메뉴 건너뛰기




Volumn 80, Issue 14, 2006, Pages 6917-6925

Analyses of phosphorylation events in the Rubella virus capsid protein: Role in early replication events

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CAPSID PROTEIN; GENOMIC RNA; PHOSPHATE; SERINE; THREONINE;

EID: 33745784164     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01152-05     Document Type: Article
Times cited : (22)

References (41)
  • 1
    • 0038240823 scopus 로고    scopus 로고
    • Analysis of intermolecular RNA-RNA recombination by rubella virus
    • Adams, S. D., W. P. Tzeng, M. H. Chen, and T. K. Frey. 2003. Analysis of intermolecular RNA-RNA recombination by rubella virus. Virology 309:258-271.
    • (2003) Virology , vol.309 , pp. 258-271
    • Adams, S.D.1    Tzeng, W.P.2    Chen, M.H.3    Frey, T.K.4
  • 4
    • 0042317020 scopus 로고    scopus 로고
    • Active cAMP-dependent protein kinase incorporated within highly purified HIV-1 particles is required for viral infectivity and interacts with viral capsid protein
    • Cartier, C., B. Hemonnot, B. Gay, M. Bardy, C. Sanchiz, C. Devaux, and L. Briant. 2003. Active cAMP-dependent protein kinase incorporated within highly purified HIV-1 particles is required for viral infectivity and interacts with viral capsid protein. J. Biol. Chem. 278:35211-35219.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35211-35219
    • Cartier, C.1    Hemonnot, B.2    Gay, B.3    Bardy, M.4    Sanchiz, C.5    Devaux, C.6    Briant, L.7
  • 5
    • 0033516642 scopus 로고    scopus 로고
    • Identification of three major phosphorylation sites within HIV-1 capsid. Role of phosphorylation during the early steps of infection
    • Cartier, C., P. Sivard, C. Tranchat, D. Decimo, C. Desgranges, and V. Boyer. 1999. Identification of three major phosphorylation sites within HIV-1 capsid. Role of phosphorylation during the early steps of infection. J. Biol. Chem. 274:19434-19440.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19434-19440
    • Cartier, C.1    Sivard, P.2    Tranchat, C.3    Decimo, D.4    Desgranges, C.5    Boyer, V.6
  • 6
    • 0005289936 scopus 로고    scopus 로고
    • Rubella virus
    • D. M. Knipe, B. N. Fields, P. M. Howley, and D. E. Griffin (ed.). Lippincott Willams & Wilkins, Philadelphia, Pa.
    • Chantier, J. K., J. S. Wolinsky, and A. J. Tingle. 2001. Rubella virus, p. 963-990. In D. M. Knipe, B. N. Fields, P. M. Howley, and D. E. Griffin (ed.), Fields virology, 4th ed. Lippincott Willams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology, 4th Ed. , pp. 963-990
    • Chantier, J.K.1    Wolinsky, J.S.2    Tingle, A.J.3
  • 7
    • 0036827546 scopus 로고    scopus 로고
    • Mutation of capsid protein phosphorylation sites abolishes cauliflower mosaic virus infectivity
    • Chapdelaine, Y., D. Kirk, A. Karsies, T. Hohn, and D. Leclerc. 2002. Mutation of capsid protein phosphorylation sites abolishes cauliflower mosaic virus infectivity. J. Virol. 76:11748-11752.
    • (2002) J. Virol. , vol.76 , pp. 11748-11752
    • Chapdelaine, Y.1    Kirk, D.2    Karsies, A.3    Hohn, T.4    Leclerc, D.5
  • 8
    • 1842431531 scopus 로고    scopus 로고
    • Rubella virus capsid protein modulates viral genome replication and virus infectivity
    • Chen, M. H., and J. P. Icenogle. 2004. Rubella virus capsid protein modulates viral genome replication and virus infectivity. J. Virol. 78:4314-4322.
