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Volumn 72, Issue 12, 1998, Pages 9865-9872

BiP (GRP78) and endoplasmin (GRP94) are induced following rotavirus infection and bind transiently to an endoplasmic reticulum-localized virion component

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; MESSENGER RNA; VIRUS GLYCOPROTEIN;

EID: 0031797727     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.12.9865-9872.1998     Document Type: Article
Times cited : (77)

References (39)
  • 1
    • 0024446502 scopus 로고
    • Receptor activity of rotavirus nonstructural glycoprotein NS28
    • Au, K.-S., W.-K. Chan, J. W. Burns, and M. K. Estes. 1989. Receptor activity of rotavirus nonstructural glycoprotein NS28. J. Virol. 63:4553-4562.
    • (1989) J. Virol. , vol.63 , pp. 4553-4562
    • Au, K.-S.1    Chan, W.-K.2    Burns, J.W.3    Estes, M.K.4
  • 2
    • 0029972477 scopus 로고    scopus 로고
    • Age-dependent diarrhea induced by a rotaviral nonstructural glycoprotein
    • Ball, J. M., P. Tian, C. W-Y. Zeng, A. P. Morris, and M. K. Estes. 1996. Age-dependent diarrhea induced by a rotaviral nonstructural glycoprotein. Science 272:101-104.
    • (1996) Science , vol.272 , pp. 101-104
    • Ball, J.M.1    Tian, P.2    Zeng, C.W.-Y.3    Morris, A.P.4    Estes, M.K.5
  • 3
    • 0024426841 scopus 로고
    • Topology of the non-structural rotavirus receptor glycoprotein NS28 in the rough endoplasmic reticulum
    • Bergmann, C. C., D. Maass, M. K. Poruchynsky, P. H. Atkinson, and A. R. Bellamy. 1989. Topology of the non-structural rotavirus receptor glycoprotein NS28 in the rough endoplasmic reticulum. EMBO J. 8:1695-1703.
    • (1989) EMBO J. , vol.8 , pp. 1695-1703
    • Bergmann, C.C.1    Maass, D.2    Poruchynsky, M.K.3    Atkinson, P.H.4    Bellamy, A.R.5
  • 4
    • 0031060310 scopus 로고    scopus 로고
    • Serine protein kinase activity associated with rotavirus phosphoprotein NSP5
    • Blackhall, J., A. Fuentes, K. Hansen, and G. Magnusson. 1997. Serine protein kinase activity associated with rotavirus phosphoprotein NSP5. J. Virol. 71:138-144.
    • (1997) J. Virol. , vol.71 , pp. 138-144
    • Blackhall, J.1    Fuentes, A.2    Hansen, K.3    Magnusson, G.4
  • 5
    • 0020612963 scopus 로고
    • Coding assignment and nucleotide sequence of simian rotavirus SA11 gene segment 10: Location of glycosylation sites suggests that the signal peptide is not cleaved
    • Both, G. W., L. J. Siegman, A. R. Bellamy, and P. H. Atkinson. 1983. Coding assignment and nucleotide sequence of simian rotavirus SA11 gene segment 10: location of glycosylation sites suggests that the signal peptide is not cleaved. J. Virol. 48:335-339.
    • (1983) J. Virol. , vol.48 , pp. 335-339
    • Both, G.W.1    Siegman, L.J.2    Bellamy, A.R.3    Atkinson, P.H.4
  • 6
    • 0019486841 scopus 로고
    • Bovine rotavirus interactions: Effect of virus infection on cellular integrity and macromolecular synthesis
    • Carpio, M. M., L. A. Babiuk, V. Misra, and R. M. Blumenthal. 1981. Bovine rotavirus interactions: effect of virus infection on cellular integrity and macromolecular synthesis. Virology 114:86-97.
