메뉴 건너뛰기




Volumn 375, Issue 1, 2008, Pages 118-129

Mutation in murine coronavirus replication protein nsp4 alters assembly of double membrane vesicles

Author keywords

Coronavirus; Double membrane vesicles; Nonstructural proteins; ts mutant

Indexed keywords

ALANINE; ASPARAGINE; NONSTRUCTURAL PROTEIN 3; NONSTRUCTURAL PROTEIN 4; THREONINE;

EID: 42749085841     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2008.01.018     Document Type: Article
Times cited : (75)

References (43)
  • 1
    • 0024405242 scopus 로고
    • Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein
    • Baker S.C., Shieh C.K., Soe L.H., Chang M.F., Vannier D.M., and Lai M.M. Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein. J. Virol. 63 9 (1989) 3693-3699
    • (1989) J. Virol. , vol.63 , Issue.9 , 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
  • 2
    • 42749086863 scopus 로고    scopus 로고
    • Cell biology of nidovirus replication complexes
    • Perlman S., Gallagher T., and Snijder E. (Eds), ASM Press, Washington
    • Baker S.C., and Denison M.R. Cell biology of nidovirus replication complexes. In: Perlman S., Gallagher T., and Snijder E. (Eds). Nidoviruses (2008), ASM Press, Washington 103-113
    • (2008) Nidoviruses , pp. 103-113
    • Baker, S.C.1    Denison, M.R.2
  • 3
    • 0025193363 scopus 로고
    • Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups
    • Baric R.S., Fu K., Schaad M.C., and Stohlman S.A. Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups. Virology 177 2 (1990) 646-656
    • (1990) Virology , vol.177 , Issue.2 , pp. 646-656
    • Baric, R.S.1    Fu, K.2    Schaad, M.C.3    Stohlman, S.A.4
  • 4
    • 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., Hughes S.A., and Weiss S.R. 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 2 (1997) 900-909
    • (1997) J. Virol. , vol.71 , Issue.2 , pp. 900-909
    • Bonilla, P.J.1    Hughes, S.A.2    Weiss, S.R.3
  • 5
    • 0034054288 scopus 로고    scopus 로고
    • Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly
    • Bost A.G., Carnahan R.H., Lu X.T., and Denison M.R. Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly. J. Virol. 74 7 (2000) 3379-3387
    • (2000) J. Virol. , vol.74 , Issue.7 , pp. 3379-3387
    • Bost, A.G.1    Carnahan, R.H.2    Lu, X.T.3    Denison, M.R.4
  • 6
    • 34648834060 scopus 로고    scopus 로고
    • Processing of open reading frame 1a replicase proteins nsp7 to nsp10 in murine hepatitis virus strain A59 replication
    • Deming D.J., Graham R.L., Denison M.R., and Baric R.S. Processing of open reading frame 1a replicase proteins nsp7 to nsp10 in murine hepatitis virus strain A59 replication. J. Virol. 81 19 (2007) 10280-10291
    • (2007) J. Virol. , vol.81 , Issue.19 , pp. 10280-10291
    • Deming, D.J.1    Graham, R.L.2    Denison, M.R.3    Baric, R.S.4
  • 7
    • 0028912686 scopus 로고
    • Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59
    • Denison M.R., Hughes S.A., and Weiss S.R. Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59. Virology 207 1 (1995) 316-320
    • (1995) Virology , vol.207 , Issue.1 , pp. 316-320
    • Denison, M.R.1    Hughes, S.A.2    Weiss, S.R.3
  • 8
    • 34250846350 scopus 로고    scopus 로고
    • Analysis of murine hepatitis virus strain A59 temperature-sensitive mutant TS-LA6 suggests that nsp10 plays a critical role in polyprotein processing
