메뉴 건너뛰기




Volumn 71, Issue 6, 1997, Pages 4364-4371

Upregulation of signalase processing and induction of prM-E secretion by the flavivirus NS2B-NS3 protease: Roles of protease components

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN PRECURSOR; PROTEINASE; TRIPEPTIDE; VIRUS PROTEIN;

EID: 0030923806     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.6.4364-4371.1997     Document Type: Article
Times cited : (30)

References (37)
  • 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
    • 0027285404 scopus 로고
    • Dengue 2 virus NS2B and NS3 form a stable complex that can cleave NS3 within the helicase domain
    • Arias, C. F., F. Preugschat, and J. M. Strauss. 1993. Dengue 2 virus NS2B and NS3 form a stable complex that can cleave NS3 within the helicase domain. Virology 193:888-899.
    • (1993) Virology , vol.193 , pp. 888-899
    • Arias, C.F.1    Preugschat, F.2    Strauss, J.M.3
  • 3
    • 0024372153 scopus 로고
    • Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses
    • Bazan, J. F., and R. J. Fletterick. 1989. Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses. Virology 171:637-639.
    • (1989) Virology , vol.171 , pp. 637-639
    • Bazan, J.F.1    Fletterick, R.J.2
  • 4
    • 0023111411 scopus 로고
    • Characterization of protease cleavage sites involved in the formation of envelope glycoprotein and three nonstructural proteins of dengue virus type 2, New Guinea C strain
    • Biedrzycka, A., M. R. Cauchi, A. Bartholomeusz, J. J. Gorman, and P. J. Wright. 1987. Characterization of protease cleavage sites involved in the formation of envelope glycoprotein and three nonstructural proteins of dengue virus type 2, New Guinea C strain. J. Gen. Virol. 68:1317-1326.
    • (1987) J. Gen. Virol. , vol.68 , pp. 1317-1326
    • Biedrzycka, A.1    Cauchi, M.R.2    Bartholomeusz, A.3    Gorman, J.J.4    Wright, P.J.5
  • 5
    • 0022632048 scopus 로고
    • Primary structure of the West Nile flavivirus genome region coding for all nonstructural proteins
    • Castle, E., U. Leidner, T. Nowak, G. Wengler, and G. Wengler. 1986. Primary structure of the West Nile flavivirus genome region coding for all nonstructural proteins. Virology 149:10-26.
    • (1986) Virology , vol.149 , pp. 10-26
    • Castle, E.1    Leidner, U.2    Nowak, T.3    Wengler, G.4    Wengler, G.5
  • 6
    • 0026039916 scopus 로고
    • Processing of yellow fever virus nonstructural polyprotein: A catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sites
    • Chambers, T. J., A. Grakoui, and C. M. Rice. 1991. Processing of yellow fever virus nonstructural polyprotein: a catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sites. J. Virol. 65: 6042-6050.
    • (1991) J. Virol. , vol.65 , pp. 6042-6050
    • Chambers, T.J.1    Grakoui, A.2    Rice, C.M.3
  • 7
    • 0027486484 scopus 로고
    • Mutagenesis of the yellow fever virus NS2B protein: Effects on proteolytic processing, NS2B-NS3 complex formation, and viral replication
    • Chambers, T. J., A. Nestorowicz, S. M. Amberg, and C. M. Rice. 1993. Mutagenesis of the yellow fever virus NS2B protein: effects on proteolytic processing, NS2B-NS3 complex formation, and viral replication. J. Virol. 67: 6797-6807.
    • (1993) J. Virol. , vol.67 , pp. 6797-6807
    • Chambers, T.J.1    Nestorowicz, A.2    Amberg, S.M.3    Rice, C.M.4
  • 9
    • 0025309446 scopus 로고
    • Production of yellow fever virus 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 virus 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
  • 10
    • 0025201350 scopus 로고
    • Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein
    • Chambers, T. J., R. C. Weir, A. Grakoui, D. W. McCourt, J. F. Bazan, R. J. Fletterick, and C. M. Rice. 1990. Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein. Proc. Natl. Acad. Sci. USA 87:8898-8902.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8898-8902
    • Chambers, T.J.1    Weir, R.C.2    Grakoui, A.3    McCourt, D.W.4    Bazan, J.F.5    Fletterick, R.J.6    Rice, C.M.7
  • 11
    • 0024553952 scopus 로고
    • Proper processing of dengue virus nonstructural glycoprotein NS1 requires the N-terminal hydrophobic signal sequence and the downstream nonstructural protein NS2a
    • Falgout, B., R. Chanock, and C.-J. Lai. 1989. Proper processing of dengue virus nonstructural glycoprotein NS1 requires the N-terminal hydrophobic signal sequence and the downstream nonstructural protein NS2a. J. Virol. 63:1852-1860.
    • (1989) J. Virol. , vol.63 , pp. 1852-1860
    • Falgout, B.1    Chanock, R.2    Lai, C.-J.3
  • 12
    • 0025864149 scopus 로고
    • Both nonstructural protein NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins
