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Volumn 74, Issue 1, 2000, Pages 24-32

Mutagenesis of the signal sequence of yellow fever virus prM protein: Enhancement of signalase cleavage in vitro is lethal for virus production

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE; SIGNAL PEPTIDE; VIRUS PROTEIN;

EID: 0033986872     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.74.1.24-32.2000     Document Type: Article
Times cited : (68)

References (31)
  • 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
    • 0025309446 scopus 로고
    • Production of yellow fever proteins in infected cells: Identification of discrete polyprotein species and analysis of cleavage kinetics using region-specific polyclonal antisera
    • Chambers, T. J., D. W. McCourt, and C. M. Rice. 1990. Production of yellow fever proteins in infected cells: identification of discrete polyprotein species and analysis of cleavage kinetics using region-specific polyclonal antisera. Virology 177:159-174.
    • (1990) Virology , vol.177 , pp. 159-174
    • Chambers, T.J.1    McCourt, D.W.2    Rice, C.M.3
  • 4
    • 0030998468 scopus 로고    scopus 로고
    • The chemistry and enzymology of the type 1 signal peptidase
    • Dalbey, R. E., M. O. Lively, S. Bron, and J. M. Van Dijl. 1997. The chemistry and enzymology of the type 1 signal peptidase, Protein Sci. 6:1129-1138.
    • (1997) Protein Sci. , vol.6 , pp. 1129-1138
    • Dalbey, R.E.1    Lively, M.O.2    Bron, S.3    Van Dijl, J.M.4
  • 5
    • 0028849770 scopus 로고
    • Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-hound host protease in the endoplasmic reticulum
    • Falgout, B., and L. Markoff. 1995. Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-hound host protease in the endoplasmic reticulum. J. Virol. 69:7232-7243.
    • (1995) J. Virol. , vol.69 , pp. 7232-7243
    • Falgout, B.1    Markoff, L.2
  • 6
    • 0027081630 scopus 로고
    • The Murray Valley encephalitis virus prM protein confers acid-resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein
    • Guirakhoo, F., R. A. Bolin, and J. T. Roehrig. 1992. The Murray Valley encephalitis virus prM protein confers acid-resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein. Virology 191:921-931.
    • (1992) Virology , vol.191 , pp. 921-931
    • Guirakhoo, F.1    Bolin, R.A.2    Roehrig, J.T.3
  • 7
    • 0025855266 scopus 로고
    • Fusion activity of flaviviruses: Comparison of mature and immature (prM-containing) tick-borne encephalitis virions
    • Guirakhoo, F., F. X. Heinz, C. W. Mandl, H. Holzmann, and C. Kunz. 1991. Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions. J. Gen. Virol. 72:1323-1329.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1323-1329
    • Guirakhoo, F.1    Heinz, F.X.2    Mandl, C.W.3    Holzmann, H.4    Kunz, C.5
  • 8
    • 0026787448 scopus 로고
    • Single amino acid substitutions can convert the uncleaved signal-anchor of sucrose-isomaltase to a cleaved signal sequence
    • Hegner, M., A. von Kiekebusch-Glück, R. Falchetto, P. James, G. Semenza, and N. Mantei. 1992. Single amino acid substitutions can convert the uncleaved signal-anchor of sucrose-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 Kiekebusch-Glück, A.2    Falchetto, R.3    James, P.4    Semenza, G.5    Mantei, N.6
  • 9
    • 0028243260 scopus 로고
    • Signal peptide cleavage regions. Functional limits on length and topological implications
    • Jain, R. G., S. L. Rusch, and D. A. Kendall. 1994. Signal peptide cleavage regions. Functional limits on length and topological implications. J. Biol. Chem. 269:16305-16310.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16305-16310
    • Jain, R.G.1    Rusch, S.L.2    Kendall, D.A.3
  • 10
    • 0027475018 scopus 로고
    • Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 protease is a prerequisite for processing at the downstream 4A/4B signalase site
    • Lin, C., S. M. Amberg, T. J. Chambers, and C. M. Rice. 1993. Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 protease is a prerequisite for processing at the downstream 4A/4B signalase site. J. Virol. 67:2327-2335.
    • (1993) J. Virol. , vol.67 , pp. 2327-2335
    • Lin, C.1    Amberg, S.M.2    Chambers, T.J.3    Rice, C.M.4
  • 11
    • 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
  • 12
    • 0026756141 scopus 로고
    • Proteolytic processing of a Murray Valley encephalitis virus non-structural 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 non-structural 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
  • 13
    • 0023577758 scopus 로고
    • Location of a neutralization domain in the E protein of yellow fever virus (17D vaccine strain)
    • Lobigs, M., L. Dalgarno, J. J. Schlesinger, and R. C. Weir. 1987. Location of a neutralization domain in the E protein of yellow fever virus (17D vaccine strain). Virology 161:474-478.
    • (1987) Virology , vol.161 , pp. 474-478
    • Lobigs, M.1    Dalgarno, L.2    Schlesinger, J.J.3    Weir, R.C.4
  • 14
    • 0027948541 scopus 로고
