope, E. Paoletti, and P. W. Mason. 1994. Recombinant vaccinia viruses co-expressing dengue-1 glycoproteins prM and E induce neutralizing antibodies in mice. Vaccine 12:279-285.
    • (1994) Vaccine , vol.12 , pp. 279-285
    • Fonseca, B.A.1    Pincus, S.2    Shope, R.E.3    Paoletti, E.4    Mason, P.W.5
  • 12
    • 0028834046 scopus 로고
    • Can Hsp70 proteins act as force-generating motors?
    • Glick, B. S. 1995. Can Hsp70 proteins act as force-generating motors? Cell 80:11-14.
    • (1995) Cell , vol.80 , pp. 11-14
    • Glick, B.S.1
  • 13
    • 0023845168 scopus 로고
    • Nucleotide sequence of dengue 2 RNA and comparison of the encoded proteins with those of other flaviviruses
    • Hahn, Y. S., R. Galler, T. Hunkapiller, J. M. Dalrymple, J. H. Strauss, and E. G. Strauss. 1988. Nucleotide sequence of dengue 2 RNA and comparison of the encoded proteins with those of other flaviviruses. Virology 162:167-180.
    • (1988) Virology , vol.162 , pp. 167-180
    • Hahn, Y.S.1    Galler, R.2    Hunkapiller, T.3    Dalrymple, J.M.4    Strauss, J.H.5    Strauss, E.G.6
  • 14
    • 0025605053 scopus 로고
    • Epitope analysis of the envelope and non-structural glycoproteins of Murray Valley encephalitis virus
    • Hall, R. A., B. H. Kay, G. W. Burgess, P. Clancy, and I. D. Fanning. 1990. Epitope analysis of the envelope and non-structural glycoproteins of Murray Valley encephalitis virus. J. Gen. Virol. 71:2923-2930.
    • (1990) J. Gen. Virol. , vol.71 , pp. 2923-2930
    • Hall, R.A.1    Kay, B.H.2    Burgess, G.W.3    Clancy, P.4    Fanning, I.D.5
  • 15
    • 0026787448 scopus 로고
    • Single amino acid substitutions can convert the uncleaved signal-anchor of sucrase-isomaltase to a cleaved signal sequence
    • Hegner, M., A. von Kieckebusch-Gück, R. Falchetto, P. James, G. Semenza, and N. Mantei. 1992. Single amino acid substitutions can convert the uncleaved signal-anchor of sucrase-isomaltase to a cleaved signal sequence. J. Biol. Chem. 267:16928-16933.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16928-16933
    • Hegner, M.1    Von Kieckebusch-Gück, A.2    Falchetto, R.3    James, P.4    Semenza, G.5    Mantei, N.6
  • 16
    • 0024830949 scopus 로고
    • Proteolytic processing of polyproteins in the replication of RNA viruses
    • Hellen, C. U. T., H.-G. Kräusslich, and E. Wimmer. 1989. Proteolytic processing of polyproteins in the replication of RNA viruses. Biochemistry 28:9881-9890.
    • (1989) Biochemistry , vol.28 , pp. 9881-9890
    • Hellen, C.U.T.1    Kräusslich, H.-G.2    Wimmer, E.3
  • 18
    • 0025998889 scopus 로고
    • Comparison of protective immunity elicited by recombinant vaccinia viruses that synthesize E or NS1 of Japanese encephalitis virus
    • Konishi, E., S. Pincus, B. A. Fonseca, R. E. Shope, E. Paoletti, and P. W. Mason. 1991. Comparison of protective immunity elicited by recombinant vaccinia viruses that synthesize E or NS1 of Japanese encephalitis virus. Virology 185:401-410.
    • (1991) Virology , vol.185 , pp. 401-410
    • Konishi, E.1    Pincus, S.2    Fonseca, B.A.3    Shope, R.E.4    Paoletti, E.5    Mason, P.W.6
  • 20
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 22
    • 0028221438 scopus 로고
    • Polypeptide requirements for assembly of functional Sindbis virus replication complexes: A model for the temporal regulation of minus- and plus-strand RNA synthesis
    • Lemm, J. A., T. Rümenapf, E. G. Strauss, J. H. Strauss, and C. M. Rice. 1994. Polypeptide requirements for assembly of functional Sindbis virus replication complexes: a model for the temporal regulation of minus-and plus-strand RNA synthesis. EMBO J. 13:2925-2934.
