메뉴 건너뛰기




Volumn 77, Issue 13, 2003, Pages 7376-7382

Identification of the murine coronavirus MP1 cleavage site recognized by papain-like proteinase 2

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; BCR ABL PROTEIN; GLYCINE; MEMBRANE PROTEIN; PAPAIN LIKE PROTEINASE 1; PAPAIN LIKE PROTEINASE 2; PHENYLALANINE; PROTEINASE; RNA DIRECTED RNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 0037791748     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.13.7376-7382.2003     Document Type: Article
Times cited : (28)

References (43)
  • 2
    • 0036646055 scopus 로고    scopus 로고
    • Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain
    • Anand, K., G. J. Palm, J. R. Mesters, S. G. Siddell, J. Ziebuhr, and R. Hilgenfeld. 2002. Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain. EMBO J. 21:3213-3224.
    • (2002) EMBO J. , vol.21 , pp. 3213-3224
    • Anand, K.1    Palm, G.J.2    Mesters, J.R.3    Siddell, S.G.4    Ziebuhr, J.5    Hilgenfeld, R.6
  • 3
    • 0024405242 scopus 로고
    • Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein
    • Baker, S. C., C. K. Shieh, L. H. Soe, M. F. Chang, D. M. Vannier, and M. M. Lai. 1989. Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein. J. Virol. 63:3693-3699.
    • (1989) J. Virol. , vol.63 , pp. 3693-3699
    • Baker, S.C.1    Shieh, C.K.2    Soe, L.H.3    Chang, M.F.4    Vannier, D.M.5    Lai, M.M.6
  • 4
    • 0027170410 scopus 로고
    • Identification of the catalytic sites of a papainlike cysteine proteinase of murine coronavirus
    • Baker, S. C., K. Yokomori, S. Dong, R. Carlisle, A. E. Gorbalenya, E. V. Koonin, and M. M. Lai. 1993. Identification of the catalytic sites of a papainlike cysteine proteinase of murine coronavirus. J. Virol. 67:6056-6063.
    • (1993) J. Virol. , vol.67 , pp. 6056-6063
    • Baker, S.C.1    Yokomori, K.2    Dong, S.3    Carlisle, R.4    Gorbalenya, A.E.5    Koonin, E.V.6    Lai, M.M.7
  • 6
    • 0028241850 scopus 로고
    • Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains
    • Bonilla, P. J., A. E. Gorbalenya, and S. R. Weiss. 1994. Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: heterogeneity among MHV strains. Virology 198:736-740.
    • (1994) Virology , vol.198 , pp. 736-740
    • Bonilla, P.J.1    Gorbalenya, A.E.2    Weiss, S.R.3
  • 7
    • 0031028291 scopus 로고    scopus 로고
    • Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59
    • Bonilla, P. J., S. A. Hughes, and S. R. Weiss. 1997. Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59. J. Virol. 71:900-909.
    • (1997) J. Virol. , vol.71 , pp. 900-909
    • Bonilla, P.J.1    Hughes, S.A.2    Weiss, S.R.3
  • 8
    • 0023512767 scopus 로고
    • An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV
    • Brierley, I., M. E. Boursnell, M. M. Binns, B. Bilimoria, V. C. Blok, T. D. Brown, and S. C. Inglis. 1987. An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV. EMBO J. 6:3779-3785.
    • (1987) EMBO J. , vol.6 , pp. 3779-3785
    • Brierley, I.1    Boursnell, M.E.2    Binns, M.M.3    Bilimoria, B.4    Blok, V.C.5    Brown, T.D.6    Inglis, S.C.7
  • 9
    • 0035194291 scopus 로고    scopus 로고
    • Reverse genetics system for the avian coronavirus infectious bronchitis virus
    • Casals, R., V. Thiel, S. G. Siddell, D. Cavanagh, and P. Britton. 2001. Reverse genetics system for the avian coronavirus infectious bronchitis virus. J. Virol. 75:12359-12369.
    • (2001) J. Virol. , vol.75 , pp. 12359-12369
    • Casals, R.1    Thiel, V.2    Siddell, S.G.3    Cavanagh, D.4    Britton, P.5
  • 10
    • 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
  • 11
    • 1542563379 scopus 로고    scopus 로고
    • Update: Outbreak of severe acute respiratory syndrome - Worldwide, 2003
    • Centers for Disease Control and Prevention. 2003. Update: outbreak of severe acute respiratory syndrome - worldwide, 2003. Morb. Mortal. Wkly. Rep. 52:241-246.
