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Volumn 71, Issue 12, 1997, Pages 9313-9322

Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: Evidence that NSP2 acts as a cofactor for the NSP4 serine protease

Author keywords

[No Author keywords available]

Indexed keywords

RNA DIRECTED RNA POLYMERASE; SERINE PROTEINASE; VIRUS ENZYME;

EID: 0030856299     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.12.9313-9322.1997     Document Type: Article
Times cited : (108)

References (43)
  • 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. H. 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.H.3
  • 3
    • 0027421842 scopus 로고
    • Sindbis virus expression vectors: Packaging of RNA replacons by using defective helper RNAs
    • Bredenbeek, P. J., I. Frolov, C. M. Rice, and S. Schlesinger. 1993. Sindbis virus expression vectors: packaging of RNA replacons by using defective helper RNAs. J. Virol. 67:6439-6446.
    • (1993) J. Virol. , vol.67 , pp. 6439-6446
    • Bredenbeek, P.J.1    Frolov, I.2    Rice, C.M.3    Schlesinger, S.4
  • 4
    • 0030634897 scopus 로고    scopus 로고
    • Nidovirales: A new order comprising Coronaviridae and Arteriviridae
    • Cavanagh, D. 1997. Nidovirales: a new order comprising Coronaviridae and Arteriviridae. Arch. Virol. 142:629-633.
    • (1997) Arch. Virol. , vol.142 , pp. 629-633
    • Cavanagh, D.1
  • 5
    • 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
  • 6
    • 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., A. Nestorowicz, and C. M. Rice. 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
  • 7
    • 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
  • 8
    • 0029074522 scopus 로고
    • Processing and evolution of the N-terminal region of the arterivirus replicase ORF1a protein: Identification of two papainlike cysteine proteases
    • den Boon, J. A., K. S. Faaberg, J. J. M. Meulenberg, A. L. M. Wassenaar, P. G. W. Plagemann, A. E. Gorbalenya, and E. J. Snijder. 1995. Processing and evolution of the N-terminal region of the arterivirus replicase ORF1a protein: identification of two papainlike cysteine proteases. J. Virol. 69:4500-4505.
    • (1995) J. Virol. , vol.69 , pp. 4500-4505
    • Den Boon, J.A.1    Faaberg, K.S.2    Meulenberg, J.J.M.3    Wassenaar, A.L.M.4    Plagemann, P.G.W.5    Gorbalenya, A.E.6    Snijder, E.J.7
  • 11
    • 0002425455 scopus 로고
    • Isolation of a filterable agent causing arteritis of horses and abortion of mares. Its differentiation from the equine (abortion) influenza virus
    • Doll, E. R., J. T. Bryans, W. H. M. McCollum, and M. E. Wallace. 1957. Isolation of a filterable agent causing arteritis of horses and abortion of mares. Its differentiation from the equine (abortion) influenza virus. Cornell Vet. 47:3-41.
    • (1957) Cornell Vet. , vol.47 , pp. 3-41
    • Doll, E.R.1    Bryans, J.T.2    McCollum, W.H.M.3    Wallace, M.E.4
  • 12
    • 0027138172 scopus 로고
    • Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes
    • Dougherty, W. G., and B. L. Semler. 1993. Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes. Microbiol. Rev. 57:781-822.
    • (1993) Microbiol. Rev. , vol.57 , pp. 781-822
    • Dougherty, W.G.1    Semler, B.L.2
  • 13
    • 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
  • 14
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., A. L. Hubbard, S. Fowler, and P. B. Lazarow. 1982. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93:97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 15
    • 0027325337 scopus 로고
    • Complete genomic sequence and phylogenetic analysis of the lactate dehydrogenase-elevating virus (LDV)
    • Godeny, E. K., L. Chen, S. N. Kumar, S. L. Methven, E. V. Koonin, and M. A. Brinton. 1993. Complete genomic sequence and phylogenetic analysis of the lactate dehydrogenase-elevating virus (LDV). Virology 194:585-596.
    • (1993) Virology , vol.194 , pp. 585-596
    • Godeny, E.K.1    Chen, L.2    Kumar, S.N.3    Methven, S.L.4    Koonin, E.V.5    Brinton, M.A.6
  • 17
    • 0023758546 scopus 로고