    • (1994) EMBO J. , vol.13 , pp. 2925-2934
    • Lemm, J.A.1    Rümenapf, T.2    Strauss, E.G.3    Strauss, J.H.4    Rice, C.M.5
  • 23
    • 0027264853 scopus 로고
    • Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3
    • Lobigs, M. 1993. Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3. Proc. Natl. Acad. Sci. USA 90:6218-6222.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6218-6222
    • Lobigs, M.1
  • 24
    • 0026756141 scopus 로고
    • Proteolytic processing of a Murray Valley encephalitis virus nonstructural polyprotein segment containing the viral proteinase: Accumulation of a NS3-4A precursor which requires mature NS3 for efficient processing
    • Lobigs, M. 1992. Proteolytic processing of a Murray Valley encephalitis virus nonstructural polyprotein segment containing the viral proteinase: accumulation of a NS3-4A precursor which requires mature NS3 for efficient processing. J. Gen. Virol. 73:2305-2312.
    • (1992) J. Gen. Virol. , vol.73 , pp. 2305-2312
    • Lobigs, M.1
  • 25
    • 0025003156 scopus 로고
    • Function of Semliki Forest virus E3 peptide in virus assembly: Replacement of E3 with an artificial signal peptide abolishes spike heterodimerization and surface expression of E1
    • Lobigs, M., H. Zhao, and H. Garoff. 1990. Function of Semliki Forest virus E3 peptide in virus assembly: replacement of E3 with an artificial signal peptide abolishes spike heterodimerization and surface expression of E1. J. Virol. 64:4346-4355.
    • (1990) J. Virol. , vol.64 , pp. 4346-4355
    • Lobigs, M.1    Zhao, H.2    Garoff, H.3
  • 26
    • 0023811062 scopus 로고
    • Sequence of the structural proteins of tick-borne encephalitis virus (western subtype) and comparative analysis with other flaviviruses
    • Mandl, C. W., F. X. Heinz, and C. Kunz. 1988. Sequence of the structural proteins of tick-borne encephalitis virus (western subtype) and comparative analysis with other flaviviruses. Virology 166:197-205.
    • (1988) Virology , vol.166 , pp. 197-205
    • Mandl, C.W.1    Heinz, F.X.2    Kunz, C.3
  • 27
    • 0028101487 scopus 로고
    • The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase
    • Nilsson, I., P. Whitley, and G. von Heijne. 1994. The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase. J. Cell Biol. 126:1127-1132.
    • (1994) J. Cell Biol. , vol.126 , pp. 1127-1132
    • Nilsson, I.1    Whitley, P.2    Von Heijne, G.3
  • 28
    • 0024513348 scopus 로고
    • Eukaryotic signal peptide structure/ function relationships
    • Nothwehr, S. F., and J. I. Gordon. 1989. Eukaryotic signal peptide structure/ function relationships. J. Biol. Chem. 264:3979-3987.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3979-3987
    • Nothwehr, S.F.1    Gordon, J.I.2
  • 29
    • 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
  • 30
    • 0026505138 scopus 로고
    • Recombinant vaccinia virus producing the prM and E proteins of yellow fever virus protects mice from lethal yellow fever encephalitis
    • Pincus, S., P. W. Mason, E. Konishi, B. A. L. Fonseca, R. E. Shope, C. M. Rice, and E. Paoletti. 1992. Recombinant vaccinia virus producing the prM and E proteins of yellow fever virus protects mice from lethal yellow fever encephalitis. Virology 187:290-297.
    • (1992) Virology , vol.187 , pp. 290-297
    • Pincus, S.1    Mason, P.W.2    Konishi, E.3    Fonseca, B.A.L.4    Shope, R.E.5    Rice, C.M.6    Paoletti, E.7
  • 31
    • 0001424128 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman and S. E. Strauss (ed.), Lippincott-Raven, Philadelphia, Pa.