    • Falgout, B., M. Pethel, Y.-M. Zhang, and C.-J. Lai. 1991. Both nonstructural protein NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins. J. Virol. 65:2467-2475.
    • (1991) J. Virol. , vol.65 , pp. 2467-2475
    • Falgout, B.1    Pethel, M.2    Zhang, Y.-M.3    Lai, C.-J.4
  • 13
    • 0027499688 scopus 로고
    • Deletion analysis of dengue virus type 4 nonstructural protein NS2B: Identification of a domain required for NS2B-NS3 proteinase activity
    • Falgout, B., R. H. Miller, and C.-J. Lai. 1993. Deletion analysis of dengue virus type 4 nonstructural protein NS2B: identification of a domain required for NS2B-NS3 proteinase activity. J. Virol. 67:2034-2042.
    • (1993) J. Virol. , vol.67 , pp. 2034-2042
    • Falgout, B.1    Miller, R.H.2    Lai, C.-J.3
  • 14
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes 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 synthesizes 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
  • 15
    • 0024341494 scopus 로고
    • N-terminal domains of putative helicases of flavi- and pestiviruses may be serine proteases
    • Gorbalenya, A. E., A. P. Donchenko, E. V. Koonin, and V. M. Blinov. 1989. N-terminal domains of putative helicases of flavi-and pestiviruses may be serine proteases. Nucleic Acids Res. 17:3889-3897.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 3889-3897
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Koonin, E.V.3    Blinov, V.M.4
  • 16
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • Gorbalenya, A. E., E. V. Koonin, A. P. Donchenko, and V. M. Blinov. 1989. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 17:4713-4729.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4713-4729
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 17
    • 0028944286 scopus 로고
    • Processing of Japanese encephalitis virus non-structural proteins: NS2B-NS3 complex and heterologous proteases
    • Jan, L. R., C. S. Yang, D. W. Trent, B. Falgout, and C. J. Lai. 1995. Processing of Japanese encephalitis virus non-structural proteins: NS2B-NS3 complex and heterologous proteases. J. Gen. Virol. 76:573-580.
    • (1995) J. Gen. Virol. , vol.76 , pp. 573-580
    • Jan, L.R.1    Yang, C.S.2    Trent, D.W.3    Falgout, B.4    Lai, C.J.5
  • 18
    • 0020475449 scopus 로고
    • A method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 19
    • 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
  • 20
    • 0023028190 scopus 로고
    • The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain
    • Maddon, P. J., A. G. Dalgleish, J. S. McDougal, P. R. Clapham, R. A. Weiss, and R. Axel. 1986. The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain. Cell 47:333-348.
    • (1986) Cell , vol.47 , pp. 333-348
    • Maddon, P.J.1    Dalgleish, A.G.2    McDougal, J.S.3    Clapham, P.R.4    Weiss, R.A.5    Axel, R.6
  • 22
    • 0024340607 scopus 로고
    • In vitro processing of dengue virus structural proteins: Cleavage of the pre-membrane protein
    • Markoff, L. 1989. In vitro processing of dengue virus structural proteins: cleavage of the pre-membrane protein. J. Virol. 63:3345-3352.
    • (1989) J. Virol. , vol.63 , pp. 3345-3352
    • Markoff, L.1
  • 23
    • 0026097661 scopus 로고
    • Japanese encephalitis virus-vaccinia recombinants produce particulate forms of the structural membrane proteins and induce high levels of protection against lethal JEV infection
    • Mason, P. W., S. Pincus, M. J. Fournier, T. L. Mason, R. E. Shope, and E. Paoletti. 1991. Japanese encephalitis virus-vaccinia recombinants produce particulate forms of the structural membrane proteins and induce high levels of protection against lethal JEV infection. Virology 180:294-305.
    • (1991) Virology , vol.180 , pp. 294-305
    • Mason, P.W.1    Pincus, S.2    Fournier, M.J.3    Mason, T.L.4    Shope, R.E.5    Paoletti, E.6
  • 24
    • 0028206422 scopus 로고
    • Mutagenesis of the yellow fever virus NS2A/2B cleavage site: Effects on proteolytic processing, viral replication and evidence for alternative processing of the NS2A protein
    • Nestorowicz, A., T. J. Chambers, and C. M. Rice. 1994. Mutagenesis of the yellow fever virus NS2A/2B cleavage site: effects on proteolytic processing, viral replication and evidence for alternative processing of the NS2A protein. Virology 199:114-123.
    • (1994) Virology , vol.199 , pp. 114-123
    • Nestorowicz, A.1    Chambers, T.J.2    Rice, C.M.3
  • 25
    • 0024592786 scopus 로고
    • Analyses of the terminal sequences of West Nile virus structural proteins and of the in vitro translation of these proteins allow the proposal of a complete scheme of the proteolytic cleavages involved in their synthesis