    • (2003) Morb. Mortal. Wkly. Rep. , vol.52 , pp. 241-246
  • 12
    • 0027995476 scopus 로고
    • Determinants of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus
    • Dong, S., and S. C. Baker. 1994. Determinants of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus. Virology 204:541-549.
    • (1994) Virology , vol.204 , pp. 541-549
    • Dong, S.1    Baker, S.C.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
    • 0029948532 scopus 로고    scopus 로고
    • Murine coronavirus membrane fusion is blocked by modification of thiols buried within the spike protein
    • Gallagher, T. M. 1996. Murine coronavirus membrane fusion is blocked by modification of thiols buried within the spike protein. J. Virol. 70:4683-4690.
    • (1996) J. Virol. , vol.70 , pp. 4683-4690
    • Gallagher, T.M.1
  • 15
    • 0025739985 scopus 로고
    • Putative papainrelated thiol proteases of positive-strand RNA viruses. Identification of rubiand aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha- and coronaviruses
    • Gorbalenya, A. E., E. V. Koonin, and M. M. Lai. 1991. Putative papainrelated thiol proteases of positive-strand RNA viruses. Identification of rubiand aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha- and coronaviruses. FEBS Lett. 288:201-205.
    • (1991) FEBS Lett. , vol.288 , pp. 201-205
    • Gorbalenya, A.E.1    Koonin, E.V.2    Lai, M.M.3
  • 16
    • 0036196634 scopus 로고    scopus 로고
    • RNA replication of mouse hepatitis virus takes place at double-membrane vesicles
    • Gosert, R., A. Kanjanahaluethai, D. Egger, K. Bienz, and S. C. Baker. 2002. RNA replication of mouse hepatitis virus takes place at double-membrane vesicles. J. Virol. 76:3697-3708.
    • (2002) J. Virol. , vol.76 , pp. 3697-3708
    • Gosert, R.1    Kanjanahaluethai, A.2    Egger, D.3    Bienz, K.4    Baker, S.C.5
  • 17
    • 0031907557 scopus 로고    scopus 로고
    • Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: Identification of a papain-like proteinase and its substrate
    • Herold, J., A. E. Gorbalenya, V. Thiel, B. Schelle, and S. G. Siddell. 1998. Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: identification of a papain-like proteinase and its substrate. J. Virol. 72:910-918.
    • (1998) J. Virol. , vol.72 , pp. 910-918
    • Herold, J.1    Gorbalenya, A.E.2    Thiel, V.3    Schelle, B.4    Siddell, S.G.5
  • 18
    • 0033591345 scopus 로고    scopus 로고
    • 2+-binding finger connecting the two domains of a papain-like fold
    • 2+-binding finger connecting the two domains of a papain-like fold. J. Biol. Chem. 274:14918-14925.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14918-14925
    • Herold, J.1    Siddell, S.G.2    Gorbalenya, A.E.3
  • 19
    • 0002257116 scopus 로고    scopus 로고
    • Coronaviruses
    • D. M. Knipe and P. M. Howley (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Holmes, K. V. 2001. Coronaviruses, p. 1187-1203. In D. M. Knipe and P. M. Howley (ed.), Fields virology, vol. 1. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology , vol.1 , pp. 1187-1203
    • Holmes, K.V.1
  • 20
    • 0028813105 scopus 로고
    • Identification of the murine coronavirus p28 cleavage site
    • Hughes, S. A., P. J. Bonilla, and S. R. Weiss. 1995. Identification of the murine coronavirus p28 cleavage site. J. Virol. 69:809-813.
    • (1995) J. Virol. , vol.69 , pp. 809-813
    • Hughes, S.A.1    Bonilla, P.J.2    Weiss, S.R.3
  • 21
    • 0033882187 scopus 로고    scopus 로고
    • Identification of mouse hepatitis virus papain-like proteinase 2 activity
    • Kanjanahaluethai, A., and S. C. Baker. 2000. Identification of mouse hepatitis virus papain-like proteinase 2 activity. J. Virol. 74:7911-7921.
    • (2000) J. Virol. , vol.74 , pp. 7911-7921
    • Kanjanahaluethai, A.1    Baker, S.C.2
  • 22
    • 0030633479 scopus 로고    scopus 로고
    • The molecular biology of coronaviruses
    • Lai, M. M., and D. Cavanagh. 1997. The molecular biology of coronaviruses. Adv. Virus Res. 48:1-100.
    • (1997) Adv. Virus Res. , vol.48 , pp. 1-100
    • Lai, M.M.1    Cavanagh, D.2
  • 23
    • 0038639970 scopus 로고    scopus 로고
    • Coronaviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howley (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa.