    • Rice, C. M. 1996. Flaviviridae: the viruses and their replication, p. 931-959. In B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman and S. E. Strauss (ed.), Fields virology, 3rd ed. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 931-959
    • Rice, C.M.1
  • 32
    • 0021863828 scopus 로고
    • Nucleotide sequence of yellow fever virus: Implications for flavivirus gene expression and evolution
    • Rice, C. M., E. M. Lenches, S. R. Eddy, S. J. Shin, R. L. Sheets, and J. H. Strauss. 1985. Nucleotide sequence of yellow fever virus: implications for flavivirus gene expression and evolution. Science 229:726-733.
    • (1985) Science , vol.229 , pp. 726-733
    • Rice, C.M.1    Lenches, E.M.2    Eddy, S.R.3    Shin, S.J.4    Sheets, R.L.5    Strauss, J.H.6
  • 33
    • 0024416324 scopus 로고
    • Processing of yellow fever virus polyprotein: Role of cellular proteases in maturation of the structural proteins
    • Ruiz-Linares, A., A. Cahour, P. Desprès, M. Girard, and M. Bouloy. 1989. Processing of yellow fever virus polyprotein: role of cellular proteases in maturation of the structural proteins. J. Virol. 63:4199-4209.
    • (1989) J. Virol. , vol.63 , pp. 4199-4209
    • Ruiz-Linares, A.1    Cahour, A.2    Desprès, P.3    Girard, M.4    Bouloy, M.5
  • 34
    • 0027282580 scopus 로고
    • High-level expression of the Japanese encephalitis virus E protein by recombinant vaccinia virus and enhancement of its extracellular release by the NS3 gene product
    • Sato, T., C. Takamura, A. Yasuda, M. Miyamoto, K. Kamogawa, and K. Yasui. 1993. High-level expression of the Japanese encephalitis virus E protein by recombinant vaccinia virus and enhancement of its extracellular release by the NS3 gene product. Virology 192:483-490.
    • (1993) Virology , vol.192 , pp. 483-490
    • Sato, T.1    Takamura, C.2    Yasuda, A.3    Miyamoto, M.4    Kamogawa, K.5    Yasui, K.6
  • 35
    • 0031567996 scopus 로고    scopus 로고
    • Are transporter associated with antigen processing (TAP) and tapasin class I MHC chaperones?
    • Solheim, J. C., B. M. Carreno, and T. H. Hansen. 1997. Are transporter associated with antigen processing (TAP) and tapasin class I MHC chaperones? J. Immunol. 158:541-543.
    • (1997) J. Immunol. , vol.158 , pp. 541-543
    • Solheim, J.C.1    Carreno, B.M.2    Hansen, T.H.3
  • 37
    • 0028822211 scopus 로고
    • Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
    • Stocks, C. E., and M. Lobigs. 1995. Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro. J. Virol. 69:8123-8126.
    • (1995) J. Virol. , vol.69 , pp. 8123-8126
    • Stocks, C.E.1    Lobigs, M.2
  • 38
    • 0023785887 scopus 로고
    • A multisite-directed mutagenesis using T7 DNA polymerase: Application for reconstructing a mammalian gene
    • Su, T.-Z., and M. R. El-Gewely. 1988. A multisite-directed mutagenesis using T7 DNA polymerase: application for reconstructing a mammalian gene. Gene 69:81-39.
    • (1988) Gene , vol.69 , pp. 81-139
    • Su, T.-Z.1    El-Gewely, M.R.2
  • 40
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 41
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne, G. 1990. The signal peptide. J. Membr. Biol. 115:195-201.
    • (1990) J. Membr. Biol. , vol.115 , pp. 195-201
    • Von Heijne, G.1
  • 42
    • 0023852637 scopus 로고
    • Proteases involved in the processing of viral polyproteins
    • Wellink, J., and A. van Kammen. 1988. Proteases involved in the processing of viral polyproteins. Arch. Virol. 98:1-26.
    • (1988) Arch. Virol. , vol.98 , pp. 1-26
    • Wellink, J.1    Van Kammen, A.2
  • 43
    • 0027308196 scopus 로고
    • Regulation of the late events in flavivirus protein processing and maturation
    • Yamshchikov, V. F., and R. W. Compans. 1993. Regulation of the late events in flavivirus protein processing and maturation. Virology 192:38-51.
    • (1993) Virology , vol.192 , pp. 38-51
    • Yamshchikov, V.F.1    Compans, R.W.2
  • 44
    • 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


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