    • Donaldson E.F., Graham R.L., Sims A.C., Denison M.R., and Baric R.S. Analysis of murine hepatitis virus strain A59 temperature-sensitive mutant TS-LA6 suggests that nsp10 plays a critical role in polyprotein processing. J. Virol. 81 13 (2007) 7086-7098
    • (2007) J. Virol. , vol.81 , Issue.13 , pp. 7086-7098
    • Donaldson, E.F.1    Graham, R.L.2    Sims, A.C.3    Denison, M.R.4    Baric, R.S.5
  • 9
    • 0028143561 scopus 로고
    • Map locations of mouse hepatitis virus temperature-sensitive mutants: confirmation of variable rates of recombination
    • Fu K., and Baric R.S. Map locations of mouse hepatitis virus temperature-sensitive mutants: confirmation of variable rates of recombination. J. Virol. 68 11 (1994) 7458-7466
    • (1994) J. Virol. , vol.68 , Issue.11 , pp. 7458-7466
    • Fu, K.1    Baric, R.S.2
  • 10
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst T.R., Niles E.G., Studier F.W., and Moss B. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. U. S. A. 83 21 (1986) 8122-8126
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , Issue.21 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 12
    • 0036196634 scopus 로고    scopus 로고
    • RNA replication of mouse hepatitis virus takes place at double-membrane vesicles
    • Gosert R., Kanjanahaluethai A., Egger D., Bienz K., and Baker S.C. RNA replication of mouse hepatitis virus takes place at double-membrane vesicles. J. Virol. 76 8 (2002) 3697-3708
    • (2002) J. Virol. , vol.76 , Issue.8 , pp. 3697-3708
    • Gosert, R.1    Kanjanahaluethai, A.2    Egger, D.3    Bienz, K.4    Baker, S.C.5
  • 13
    • 33751252280 scopus 로고    scopus 로고
    • Replication of murine hepatitis virus is regulated by papain-like proteinase 1 processing of nonstructural proteins 1, 2, and 3
    • Graham R.L., and Denison M.R. Replication of murine hepatitis virus is regulated by papain-like proteinase 1 processing of nonstructural proteins 1, 2, and 3. J. Virol. 80 23 (2006) 11610-11620
    • (2006) J. Virol. , vol.80 , Issue.23 , pp. 11610-11620
    • Graham, R.L.1    Denison, M.R.2
  • 14
    • 10044268025 scopus 로고    scopus 로고
    • Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity
    • Harcourt B.H., Jukneliene D., Kanjanahaluethai A., Bechill J., Severson K.M., Smith C.M., Rota P.A., and Baker S.C. Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity. J. Virol. 78 24 (2004) 13600-13612
    • (2004) J. Virol. , vol.78 , Issue.24 , pp. 13600-13612
    • Harcourt, B.H.1    Jukneliene, D.2    Kanjanahaluethai, A.3    Bechill, J.4    Severson, K.M.5    Smith, C.M.6    Rota, P.A.7    Baker, S.C.8
  • 15
    • 0033882187 scopus 로고    scopus 로고
    • Identification of mouse hepatitis virus papain-like proteinase 2 activity
    • Kanjanahaluethai A., and Baker S.C. Identification of mouse hepatitis virus papain-like proteinase 2 activity. J. Virol. 74 17 (2000) 7911-7921
    • (2000) J. Virol. , vol.74 , Issue.17 , pp. 7911-7921
    • Kanjanahaluethai, A.1    Baker, S.C.2
  • 16
    • 0035699347 scopus 로고    scopus 로고
    • Processing of the replicase of murine coronavirus: papain-like proteinase 2 (PLP2) acts to generate p150 and p44
    • Kanjanahaluethai A., and Baker S.C. Processing of the replicase of murine coronavirus: papain-like proteinase 2 (PLP2) acts to generate p150 and p44. Adv. Exp. Med. Biol. 494 (2001) 267-273