    • Nowak, T., P. M. Farber, G. Wengler, and G. Wengler. 1989. Analyses of the terminal sequences of West Nile virus structural proteins and of the in vitro translation of these proteins allow the proposal of a complete scheme of the proteolytic cleavages involved in their synthesis. Virology 169:365-376.
    • (1989) Virology , vol.169 , pp. 365-376
    • Nowak, T.1    Farber, P.M.2    Wengler, G.3    Wengler, G.4
  • 26
    • 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. Despres, 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    Despres, P.3    Girard, M.4    Bouloy, M.5
  • 27
    • 0002315081 scopus 로고
    • Chemical and antigenic structure of flaviviruses
    • R. W. Schlesinger (ed.), Academic Press, Inc., New York, N.Y.
    • Russell, P. K., W. E. Brandt, and J. M. Dalrymple. 1980. Chemical and antigenic structure of flaviviruses, p. 503-529. In R. W. Schlesinger (ed.), The togaviruses. Academic Press, Inc., New York, N.Y.
    • (1980) The Togaviruses , pp. 503-529
    • Russell, P.K.1    Brandt, W.E.2    Dalrymple, J.M.3
  • 28
    • 0023836729 scopus 로고
    • Gene mapping and positive identification of the nonstructural proteins NS2A, NS2B, NS3, NS4B, and NS5 of the flavivirus Kunjin and their cleavage sites
    • Speight, G., G. Coia, M. D. Parker, and E. G. Westaway. 1988. Gene mapping and positive identification of the nonstructural proteins NS2A, NS2B, NS3, NS4B, and NS5 of the flavivirus Kunjin and their cleavage sites. J. Gen. Virol. 69:23-34.
    • (1988) J. Gen. Virol. , vol.69 , pp. 23-34
    • Speight, G.1    Coia, G.2    Parker, M.D.3    Westaway, E.G.4
  • 29
    • 0008876748 scopus 로고
    • Studies on nature of dengue viruses. 1. Correlation of particle density, infectivity, and RNA content of type 2 virus
    • Stevens, T. M., and R. W. Schlesinger. 1965. Studies on nature of dengue viruses. 1. Correlation of particle density, infectivity, and RNA content of type 2 virus. Virology 27:103-112.
    • (1965) Virology , vol.27 , pp. 103-112
    • Stevens, T.M.1    Schlesinger, R.W.2
  • 30
    • 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
  • 32
    • 0025865788 scopus 로고
    • In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active center of the protease which cleaves the viral polyprotein after multiple basic amino acids
    • Wengler, G., G. Czaya, P. M. Farber, and J. H. Hegemann. 1991. In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active center of the protease which cleaves the viral polyprotein after multiple basic amino acids. J. Gen. Virol. 72:851-858.
    • (1991) J. Gen. Virol. , vol.72 , pp. 851-858
    • Wengler, G.1    Czaya, G.2    Farber, P.M.3    Hegemann, J.H.4
  • 33
    • 0024370410 scopus 로고
    • Definition of the carboxy termini of the three glycoproteins specified by dengue virus type 2
    • Wright, P. S., M. R. Cauchi, and M. L. Ng. 1989. Definition of the carboxy termini of the three glycoproteins specified by dengue virus type 2. Virology 171:61-67.
    • (1989) Virology , vol.171 , pp. 61-67
    • Wright, P.S.1    Cauchi, M.R.2    Ng, M.L.3
  • 34
    • 0027308196 scopus 로고
    • Regulation of late events in flavivirus polyprotein processing and maturation
    • Yamshchikov, V. F., and R. W. Compans. 1993. Regulation of late events in flavivirus polyprotein processing and maturation. Virology 192:38-51.
    • (1993) Virology , vol.192 , pp. 38-51
    • Yamshchikov, V.F.1    Compans, R.W.2
  • 35
    • 0027971433 scopus 로고
    • Generation of long flavivirus expression cassettes by in vivo recombination and transient dominant selection
    • Yamshchikov, V. F., and R. W. Compans. 1994. Generation of long flavivirus expression cassettes by in vivo recombination and transient dominant selection. Gene 149:193-201.
    • (1994) Gene , vol.149 , pp. 193-201
    • Yamshchikov, V.F.1    Compans, R.W.2
  • 36
    • 0028146784 scopus 로고
    • Processing of the intracellular form of the West Nile virus capsid protein by the viral NS2B-NS3 protease: An in vitro study
    • Yamshchikov, V. F., and R. W. Compans. 1994. Processing of the intracellular form of the West Nile virus capsid protein by the viral NS2B-NS3 protease: an in vitro study. J. Virol. 68:5765-5771.
    • (1994) J. Virol. , vol.68 , pp. 5765-5771
    • Yamshchikov, V.F.1    Compans, R.W.2
  • 37
    • 0028916051 scopus 로고
    • Formation of the flavivirus envelope: Role of the viral NS2B-NS3 protease
    • Yamshchikov, V. F., and R. W. Compans. 1995. Formation of the flavivirus envelope: role of the viral NS2B-NS3 protease. J. Virol. 69:1995-2003.
    • (1995) J. Virol. , vol.69 , pp. 1995-2003
    • Yamshchikov, V.F.1    Compans, R.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.