    • A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation
    • Jang, S. K., H. G. Krausslich, M. J. Nicklin, G. M. Duke, A. C. Palmenberg, and E. Wimmer. 1988. A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation. J. Virol. 62:2636-2643.
    • (1988) J. Virol. , vol.62 , pp. 2636-2643
    • Jang, S.K.1    Krausslich, H.G.2    Nicklin, M.J.3    Duke, G.M.4    Palmenberg, A.C.5    Wimmer, E.6
  • 18
    • 0023952330 scopus 로고
    • Poliovirus protein 3CD is the active protease for processing of the precursor protein P1 in vitro
    • Jore, J., B. De Geus, R. J. Jackson, P. H. Pouwels, and B. E. Enger Valk. 1988. Poliovirus protein 3CD is the active protease for processing of the precursor protein P1 in vitro. J. Gen. Virol. 69:1627-1636.
    • (1988) J. Gen. Virol. , vol.69 , pp. 1627-1636
    • Jore, J.1    De Geus, B.2    Jackson, R.J.3    Pouwels, P.H.4    Enger Valk, B.E.5
  • 20
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt, O., H. P. Grunert, and U. Hahn. 1990. A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene 96:125-128.
    • (1990) Gene , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.P.2    Hahn, U.3
  • 21
    • 0026788162 scopus 로고
    • Alternate poliovirus nonstructural protein processing cascades generated by primary sites of 3C proteinase cleavage
    • Lawson, M. A., and B. L. Semler. 1992. Alternate poliovirus nonstructural protein processing cascades generated by primary sites of 3C proteinase cleavage. Virology 191:309-320.
    • (1992) Virology , vol.191 , pp. 309-320
    • Lawson, M.A.1    Semler, B.L.2
  • 22
    • 0027475009 scopus 로고
    • Roles of nonstructural polyproteins and cleavage products in regulating Sindbis virus RNA replication and transcription
    • Lemm, J. A., and C. M. Rice. 1993. Roles of nonstructural polyproteins and cleavage products in regulating Sindbis virus RNA replication and transcription. J. Virol. 67:1916-1926.
    • (1993) J. Virol. , vol.67 , pp. 1916-1926
    • Lemm, J.A.1    Rice, C.M.2
  • 23
    • 0027463085 scopus 로고
    • Assembly of functional Sindbis virus RNA replication complexes: Requirement for coexpression of p123 and p34
    • Lemm, J. A., and C. M. Rice. 1993. Assembly of functional Sindbis virus RNA replication complexes: requirement for coexpression of p123 and p34. J. Virol. 67:1905-1915.
    • (1993) J. Virol. , vol.67 , pp. 1905-1915
    • Lemm, J.A.1    Rice, C.M.2
  • 24
    • 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. Rumenapf, 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    Rumenapf, T.2    Strauss, E.G.3    Strauss, J.H.4    Rice, C.M.5
  • 27
    • 0029034168 scopus 로고
    • Sequence of the genome of lactate dehydrogenase-elevating virus: Heterogenicity between strains P and C
    • Palmer, G. A., L. Kuo, Z. Chen, K. S. Faaberg, and P. G. W. Plagemann. 1995. Sequence of the genome of lactate dehydrogenase-elevating virus: heterogenicity between strains P and C. Virology 209:637-642.
    • (1995) Virology , vol.209 , pp. 637-642
    • Palmer, G.A.1    Kuo, L.2    Chen, Z.3    Faaberg, K.S.4    Plagemann, P.G.W.5
  • 28
    • 0000100028 scopus 로고    scopus 로고
    • Lactate dehydrogenase-elevating virus and related viruses
    • B. N. Fields, P. M. Knipe, and P. M. Howley (ed.), Lippincott-Raven Publishers, Philadelphia, Pa.
    • Plagemann, P. G. W. 1996. Lactate dehydrogenase-elevating virus and related viruses, p. 1105-1120. In B. N. Fields, P. M. Knipe, and P. M. Howley (ed.), Fields virology. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1996) Fields Virology , pp. 1105-1120
    • Plagemann, P.G.W.1
  • 29
    • 0027979138 scopus 로고
    • Regulation of Sindbis virus RNA replication: Uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis
    • Shirako, Y., and J. H. Strauss. 1994. Regulation of Sindbis virus RNA replication: uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis. J. Virol. 68:1874-1885.
    • (1994) J. Virol. , vol.68 , pp. 1874-1885
    • Shirako, Y.1    Strauss, J.H.2
  • 31
    • 0002049970 scopus 로고