    • (2001) Adv. Exp. Med. Biol. , vol.494 , pp. 267-273
    • Kanjanahaluethai, A.1    Baker, S.C.2
  • 17
    • 0037791748 scopus 로고    scopus 로고
    • Identification of the murine coronavirus MP1 cleavage site recognized by papain-like proteinase 2
    • Kanjanahaluethai A., Jukneliene D., and Baker S.C. Identification of the murine coronavirus MP1 cleavage site recognized by papain-like proteinase 2. J. Virol. 77 13 (2003) 7376-7382
    • (2003) J. Virol. , vol.77 , Issue.13 , pp. 7376-7382
    • Kanjanahaluethai, A.1    Jukneliene, D.2    Baker, S.C.3
  • 18
    • 34247163017 scopus 로고    scopus 로고
    • Membrane topology of murine coronavirus replicase nonstructural protein 3
    • Kanjanahaluethai A., Chen Z., Jukneliene D., and Baker S.C. Membrane topology of murine coronavirus replicase nonstructural protein 3. Virology 361 2 (2007) 391-401
    • (2007) Virology , vol.361 , Issue.2 , pp. 391-401
    • Kanjanahaluethai, A.1    Chen, Z.2    Jukneliene, D.3    Baker, S.C.4
  • 19
    • 34548679815 scopus 로고    scopus 로고
    • Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle
    • Kopek B.G., Perkins G., Miller D.J., Ellisman M.H., and Ahlquist P. Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle. PLoS Biol. 5 9 (2007) e220
    • (2007) PLoS Biol. , vol.5 , Issue.9
    • Kopek, B.G.1    Perkins, G.2    Miller, D.J.3    Ellisman, M.H.4    Ahlquist, P.5
  • 20
    • 0029063624 scopus 로고
    • Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59
    • Lu Y., Lu X., and Denison M.R. Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59. J. Virol. 69 6 (1995) 3554-3559
    • (1995) J. Virol. , vol.69 , Issue.6 , pp. 3554-3559
    • Lu, Y.1    Lu, X.2    Denison, M.R.3
  • 21
    • 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., Sims A.C., and Denison M.R. 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 3 (1998) 2265-2271
    • (1998) J. Virol. , vol.72 , Issue.3 , pp. 2265-2271
    • Lu, X.T.1    Sims, A.C.2    Denison, M.R.3
  • 22
    • 33746317830 scopus 로고    scopus 로고
    • The molecular biology of coronaviruses
    • Masters P.S. The molecular biology of coronaviruses. Adv. Virus Res. 66 (2006) 193-292
    • (2006) Adv. Virus Res. , vol.66 , pp. 193-292
    • Masters, P.S.1
  • 23
    • 0036776626 scopus 로고    scopus 로고
    • Flock house virus RNA polymerase is a transmembrane protein with amino-terminal sequences sufficient for mitochondrial localization and membrane insertion
    • Miller D.J., and Ahlquist P. Flock house virus RNA polymerase is a transmembrane protein with amino-terminal sequences sufficient for mitochondrial localization and membrane insertion. J. Virol. 76 19 (2002) 9856-9867
    • (2002) J. Virol. , vol.76 , Issue.19 , pp. 9856-9867
    • Miller, D.J.1    Ahlquist, P.2
  • 24
    • 0035169546 scopus 로고    scopus 로고
    • Flock house virus RNA replicates on outer mitochondrial membranes in Drosophila cells
    • Miller D.J., Schwartz M.D., and Ahlquist P. Flock house virus RNA replicates on outer mitochondrial membranes in Drosophila cells. J. Virol. 75 23 (2001) 11664-11676
    • (2001) J. Virol. , vol.75 , Issue.23 , pp. 11664-11676
    • Miller, D.J.1    Schwartz, M.D.2    Ahlquist, P.3
  • 25
    • 0242300174 scopus 로고    scopus 로고
    • Engineered retargeting of viral RNA replication complexes to an alternative intracellular membrane