    • Lai, M. M. C., and K. V. Holmes. 2001. Coronaviridae: the viruses and their replication, p. 1163-1185. In D. M. Knipe and P. M. Howley (ed.), Fields Virology, vol. 1. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology , vol.1 , pp. 1163-1185
    • Lai, M.M.C.1    Holmes, K.V.2
  • 24
    • 0026074776 scopus 로고
    • The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase
    • Lee, H. J., C. K. Shieh, A. E. Gorbalenya, E. V. Koonin, N. La Monica, J. Tuler, A. Bagdzhadzhyan, and M. M. Lai. 1991. The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase. Virology 180:567-582.
    • (1991) Virology , vol.180 , pp. 567-582
    • Lee, H.J.1    Shieh, C.K.2    Gorbalenya, A.E.3    Koonin, E.V.4    La Monica, N.5    Tuler, J.6    Bagdzhadzhyan, A.7    Lai, M.M.8
  • 25
    • 0032486388 scopus 로고    scopus 로고
    • Characterization of the two overlapping papain-like proteinase domains encoded in gene 1 of the coronavirus infectious bronchitis virus and determination of the C-terminal cleavage site of an 87-kDa protein
    • Lim, K. P., and D. X. Liu. 1998. Characterization of the two overlapping papain-like proteinase domains encoded in gene 1 of the coronavirus infectious bronchitis virus and determination of the C-terminal cleavage site of an 87-kDa protein. Virology 245:303-312.
    • (1998) Virology , vol.245 , pp. 303-312
    • Lim, K.P.1    Liu, D.X.2
  • 26
    • 0033947165 scopus 로고    scopus 로고
    • Identification of a novel cleavage activity of the first papain-like proteinase domain encoded by open reading frame la of the coronavirus avian infectious bronchitis virus and characterization of the cleavage products
    • Lim, K. P., L. F. Ng, and D. X. Liu. 2000. Identification of a novel cleavage activity of the first papain-like proteinase domain encoded by open reading frame la of the coronavirus avian infectious bronchitis virus and characterization of the cleavage products. J. Virol. 74:1674-1685.
    • (2000) J. Virol. , vol.74 , pp. 1674-1685
    • Lim, K.P.1    Ng, L.F.2    Liu, D.X.3
  • 27
    • 0030586696 scopus 로고    scopus 로고
    • Intracellular and in vitro-translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59
    • Lu, X., Y. Lu, and M. R. Denison. 1996. Intracellular and in vitro-translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59. Virology 222:375-382.
    • (1996) Virology , vol.222 , pp. 375-382
    • Lu, X.1    Lu, Y.2    Denison, M.R.3
  • 28
    • 0242280088 scopus 로고    scopus 로고
    • Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton protein from the open reading frame 1a polyprotein in virus-infected cells and in vitro
    • Lu, X. T., A. C. Sims, and M. R. Denison. 1998. Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton protein from the open reading frame 1a polyprotein in virus-infected cells and in vitro. J. Virol. 72:2265-2271.
    • (1998) J. Virol. , vol.72 , pp. 2265-2271
    • Lu, X.T.1    Sims, A.C.2    Denison, M.R.3
  • 29
    • 0030988810 scopus 로고    scopus 로고
    • Determinants of mouse hepatitis virus 3C-like proteinase activity
    • Lu, Y., and M. R. Denison. 1997. Determinants of mouse hepatitis virus 3C-like proteinase activity. Virology 230:335-342.
    • (1997) Virology , vol.230 , pp. 335-342
    • Lu, Y.1    Denison, M.R.2
  • 30
    • 0029063624 scopus 로고
    • Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59
    • Lu, Y., X. Lu, and M. R. Denison. 1995. Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59. J. Virol. 69:3554-3559.
    • (1995) J. Virol. , vol.69 , pp. 3554-3559
    • Lu, Y.1    Lu, X.2    Denison, M.R.3
  • 31
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262:10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 32
    • 0033017866 scopus 로고    scopus 로고
    • Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex
    • Pedersen, K. W., Y. van der Meer, N. Roos, and E. J. Snijder. 1999. Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex. J. Virol. 73:2016-2026.
    • (1999) J. Virol. , vol.73 , pp. 2016-2026
    • Pedersen, K.W.1    Van der Meer, Y.2    Roos, N.3    Snijder, E.J.4
  • 33
    • 18244432238 scopus 로고    scopus 로고
    • Efficient autoproteolytic processing of the MHV-A59 3C-like proteinase from the flanking hydrophobic domains requires membranes
    • Pinon, J. D., R. R. Mayreddy, J. D. Turner, F. S. Khan, P. J. Bonilla, and S. R. Weiss. 1997. Efficient autoproteolytic processing of the MHV-A59 3C-like proteinase from the flanking hydrophobic domains requires membranes. Virology 230:309-322.