    • (1981) Virology , vol.114 , pp. 86-97
    • Carpio, M.M.1    Babiuk, L.A.2    Misra, V.3    Blumenthal, R.M.4
  • 7
    • 0023936331 scopus 로고
    • Topography of the simian rotavirus nonstructural glycoprotein (NS28) in the endoplasmic reticulum membrane
    • Chan, W. K., K. S. Au, and M. K. Estes. 1988. Topography of the simian rotavirus nonstructural glycoprotein (NS28) in the endoplasmic reticulum membrane. Virology 164:435-442.
    • (1988) Virology , vol.164 , pp. 435-442
    • Chan, W.K.1    Au, K.S.2    Estes, M.K.3
  • 8
    • 0039797301 scopus 로고
    • Cap-independent translation of mRNA conferred by encephalomyocarditis virus 5′ sequence improves the performance of the vaccinia virus/bacteriophage T7 hybrid expression system
    • Elroy-Stein, O. T., T. Fuerst, and B. Moss. 1989. Cap-independent translation of mRNA conferred by encephalomyocarditis virus 5′ sequence improves the performance of the vaccinia virus/bacteriophage T7 hybrid expression system. Proc. Natl. Acad. Sci. USA 86:6126-6130.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6126-6130
    • Elroy-Stein, O.T.1    Fuerst, T.2    Moss, B.3
  • 10
    • 0020036971 scopus 로고
    • Identification, synthesis, and modifications of simian rotavirus SA11 polypeptides in infected cells
    • Ericson, B. L., D. Y. Graham, B. B. Mason, and M. K. Estes. 1982. Identification, synthesis, and modifications of simian rotavirus SA11 polypeptides in infected cells. J. Virol. 42:825-839.
    • (1982) J. Virol. , vol.42 , pp. 825-839
    • Ericson, B.L.1    Graham, D.Y.2    Mason, B.B.3    Estes, M.K.4
  • 11
    • 0000730162 scopus 로고
    • Rotaviruses and their replication
    • B. N. Fields, D. Knipe, P. M. Howley, et al. (ed.), Lippincott-Raven Publishers, Philadelphia, Pa.
    • Estes, M. K. 1995. Rotaviruses and their replication, p. 731-761. In B. N. Fields, D. Knipe, P. M. Howley, et al. (ed.), Fields virology, 3rd ed. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1995) Fields Virology, 3rd Ed. , pp. 731-761
    • Estes, M.K.1
  • 12
    • 0023373687 scopus 로고
    • Use of a hybrid vaccinia virus-T7 RNA polymerase system for expression of target genes
    • Fuerst, T. R., P. L. Earl, and B. Moss. 1987. Use of a hybrid vaccinia virus-T7 RNA polymerase system for expression of target genes. Mol. Cell. Biol. 7: 2538-2544.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2538-2544
    • Fuerst, T.R.1    Earl, P.L.2    Moss, B.3
  • 13
    • 0026803306 scopus 로고
    • Vaccinia virus infection induces a stress response that leads to association of Hsp70 with viral proteins
    • Jindal, S., and R. A. Young. 1992. Vaccinia virus infection induces a stress response that leads to association of Hsp70 with viral proteins. J. Virol. 66: 5357-5362.
    • (1992) J. Virol. , vol.66 , pp. 5357-5362
    • Jindal, S.1    Young, R.A.2
  • 14
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose regulated proteins
    • Kozutsumi, Y. M., M. Segal, K. Normington, M.-J. Gething, and J. Sambrook. 1988. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose regulated proteins. Nature (London) 332:462-464.