    • Processing of the flavivirus structural glycoproteins: Stable membrane insertion of premembrane requires the envelope signal peptide
    • Markoff, L., A. Chang, and B. Falgout. 1994. Processing of the flavivirus structural glycoproteins: stable membrane insertion of premembrane requires the envelope signal peptide. Virology 204:526-540.
    • (1994) Virology , vol.204 , pp. 526-540
    • Markoff, L.1    Chang, A.2    Falgout, B.3
  • 15
    • 0001925194 scopus 로고    scopus 로고
    • Flaviviruses
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven Publishers, Philadelphia, Pa.
    • Monath, T. P., and F. X. Heinz. 1996. Flaviviruses, p. 961-1034. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Fields virology, 3rd ed. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 961-1034
    • Monath, T.P.1    Heinz, F.X.2
  • 16
    • 0030218225 scopus 로고    scopus 로고
    • Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: Effect on virus replication and mouse neurovirulence
    • Muylaert, I. R., T. J. Chambers, R. Galler, and C. M. Rice. 1996. Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: effect on virus replication and mouse neurovirulence. Virology 222:159-168.
    • (1996) Virology , vol.222 , pp. 159-168
    • Muylaert, I.R.1    Chambers, T.J.2    Galler, R.3    Rice, C.M.4
  • 17
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor
    • Paetzel, M., R. E. Dalbey, and N. C. J. Strynadka. 1998. Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor. Nature 396:186-190.
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.J.3
  • 18
    • 0026443667 scopus 로고
    • Mutational analysis of the octapeptide sequence motif at the NS1-NS2A cleavage junction of dengue type 4 virus
    • Pethel, M., B. Falgout, and C.-J. Lai. 1992. Mutational analysis of the octapeptide sequence motif at the NS1-NS2A cleavage junction of dengue type 4 virus. J. Virol. 66:7225-7231.
    • (1992) J. Virol. , vol.66 , pp. 7225-7231
    • Pethel, M.1    Falgout, B.2    Lai, C.-J.3
  • 19
    • 0032997525 scopus 로고    scopus 로고
    • Protein translocation: How HSP70 pulls it off
    • Pilon, M., and R. Schekman. 1999. Protein translocation: how HSP70 pulls it off. Cell 97:679-682.
    • (1999) Cell , vol.97 , pp. 679-682
    • Pilon, M.1    Schekman, R.2
  • 20
    • 0025064269 scopus 로고
    • Acidotropic amines inhibit proteolytic processing of flavivirus prM protein
    • Randolph, V. R., G. Winkler, and V. Stollar. 1990. Acidotropic amines inhibit proteolytic processing of flavivirus prM protein. Virology 174:450-458.
    • (1990) Virology , vol.174 , pp. 450-458
    • Randolph, V.R.1    Winkler, G.2    Stollar, V.3
  • 21
    • 0026471714 scopus 로고
    • Transport of proteins across the endoplasmic reticulum membrane
    • Rapoporl, T. A. 1992. Transport of proteins across the endoplasmic reticulum membrane. Science 258:931-935.
    • (1992) Science , vol.258 , pp. 931-935
    • Rapoporl, T.A.1
  • 22
    • 0001424128 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven Publishers, Philadelphia, Pa.
    • Rice, C. M. 1996. Flaviviridae: the viruses and their replication, p. 931-959. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 931-959
    • Rice, C.M.1
  • 23
    • 0024892209 scopus 로고
    • Transcription of infectious yellow fever virus RNA from full-length cDNA templates produced by in vitro ligation
    • Rice, C. M., A. Grakoui, R. Galler, and T. J. Chambers. 1989 Transcription of infectious yellow fever virus RNA from full-length cDNA templates produced by in vitro ligation. New Biol. 1:285-296.
    • (1989) New Biol. , vol.1 , pp. 285-296
    • Rice, C.M.1    Grakoui, A.2    Galler, R.3    Chambers, T.J.4
  • 24
    • 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
  • 25
    • 0031935890 scopus 로고    scopus 로고
    • 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
    • Stocks, C. E., and M. Lobigs. 1998. 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. J. Virol. 72:2141-2149.
    • (1998) J. Virol. , vol.72 , pp. 2141-2149
    • Stocks, C.E.1    Lobigs, M.2
  • 26
    • 0032511879 scopus 로고    scopus 로고
    • Life and death of a signal peptide
    • von Heijne, G. 1998. Life and death of a signal peptide. Nature 396:111-113.
    • (1998) Nature , vol.396 , pp. 111-113
    • Von Heijne, G.1
  • 27
    • 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
  • 28
    • 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
  • 29
    • 0023928974 scopus 로고
    • Transcending the impenetrable: How proteins come to terms with membranes
    • von Heijne, G. 1988. Transcending the impenetrable: how proteins come to terms with membranes. Biochim. Biophys. Acta 947:307-333.
    • (1988) Biochim. Biophys. Acta , vol.947 , pp. 307-333
    • Von Heijne, G.1
  • 30
    • 0025997062 scopus 로고
    • Rapid, small-scale RNA isolation from tissue culture cells
    • Xie, W. Q., and L. I. Rothblum. 1991. Rapid, small-scale RNA isolation from tissue culture cells. BioTechniques 11:324-327.
    • (1991) BioTechniques , vol.11 , pp. 324-327
    • Xie, W.Q.1    Rothblum, L.I.2
  • 31
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.