메뉴 건너뛰기




Volumn 86, Issue 5, 2005, Pages 1403-1413

Yellow fever virus NS2B-NS3 protease: Characterization of charged-to-alanine mutant and revertant viruses and analysis of polyprotein-cleavage activities

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; POLYPROTEIN; PROTEINASE; STRUCTURAL PROTEIN; VIRUS RNA;

EID: 18144425100     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.80427-0     Document Type: Article
Times cited : (29)

References (38)
  • 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., Nestorowicz, A., McCourt, D. W. & Rice, C. M. (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., Preugschat, F. & Strauss, J. H. (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.H.3
  • 3
    • 0024372153 scopus 로고
    • Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses
    • Bazan, J. F. & Fletterick, R. J. (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
    • 0032930982 scopus 로고    scopus 로고
    • Homology model of the dengue 2 virus NS3 protease: Putative interactions with both substrate and NS2B cofactor
    • Brinkworth, R. I., Fairlie, D. P., Leung, D. & Young, P. R. (1999). Homology model of the dengue 2 virus NS3 protease: putative interactions with both substrate and NS2B cofactor. J Gen Virol 80, 1167-1177.
    • (1999) J. Gen. Virol. , vol.80 , pp. 1167-1177
    • Brinkworth, R.I.1    Fairlie, D.P.2    Leung, D.3    Young, P.R.4
  • 5
    • 0030589011 scopus 로고    scopus 로고
    • Enhancement of hepatitis C virus NS3 proteinase activity by association with NS4A-specific synthetic peptides: Identification of sequence and critical residues of NS4A for the cofactor activity
    • 10 other authors
    • Butkiewicz, N. J., Wendel, M., Zhang, R. & 10 other authors (1996). Enhancement of hepatitis C virus NS3 proteinase activity by association with NS4A-specific synthetic peptides: identification of sequence and critical residues of NS4A for the cofactor activity. Virology 225, 328-338.
    • (1996) Virology , vol.225 , pp. 328-338
    • Butkiewicz, N.J.1    Wendel, M.2    Zhang, R.3
  • 6
    • 0026540617 scopus 로고
    • Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease
    • Cahour, A., Falgout, B. & Lai, C.-J. (1992). Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease. J Virol 66, 1535-1542.
    • (1992) J. Virol. , vol.66 , pp. 1535-1542
    • Cahour, A.1    Falgout, B.2    Lai, C.-J.3
  • 7
    • 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., McCourt, D. W. & Rice, C. M. (1990a). 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
  • 8
    • 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., Weir, R. C., Grakoui, A., McCourt, D. W., Bazan, J. F., Fletterick, R. J. & Rice, C. M. (1990b). 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 U S A 87, 8898-8902.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , 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
  • 9
    • 0026039916 scopus 로고
    • Processing of the yellow fever virus nonstructural polyprotein: A catalytically active NS3 proteinase domain and NS2B are required for cleavages at dibasic sites
    • Chambers, T. J., Grakoui, A. & Rice, C. M. (1991). Processing of the 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
  • 10
    • 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., Nestorowicz, A., Amberg, S. M. & Rice, C. M. (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
  • 11
    • 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., Nestorowicz, A. & Rice, C. M. (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    Nestorowicz, A.2    Rice, C.M.3
  • 12
    • 0034734773 scopus 로고    scopus 로고
    • Yellow fever virus NS2B-NS3 protease: Charged-to-alanine mutagenesis and deletion analysis define regions important for protease complex formation and function
    • Droll, D. A., Krishna-Murthy, H. M. & Chambers, T. J. (2000). Yellow fever virus NS2B-NS3 protease: charged-to-alanine mutagenesis and deletion analysis define regions important for protease complex formation and function. Virology 275, 335-347.
    • (2000) Virology , vol.275 , pp. 335-347
    • Droll, D.A.1    Krishna-Murthy, H.M.2    Chambers, T.J.3
  • 13
    • 0028849770 scopus 로고
    • Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum
    • Falgout, B. & Markoff, L. (1995). Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound 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
  • 14
    • 0025864149 scopus 로고
    • Both non-structural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins
    • Falgout, B., Pethel, M., Zhang, Y. M. & Lai, C.-J. (1991). Both non-structural proteins 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
  • 15
    • 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., Miller, R. H. & Lai, C.-J. (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
  • 16
    • 0024341494 scopus 로고
    • N-terminal domains of putative helicases of flavi- and pesti-viruses may be serine proteases
    • Gorbalenya, A. E., Donchenko, A. P., Koonin, E. V. & Blinov, V. M. (1989). N-terminal domains of putative helicases of flavi- and pesti-viruses 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
  • 17
    • 0036232747 scopus 로고    scopus 로고
    • Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles
    • Kummerer, B. M. & Rice, C. M. (2002). Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles. J Virol 76, 4773-4784.
    • (2002) J. Virol. , vol.76 , pp. 4773-4784
    • Kummerer, B.M.1    Rice, C.M.2
  • 18
    • 0027475018 scopus 로고
    • Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 proteinase is a prerequisite for processing at the downstream 4A/4B signalase site
    • Lin, C., Amberg, S. M., Chambers, T. J. & Rice, C. M. (1993a). Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 proteinase 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
  • 19
    • 0027186129 scopus 로고
    • Mutagenesis of conserved residues at the yellow fever 3/4A and 4B/5 dibasic cleavage sites: Effects on cleavage efficiency and polyprotein processing
    • Lin, C., Chambers, T. J. & Rice, C. M. (1993b). Mutagenesis of conserved residues at the yellow fever 3/4A and 4B/5 dibasic cleavage sites: effects on cleavage efficiency and polyprotein processing. Virology 192, 596-604.
    • (1993) Virology , vol.192 , pp. 596-604
    • Lin, C.1    Chambers, T.J.2    Rice, C.M.3
  • 20
    • 0029074519 scopus 로고
    • A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro
    • Lin, C., Thomson, J. A. & Rice, C. M. (1995). A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro. J Virol 69, 4373-4380.
    • (1995) J. Virol. , vol.69 , pp. 4373-4380
    • Lin, C.1    Thomson, J.A.2    Rice, C.M.3
  • 21
    • 0000163169 scopus 로고    scopus 로고
    • Flaviviridae
    • 3rd edn, Edited by D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman & S. E. Straus. Philadelphia: Lippincott
    • Lindenbach, B. D. & Rice, C. M. (2001). Flaviviridae. In Fields Virology, 3rd edn, pp. 991-1041. Edited by D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman & S. E. Straus. Philadelphia: Lippincott.
    • (2001) Fields Virology , pp. 991-1041
    • Lindenbach, B.D.1    Rice, C.M.2
  • 22
    • 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
  • 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 U S A 90, 6218-6222.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 6218-6222
    • Lobigs, M.1
  • 24
    • 0032527418 scopus 로고    scopus 로고
    • The conformation of hepatitis C virus NS3 proteinase with and without NS4A: A structural basis for the activation of the enzyme by its cofactor
    • 7 other authors
    • Love, R. A., Parge, H. E., Wickersham, J. A. & 7 other authors (1998). The conformation of hepatitis C virus NS3 proteinase with and without NS4A: a structural basis for the activation of the enzyme by its cofactor. Clin Diagn Virol 19, 151-156.
    • (1998) Clin. Diagn. Virol. , vol.19 , pp. 151-156
    • Love, R.A.1    Parge, H.E.2    Wickersham, J.A.3
  • 25
    • 0034802008 scopus 로고    scopus 로고
    • Mutagenesis of the Dengue virus type 2 NS3 protein within and outside helicase motifs: Effects on enzyme activity and virus replication
    • Matusan, A. E., Pryor, M. J., Davidson, A. D. & Wright, P. J. (2001). Mutagenesis of the Dengue virus type 2 NS3 protein within and outside helicase motifs: effects on enzyme activity and virus replication. J Virol 75, 9633-9643.
    • (2001) J. Virol. , vol.75 , pp. 9633-9643