    • (1988) Nature (London) , vol.332 , pp. 462-464
    • Kozutsumi, Y.M.1    Segal, M.2    Normington, K.3    Gething, M.-J.4    Sambrook, J.5
  • 15
    • 0019823683 scopus 로고
    • Highly conserved glucose-regulated-protein in hamster and chicken cells: Preliminary characterization of its cDNA clone
    • Lee, A. S., A. Delegeane, and D. Scharf. 1981. Highly conserved glucose-regulated-protein in hamster and chicken cells: preliminary characterization of its cDNA clone. Proc. Natl. Acad. Sci. USA 78:4922-4925.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4922-4925
    • Lee, A.S.1    Delegeane, A.2    Scharf, D.3
  • 18
    • 0027958873 scopus 로고
    • The glucose regulated proteins (GRP 78 and GRP94): Function, gene regulation and applications
    • Little, E., M. Ramakrishnan, B. Roy, G. Gazit, and A. S. Lee. 1994. The glucose regulated proteins (GRP 78 and GRP94): function, gene regulation and applications. Crit. Rev. Eukaryot. Gene Expr. 4:1-18.
    • (1994) Crit. Rev. Eukaryot. Gene Expr. , vol.4 , pp. 1-18
    • Little, E.1    Ramakrishnan, M.2    Roy, B.3    Gazit, G.4    Lee, A.S.5
  • 19
    • 0025313861 scopus 로고
    • Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum
    • Lodish, H. F., and N. Kong. 1990. Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum. J. Biol. Chem. 265:10893-10899.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10893-10899
    • Lodish, H.F.1    Kong, N.2
  • 20
    • 3643107355 scopus 로고
    • Heavy chain binding protein recognizes incompletely disulphide-bonded forms of vesicular stomatitis virus G protein
    • Machamer, C. E., R. W. Doms, D. G. Bole, A. Helenius, and J. K. Rose. 1990. Heavy chain binding protein recognizes incompletely disulphide-bonded forms of vesicular stomatitis virus G protein. J. Biol. Chem 263:2107-2110.
    • (1990) J. Biol. Chem , vol.263 , pp. 2107-2110
    • Machamer, C.E.1    Doms, R.W.2    Bole, D.G.3    Helenius, A.4    Rose, J.K.5
  • 21
    • 0031040806 scopus 로고    scopus 로고
    • Mouse lymphoma cells destined to undergo apoptosis in response to thapsigargin treatment fail to generate a calcium-mediated grp78/grp94 stress response
    • McCormick, T. S., K. S. McColl, and C. W. Distelhorst. 1997. Mouse lymphoma cells destined to undergo apoptosis in response to thapsigargin treatment fail to generate a calcium-mediated grp78/grp94 stress response. J. Biol. Chem. 272:6087-6092.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6087-6092
    • McCormick, T.S.1    McColl, K.S.2    Distelhorst, C.W.3
  • 22
    • 0019402022 scopus 로고
    • Molecular biology of rotaviruses. I. Characterization of basic growth parameters and pattern of macromolecular synthesis
    • McCrae, M. A., and G. P. Faulkener-Valle. 1981. Molecular biology of rotaviruses. I. Characterization of basic growth parameters and pattern of macromolecular synthesis. J. Virol. 39:490-496.
    • (1981) J. Virol. , vol.39 , pp. 490-496
    • McCrae, M.A.1    Faulkener-Valle, G.P.2
  • 23
    • 0024375382 scopus 로고
    • Interaction of rotavirus cores with the nonstructural glycoprotein NS28
    • Meyer, J. C., C. C. Bergmann, and A. R. Bellamy. 1989. Interaction of rotavirus cores with the nonstructural glycoprotein NS28. Virology 171:98-107.
    • (1989) Virology , vol.171 , pp. 98-107
    • Meyer, J.C.1    Bergmann, C.C.2    Bellamy, A.R.3
  • 24
    • 0029063636 scopus 로고
    • Selective depletion of calcium by thapsigargin blocks rotavirus maturation but not the cytopathic effect
    • Michelangeli, F., F. Liprandi, M. E. Chemello, M. Ciarlet, and M.-C. Ruiz. 1995. Selective depletion of calcium by thapsigargin blocks rotavirus maturation but not the cytopathic effect. J. Virol. 69:3838-3847.