    • (1997) Virology , vol.230 , pp. 309-322
    • Pinon, J.D.1    Mayreddy, R.R.2    Turner, J.D.3    Khan, F.S.4    Bonilla, P.J.5    Weiss, S.R.6
  • 34
    • 0344994525 scopus 로고    scopus 로고
    • Further requirements for cleavage by the murine coronavirus 3C-like proteinase: Identification of a cleavage site within ORF1b
    • Pinon, J. D., H. Teng, and S. R. Weiss. 1999. Further requirements for cleavage by the murine coronavirus 3C-like proteinase: identification of a cleavage site within ORF1b. Virology 263:471-484.
    • (1999) Virology , vol.263 , pp. 471-484
    • Pinon, J.D.1    Teng, H.2    Weiss, S.R.3
  • 36
    • 0032520567 scopus 로고    scopus 로고
    • Processing of the coronavirus MHV-JHM polymerase polyprotein: Identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a
    • Schiller, J. J., A. Kanjanahaluethai, and S. C. Baker. 1998. Processing of the coronavirus MHV-JHM polymerase polyprotein: identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a. Virology 242:288-302.
    • (1998) Virology , vol.242 , pp. 288-302
    • Schiller, J.J.1    Kanjanahaluethai, A.2    Baker, S.C.3
  • 37
    • 0032989122 scopus 로고    scopus 로고
    • Colocalization and membrane association of murine hepatitis virus gene 1 products and de novo-synthesized viral RNA in infected cells
    • Shi, S. T., J. J. Schiller, A. Kanjanahjaluethai, S. C. Baker, J. W. Oh, and M. M. Lai. 1999. Colocalization and membrane association of murine hepatitis virus gene 1 products and de novo-synthesized viral RNA in infected cells. J. Virol. 73:5957-5969.
    • (1999) J. Virol. , vol.73 , pp. 5957-5969
    • Shi, S.T.1    Schiller, J.J.2    Kanjanahjaluethai, A.3    Baker, S.C.4    Oh, J.W.5    Lai, M.M.6
  • 38
    • 0031925071 scopus 로고    scopus 로고
    • The molecular biology of arteriviruses
    • Snijder, E. J., and J. J. Meulenberg. 1998. The molecular biology of arteriviruses. J. Gen. Virol. 79:961-979.
    • (1998) J. Gen. Virol. , vol.79 , pp. 961-979
    • Snijder, E.J.1    Meulenberg, J.J.2
  • 39
    • 0034969913 scopus 로고    scopus 로고
    • Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus
    • Thiel, V., J. Herold, B. Schelle, and S. G. Siddell. 2001. Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus. J. Gen. Virol. 82:1273-1281.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1273-1281
    • Thiel, V.1    Herold, J.2    Schelle, B.3    Siddell, S.G.4
  • 40
    • 0033762254 scopus 로고    scopus 로고
    • Strategy for systematic assembly of large RNA and DNA genomes: Transmissible gastroenteritis virus model
    • Yount, B., K. M. Curtis, and R. S. Baric. 2000. Strategy for systematic assembly of large RNA and DNA genomes: transmissible gastroenteritis virus model. J. Virol. 74:10600-10611.
    • (2000) J. Virol. , vol.74 , pp. 10600-10611
    • Yount, B.1    Curtis, K.M.2    Baric, R.S.3
  • 41
    • 0036838992 scopus 로고    scopus 로고
    • Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59
    • Yount, B., M. R. Denison, S. R. Weiss, and R. S. Baric. 2002. Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59. J. Virol. 76:11065-11078.
    • (2002) J. Virol. , vol.76 , pp. 11065-11078
    • Yount, B.1    Denison, M.R.2    Weiss, S.R.3    Baric, R.S.4
  • 42
    • 0034072633 scopus 로고    scopus 로고
    • Virus-encoded proteinases and proteolytic processing in the Nidovirales
    • Ziebuhr, J., E. J. Snijder, and A. E. Gorbalenya. 2000. Virus-encoded proteinases and proteolytic processing in the Nidovirales. J. Gen. Virol. 81:853-879.
    • (2000) J. Gen. Virol. , vol.81 , pp. 853-879
    • Ziebuhr, J.1    Snijder, E.J.2    Gorbalenya, A.E.3
  • 43
    • 0035980126 scopus 로고    scopus 로고
    • The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond
    • Ziebuhr, J., V. Thiel, and A. E. Gorbalenya. 2001. The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond. J. Biol. Chem. 276:33220-33232.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33220-33232
    • Ziebuhr, J.1    Thiel, V.2    Gorbalenya, A.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.