    • The coronaviruslike superfamily
    • S. G. Siddell (ed.), Plenum Press, New York, N.Y.
    • Snijder, E. J., and W. J. M. Spaan. 1995. The coronaviruslike superfamily, p. 239-255. In S. G. Siddell (ed.), The Coronaviridae. Plenum Press, New York, N.Y.
    • (1995) The Coronaviridae , pp. 239-255
    • Snijder, E.J.1    Spaan, W.J.M.2
  • 33
    • 0026475757 scopus 로고
    • The 5′ end of the equine arteritis virus replicase gene encodes a papainlike cysteine protease
    • Snijder, E. J., A. L. M. Wassenaar, and W. J. M. Spaan. 1992. The 5′ end of the equine arteritis virus replicase gene encodes a papainlike cysteine protease. J. Virol. 66:7040-7048.
    • (1992) J. Virol. , vol.66 , pp. 7040-7048
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.M.3
  • 34
    • 0028067318 scopus 로고
    • Proteolytic processing of the replicase ORF1a protein of equine arteritis virus
    • Snijder, E. J., A. L. M. Wassenaar, and W. J. M. Spaan. 1994. Proteolytic processing of the replicase ORF1a protein of equine arteritis virus. J. Virol. 68:5755-5764.
    • (1994) J. Virol. , vol.68 , pp. 5755-5764
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.M.3
  • 35
    • 0029044301 scopus 로고
    • The arterivirus nsp2 protease: An unusual cysteine protease with primary structure similarities to both papain-like and chymotrypsin-like proteases
    • Snijder, E. J., A. L. M. Wassenaar, W. J. M. Spaan, and A. E. Gorbalenya. 1995. The arterivirus nsp2 protease: an unusual cysteine protease with primary structure similarities to both papain-like and chymotrypsin-like proteases. J. Biol. Chem. 270:16671-16676.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16671-16676
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.M.3    Gorbalenya, A.E.4
  • 36
    • 0029966508 scopus 로고    scopus 로고
    • The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases
    • Snijder, E. J., A. L. M. Wassenaar, L. C. van Dinten, W. J. M. Spaan, and A. E. Gorbalenya. 1996. The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases. J. Biol. Chem. 271:4864-4871.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4864-4871
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Van Dinten, L.C.3    Spaan, W.J.M.4    Gorbalenya, A.E.5
  • 39
    • 0031017109 scopus 로고    scopus 로고
    • An infectious arterivirus cDNA clone: Identification of a replicase point mutation which abolishes discontinuous mRNa transcription
    • van Dinten, L. C., J. A. den Boon, A. L. M. Wassenaar, W. J. M. Spaan, and E. J. Snijder. 1997. An infectious arterivirus cDNA clone: identification of a replicase point mutation which abolishes discontinuous mRNA transcription. Proc. Natl. Acad. Sci. USA 94:991-996.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 991-996
    • Van Dinten, L.C.1    Den Boon, J.A.2    Wassenaar, A.L.M.3    Spaan, W.J.M.4    Snijder, E.J.5
  • 41
    • 0029844841 scopus 로고    scopus 로고
    • Processing of the equine arteritis virus replicase ORF1b protein: Identification of cleavage products containing the putative viral polymerase and helicase domains
    • van Dinten, L. C., A. L. M. Wassenaar, A. E. Gorbalenya, W. J. M. Spaan, and E. J. Snijder. 1996. Processing of the equine arteritis virus replicase ORF1b protein: identification of cleavage products containing the putative viral polymerase and helicase domains. J. Virol. 70:6625-6633.
    • (1996) J. Virol. , vol.70 , pp. 6625-6633
    • Van Dinten, L.C.1    Wassenaar, A.L.M.2    Gorbalenya, A.E.3    Spaan, W.J.M.4    Snijder, E.J.5
  • 42
    • 0028040383 scopus 로고
    • Alphavirus nsP3 functions to form replication complexes transcribing negative-strand RNA
    • Wang, Y.-F., Sawicki, S. G., and Sawicki, D. L. 1994. Alphavirus nsP3 functions to form replication complexes transcribing negative-strand RNA. J. Virol. 68:6466-6475.
    • (1994) J. Virol. , vol.68 , pp. 6466-6475
    • Wang, Y.-F.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 43
    • 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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