    • (1995) J. Virol. , vol.69 , pp. 3838-3847
    • Michelangeli, F.1    Liprandi, F.2    Chemello, M.E.3    Ciarlet, M.4    Ruiz, M.-C.5
  • 25
    • 0025754838 scopus 로고
    • Effect of rotavirus infection on intracellular calcium homeostasis in cultured cells
    • Michelangeli, F., M.-C. Ruiz, J. R. del Castillo, J. E. Ludert, and F. Liprandi. 1991. Effect of rotavirus infection on intracellular calcium homeostasis in cultured cells. Virology 181:520-527.
    • (1991) Virology , vol.181 , pp. 520-527
    • Michelangeli, F.1    Ruiz, M.-C.2    Del Castillo, J.R.3    Ludert, J.E.4    Liprandi, F.5
  • 26
    • 0031979773 scopus 로고    scopus 로고
    • Carbohydrates facilitate correct disulfide bond formation and folding of rotavirus VP7
    • Mirazimi, A., and L. Svensson. 1998. Carbohydrates facilitate correct disulfide bond formation and folding of rotavirus VP7. J. Virol. 72:3887-3892.
    • (1998) J. Virol. , vol.72 , pp. 3887-3892
    • Mirazimi, A.1    Svensson, L.2
  • 27
    • 3643075145 scopus 로고
    • A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the ER
    • Navarro, D., I. Quadri, and L. Pereira. 1991. A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the ER. Virology 180:135-143.
    • (1991) Virology , vol.180 , pp. 135-143
    • Navarro, D.1    Quadri, I.2    Pereira, L.3
  • 28
    • 0030774239 scopus 로고    scopus 로고
    • Rotavirus nonstructural glycoprotein NSP4 alters plasma membrane permeability in mammalian cells
    • Newton, K., J. C. Meyer, A. R. Bellamy, and J. A. Taylor. 1997. Rotavirus nonstructural glycoprotein NSP4 alters plasma membrane permeability in mammalian cells. J. Virol. 71:9458-9465.
    • (1997) J. Virol. , vol.71 , pp. 9458-9465
    • Newton, K.1    Meyer, J.C.2    Bellamy, A.R.3    Taylor, J.A.4
  • 29
    • 0018234882 scopus 로고
    • Infection with paramyxoviruses stimulates synthesis of cellular polypeptides that are also stimulated in cells transformed by Rous sarcoma virus or deprived of glucose
    • Peluso, R. W., R. A. Lamb, and P. W. Choppin. 1978. Infection with paramyxoviruses stimulates synthesis of cellular polypeptides that are also stimulated in cells transformed by Rous sarcoma virus or deprived of glucose. Proc. Natl. Acad. Sci. USA 75:6120-6124.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 6120-6124
    • Peluso, R.W.1    Lamb, R.A.2    Choppin, P.W.3
  • 30
    • 0025913093 scopus 로고
    • Calcium depletion blocks the maturation of rotavirus by altering the oligomerization of virus-encoded proteins in the ER
    • Poruchynsky, M. S., D. R. Maass, and P. H. Atkinson. 1991. Calcium depletion blocks the maturation of rotavirus by altering the oligomerization of virus-encoded proteins in the ER. J. Cell Biol. 114:651-661.
    • (1991) J. Cell Biol. , vol.114 , pp. 651-661
    • Poruchynsky, M.S.1    Maass, D.R.2    Atkinson, P.H.3
  • 31
    • 0028999264 scopus 로고
    • Conformation-defective herpes simplex virus 1 glycoprotein B activates the promoter of the grp94 gene that codes for a 94 kDa stress protein in the endoplasmic reticulum
    • Ramakrishnan, M., S. Tugizov, L. Pereira, and A. S. Lee. 1995. Conformation-defective herpes simplex virus 1 glycoprotein B activates the promoter of the grp94 gene that codes for a 94 kDa stress protein in the endoplasmic reticulum. DNA Cell Biol. 14:373-384.