    • Miller D.J., Schwartz M.D., Dye B.T., and Ahlquist P. Engineered retargeting of viral RNA replication complexes to an alternative intracellular membrane. J. Virol. 77 22 (2003) 12193-12202
    • (2003) J. Virol. , vol.77 , Issue.22 , pp. 12193-12202
    • Miller, D.J.1    Schwartz, M.D.2    Dye, B.T.3    Ahlquist, P.4
  • 26
    • 36049013168 scopus 로고    scopus 로고
    • Localization and membrane topology of the coronavirus nonstructural protein 4: involvement of the early secretory pathway in replication
    • Oostra M., Te Lintelo E.G., Deijs M., Verheije M.H., Rottier P.J., and de Haan C.A. Localization and membrane topology of the coronavirus nonstructural protein 4: involvement of the early secretory pathway in replication. J. Virol. 81 22 (2007) 12323-12336
    • (2007) J. Virol. , vol.81 , Issue.22 , pp. 12323-12336
    • Oostra, M.1    Te Lintelo, E.G.2    Deijs, M.3    Verheije, M.H.4    Rottier, P.J.5    de Haan, C.A.6
  • 27
    • 10944238037 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome
    • Peiris J.S., Guan Y., and Yuen K.Y. Severe acute respiratory syndrome. Nat. Med. 10 12 Suppl (2004) S88-S97
    • (2004) Nat. Med. , vol.10 , Issue.12 SUPPL
    • Peiris, J.S.1    Guan, Y.2    Yuen, K.Y.3
  • 28
    • 1642280930 scopus 로고    scopus 로고
    • Coronavirus replication complex formation utilizes components of cellular autophagy
    • Prentice E., Jerome W.G., Yoshimori T., Mizushima N., and Denison M.R. Coronavirus replication complex formation utilizes components of cellular autophagy. J. Biol. Chem. 279 11 (2004) 10136-10141
    • (2004) J. Biol. Chem. , vol.279 , Issue.11 , pp. 10136-10141
    • Prentice, E.1    Jerome, W.G.2    Yoshimori, T.3    Mizushima, N.4    Denison, M.R.5
  • 30
  • 32
    • 33845750075 scopus 로고    scopus 로고
    • A contemporary view of coronavirus transcription
    • Sawicki S.G., Sawicki D.L., and Siddell S.G. A contemporary view of coronavirus transcription. J. Virol. 81 1 (2007) 20-29
    • (2007) J. Virol. , vol.81 , Issue.1 , pp. 20-29
    • Sawicki, S.G.1    Sawicki, D.L.2    Siddell, S.G.3
  • 33
    • 0025374162 scopus 로고
    • Genetics of mouse hepatitis virus transcription: identification of cistrons which may function in positive and negative strand RNA synthesis
    • Schaad M.C., Stohlman S.A., Egbert J., Lum K., Fu K., Wei Jr. T., and Baric R.S. Genetics of mouse hepatitis virus transcription: identification of cistrons which may function in positive and negative strand RNA synthesis. Virology 177 2 (1990) 634-645
    • (1990) Virology , vol.177 , Issue.2 , pp. 634-645
    • Schaad, M.C.1    Stohlman, S.A.2    Egbert, J.3    Lum, K.4    Fu, K.5    Wei Jr., T.6    Baric, R.S.7
  • 34
    • 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., Kanjanahaluethai A., and Baker S.C. Processing of the coronavirus MHV-JHM polymerase polyprotein: identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a. Virology 242 2 (1998) 288-302
    • (1998) Virology , vol.242 , Issue.2 , pp. 288-302
    • Schiller, J.J.1    Kanjanahaluethai, A.2    Baker, S.C.3
  • 35
    • 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., Schiller J.J., Kanjanahaluethai A., Baker S.C., Oh J.W., and Lai M.M. Colocalization and membrane association of murine hepatitis virus gene 1 products and de novo-synthesized viral RNA in infected cells. J. Virol. 73 7 (1999) 5957-5969
    • (1999) J. Virol. , vol.73 , Issue.7 , pp. 5957-5969