    • Matusan, A.E.1    Pryor, M.J.2    Davidson, A.D.3    Wright, P.J.4
  • 26
    • 0033605260 scopus 로고    scopus 로고
    • Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects
    • Murthy, H. K., Clum, S. & Padmanabhan, R. (1999). Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects. J Biol Chem 274, 5573-5580.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5573-5580
    • Murthy, H.K.1    Clum, S.2    Padmanabhan, R.3
  • 27
    • 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., Chambers, T. J. & Rice, C. M. (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
  • 28
    • 0026322815 scopus 로고
    • Processing of nonstructural proteins NS4A and NS4B of dengue 2 virus in vitro and in vivo
    • Preugschat, F. & Strauss, J. H. (1991). Processing of nonstructural proteins NS4A and NS4B of dengue 2 virus in vitro and in vivo. Virology 185, 689-697.
    • (1991) Virology , vol.185 , pp. 689-697
    • Preugschat, F.1    Strauss, J.H.2
  • 29
    • 0025033393 scopus 로고
    • In vitro processing of dengue 2 nonstructural proteins NS2A, NS2B, and NS3
    • Preugschat, F., Yao, C.-W. & Strauss, J. H. (1990). In vitro processing of dengue 2 nonstructural proteins NS2A, NS2B, and NS3. J Virol 64, 4364-4374.
    • (1990) J. Virol. , vol.64 , pp. 4364-4374
    • Preugschat, F.1    Yao, C.-W.2    Strauss, J.H.3
  • 30
    • 0024892209 scopus 로고
    • Transcription of infectious yellow fever virus RNA from full-length cDNA templates produced by in vitro ligation
    • Rice, C. M., Grakoui, A., Galler, R. & Chambers, T. J. (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
  • 31
    • 0029076837 scopus 로고
    • The N-terminal region of hepatitis C virus nonstructural protein 3 (NS3), is essential for stable complex formation with NS4A
    • Satoh, S., Tanji, Y., Hijikata, M., Kimura, K. & Shimotohno, K. (1995). The N-terminal region of hepatitis C virus nonstructural protein 3 (NS3), is essential for stable complex formation with NS4A. J Virol 69, 4255-4260.
    • (1995) J. Virol. , vol.69 , pp. 4255-4260
    • Satoh, S.1    Tanji, Y.2    Hijikata, M.3    Kimura, K.4    Shimotohno, K.5
  • 33
    • 0031020347 scopus 로고    scopus 로고
    • Internal proteolysis of the NS3 protein specified by dengue virus 2
    • Teo, K. F. & Wright, P. J. (1997). Internal proteolysis of the NS3 protein specified by dengue virus 2. J Gen Virol 78, 337-341.
    • (1997) J. Gen. Virol. , vol.78 , pp. 337-341
    • Teo, K.F.1    Wright, P.J.2
  • 34
    • 0025865788 scopus 로고
    • In vitro synthesis of West Nile virus proteins indicates that the amino terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acids
    • Wangler, G., Czaya, G., Farber, P. M. & Hegemann, J. H. (1991). In vitro synthesis of West Nile virus proteins indicates that the amino terminal segment of the NS3 protein contains the active centre 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
    • Wangler, G.1    Czaya, G.2    Farber, P.M.3    Hegemann, J.H.4
  • 35
    • 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. & Compans, R. W. (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
  • 36
    • 0028916051 scopus 로고
    • Formation of the flavivirus envelope: Role of the viral NS2B-NS3 protease
    • Yamshchikov, V. F. & Compans, R. W. (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
  • 37
    • 0034616194 scopus 로고    scopus 로고
    • Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro
    • Yusof, R., Clum, S., Wetzel, M., Murthy, K. H. M. & Padmanabhan, R. (2000). Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro. J Biol Chem 275, 9963-9969.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9963-9969
    • Yusof, R.1    Clum, S.2    Wetzel, M.3    Murthy, K.H.M.4    Padmanabhan, R.5
  • 38
    • 0026471347 scopus 로고
    • Processing and localization of Dengue virus type 2 polyprotein precursor NS3-NS4A-NS4B-NS5
    • Zhang, L., Mohan, P. M. & Padmanabhan, R. (1992). Processing and localization of Dengue virus type 2 polyprotein precursor NS3-NS4A-NS4B-NS5. J Virol 66, 7549-7554.
    • (1992) J. Virol. , vol.66 , pp. 7549-7554
    • Zhang, L.1    Mohan, P.M.2    Padmanabhan, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.