    • (1995) DNA Cell Biol. , vol.14 , pp. 373-384
    • Ramakrishnan, M.1    Tugizov, S.2    Pereira, L.3    Lee, A.S.4
  • 32
    • 0021945545 scopus 로고
    • Calcium ionophore A23187 induces expression of glucose-regulated genes and their heterologous fusion genes
    • Resendez, E., Jr., J. W. Attenello, A. Grafsky, C. S. Chang, and A. S. Lee. 1985. Calcium ionophore A23187 induces expression of glucose-regulated genes and their heterologous fusion genes. Mol. Cell. Biol. 5:1212-1219.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1212-1219
    • Resendez Jr., E.1    Attenello, J.W.2    Grafsky, A.3    Chang, C.S.4    Lee, A.S.5
  • 33
    • 0020564083 scopus 로고
    • Vaccinia virus induces cellular mRNA degradation
    • Rice, A. P., and B. E. Roberts. 1983. Vaccinia virus induces cellular mRNA degradation. J. Virol. 47:529-539.
    • (1983) J. Virol. , vol.47 , pp. 529-539
    • Rice, A.P.1    Roberts, B.E.2
  • 34
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one or two gel electrophoresis
    • Rosenfield, T., J. Capedevielle, J. Guillemot, and P. Ferrara. 1992. In-gel digestion of proteins for internal sequence analysis after one or two gel electrophoresis. Anal. Biochem. 203:173-179.
    • (1992) Anal. Biochem. , vol.203 , pp. 173-179
    • Rosenfield, T.1    Capedevielle, J.2    Guillemot, J.3    Ferrara, P.4
  • 35
    • 0019991062 scopus 로고
    • Sequence diversity of human rotavirus strains investigated by Northern blot hybridization analysis
    • Street, J. E., M. C. Croxson, W. F. Chadderton, and A. R. Bellamy. 1982. Sequence diversity of human rotavirus strains investigated by Northern blot hybridization analysis. J. Virol. 43:369-378.
    • (1982) J. Virol. , vol.43 , pp. 369-378
    • Street, J.E.1    Croxson, M.C.2    Chadderton, W.F.3    Bellamy, A.R.4
  • 36
    • 0029796011 scopus 로고    scopus 로고
    • The rotavirus nonstructural glycoprotein NSP4 possesses membrane destabilization activity
    • Tian, P., J. M. Ball, C. Q. Y. Zeng, and M. K. Estes. 1996. The rotavirus nonstructural glycoprotein NSP4 possesses membrane destabilization activity. J. Virol. 70:6973-6981.
    • (1996) J. Virol. , vol.70 , pp. 6973-6981
    • Tian, P.1    Ball, J.M.2    Zeng, C.Q.Y.3    Estes, M.K.4
  • 37
    • 0028049103 scopus 로고
    • The nonstructural glycoprotein of rotavirus affects intracellular calcium levels
    • Tian, P., Y. Hu, W. P. Schilling, D. A. Lindsay, J. Eiden, and M. K. Estes. 1994. The nonstructural glycoprotein of rotavirus affects intracellular calcium levels. J. Virol. 68:251-257.
    • (1994) J. Virol. , vol.68 , pp. 251-257
    • Tian, P.1    Hu, Y.2    Schilling, W.P.3    Lindsay, D.A.4    Eiden, J.5    Estes, M.K.6
  • 39
    • 0025866240 scopus 로고
    • Flux of the paramyxovirus hemagglutinin-neuraminidase glycoprotein through the endoplasmic reticulum activates transcription of the GRP78-BiP gene
    • Watowich, S. S., R. I. Moromoto, and R. A. Lamb. 1992. Flux of the paramyxovirus hemagglutinin-neuraminidase glycoprotein through the endoplasmic reticulum activates transcription of the GRP78-BiP gene. J. Virol. 65:3590-3597.
    • (1992) J. Virol. , vol.65 , pp. 3590-3597
    • Watowich, S.S.1    Moromoto, R.I.2    Lamb, R.A.3


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