    • Shi, S.T.1    Schiller, J.J.2    Kanjanahaluethai, A.3    Baker, S.C.4    Oh, J.W.5    Lai, M.M.6
  • 36
    • 0035703924 scopus 로고    scopus 로고
    • Identification of the mutations responsible for the phenotype of three MHV RNA-negative ts mutants
    • Siddell S., Sawicki D., Meyer Y., Thiel V., and Sawicki S. Identification of the mutations responsible for the phenotype of three MHV RNA-negative ts mutants. Adv. Exp. Med. Biol. 494 (2001) 453-458
    • (2001) Adv. Exp. Med. Biol. , vol.494 , pp. 453-458
    • Siddell, S.1    Sawicki, D.2    Meyer, Y.3    Thiel, V.4    Sawicki, S.5
  • 37
    • 33744928372 scopus 로고    scopus 로고
    • Ultrastructure and origin of membrane vesicles associated with the severe acute respiratory syndrome coronavirus replication complex
    • Snijder E.J., van der Meer Y., Zevenhoven-Dobbe J., Onderwater J.J., van der Meulen J., Koerten H.K., and Mommaas A.M. Ultrastructure and origin of membrane vesicles associated with the severe acute respiratory syndrome coronavirus replication complex. J. Virol. 80 12 (2006) 5927-5940
    • (2006) J. Virol. , vol.80 , Issue.12 , pp. 5927-5940
    • Snijder, E.J.1    van der Meer, Y.2    Zevenhoven-Dobbe, J.3    Onderwater, J.J.4    van der Meulen, J.5    Koerten, H.K.6    Mommaas, A.M.7
  • 38
    • 36048991887 scopus 로고    scopus 로고
    • Genetic analysis of murine hepatitis virus nsp4 in virus replication
    • Sparks J.S., Lu X., and Denison M.R. Genetic analysis of murine hepatitis virus nsp4 in virus replication. J. Virol. 81 22 (2007) 12554-12563
    • (2007) J. Virol. , vol.81 , Issue.22 , pp. 12554-12563
    • Sparks, J.S.1    Lu, X.2    Denison, M.R.3
  • 40
    • 0031754152 scopus 로고    scopus 로고
    • Negative strand RNA synthesis by temperature-sensitive mutants of mouse hepatitis virus
    • Younker D.R., and Sawicki S.G. Negative strand RNA synthesis by temperature-sensitive mutants of mouse hepatitis virus. Adv. Exp. Med. Biol. 440 (1998) 221-226
    • (1998) Adv. Exp. Med. Biol. , vol.440 , pp. 221-226
    • Younker, D.R.1    Sawicki, S.G.2
  • 41
    • 0036838992 scopus 로고    scopus 로고
    • Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59
    • Yount B., Denison M.R., Weiss S.R., and Baric R.S. Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59. J. Virol. 76 21 (2002) 11065-11078
    • (2002) J. Virol. , vol.76 , Issue.21 , pp. 11065-11078
    • Yount, B.1    Denison, M.R.2    Weiss, S.R.3    Baric, R.S.4
  • 42
    • 40849094932 scopus 로고    scopus 로고
    • The coronavirus replicase gene: special enzymes for special viruses
    • Thiel V. (Ed), Caister Academic Press
    • Ziebuhr J., and Snijder E.J. The coronavirus replicase gene: special enzymes for special viruses. In: Thiel V. (Ed). "Coronaviruses: Molecular and Cellular Biology" (2007), Caister Academic Press
    • (2007) "Coronaviruses: Molecular and Cellular Biology"
    • Ziebuhr, J.1    Snijder, E.J.2
  • 43
    • 0034072633 scopus 로고    scopus 로고
    • Virus-encoded proteinases and proteolytic processing in the Nidovirales
    • Ziebuhr J., Snijder E.J., and Gorbalenya A.E. Virus-encoded proteinases and proteolytic processing in the Nidovirales. J. Gen. Virol. 81 Pt 4 (2000) 853-879
    • (2000) J. Gen. Virol. , vol.81 , Issue.PART 4 , pp. 853-879
    • Ziebuhr, J.1    Snijder, E.J.2    Gorbalenya, A.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.