    • (2004) J. Virol. , vol.78 , pp. 4314-4322
    • Chen, M.H.1    Icenogle, J.P.2
  • 9
    • 0033775794 scopus 로고    scopus 로고
    • Structural phosphoprotein M2-1 of the human respiratory syncytial virus is an RNA binding protein
    • Cuesta, I., X. Geng, A. Asenjo, and N. Villanueva. 2000. Structural phosphoprotein M2-1 of the human respiratory syncytial virus is an RNA binding protein. J. Virol. 74:9858-9867.
    • (2000) J. Virol. , vol.74 , pp. 9858-9867
    • Cuesta, I.1    Geng, X.2    Asenjo, A.3    Villanueva, N.4
  • 10
    • 0036318795 scopus 로고    scopus 로고
    • Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein
    • Daub, H., S. Blencke, P. Habenberger, A. Kurtenbach, J. Dennenmoser, J. Wissing, A. Ullrich, and M. Cotten. 2002. Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein. J. Virol. 76:8124-8137.
    • (2002) J. Virol. , vol.76 , pp. 8124-8137
    • Daub, H.1    Blencke, S.2    Habenberger, P.3    Kurtenbach, A.4    Dennenmoser, J.5    Wissing, J.6    Ullrich, A.7    Cotten, M.8
  • 11
    • 0028028506 scopus 로고
    • Molecular biology of rubella virus
    • Frey, T. K. 1994. Molecular biology of rubella virus. Adv. Virus Res. 44:69-160.
    • (1994) Adv. Virus Res. , vol.44 , pp. 69-160
    • Frey, T.K.1
  • 12
    • 0032923868 scopus 로고    scopus 로고
    • Role of rubella virus glycoprotein domains in assembly of virus-like particles
    • Garbutt, M., L. M. Law, H. Chan, and T. C. Hobman. 1999. Role of rubella virus glycoprotein domains in assembly of virus-like particles. J. Virol. 73:3524-3533.
    • (1999) J. Virol. , vol.73 , pp. 3524-3533
    • Garbutt, M.1    Law, L.M.2    Chan, H.3    Hobman, T.C.4
  • 13
    • 0033999564 scopus 로고    scopus 로고
    • Core protein phosphorylation modulates pregenomic RNA encapsidation to different extents in human and duck hepatitis B viruses
    • Gazina, E. V., J. E. Fielding, B. Lin, and D. A. Anderson. 2000. Core protein phosphorylation modulates pregenomic RNA encapsidation to different extents in human and duck hepatitis B viruses. J. Virol. 74:4721-4728.
    • (2000) J. Virol. , vol.74 , pp. 4721-4728
    • Gazina, E.V.1    Fielding, J.E.2    Lin, B.3    Anderson, D.A.4
  • 14
    • 3543025697 scopus 로고    scopus 로고
    • The host cell MAP kinase ERK-2 regulates viral assembly and release by phosphorylating the p6gag protein of HIV-1
    • Hemonnot, B., C. Cartier, B. Gay, S. Rebuffat, M. Bardy, C. Devaux, V. Boyer, and L. Briant. 2004. The host cell MAP kinase ERK-2 regulates viral assembly and release by phosphorylating the p6gag protein of HIV-1. J. Biol. Chem. 279:32426-32434.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32426-32434
    • Hemonnot, B.1    Cartier, C.2    Gay, B.3    Rebuffat, S.4    Bardy, M.5    Devaux, C.6    Boyer, V.7    Briant, L.8
  • 15
    • 0023830657 scopus 로고
    • Time course of virus-specific macromolecular synthesis during rubella virus infection in Vero cells
    • Hemphill, M. L., R. Y. Forng, E. S. Abernathy, and T. K. Frey. 1988. Time course of virus-specific macromolecular synthesis during rubella virus infection in Vero cells. Virology 162:65-75.
    • (1988) Virology , vol.162 , pp. 65-75
    • Hemphill, M.L.1    Forng, R.Y.2    Abernathy, E.S.3    Frey, T.K.4
  • 16
    • 0035957981 scopus 로고    scopus 로고
    • Phosphorylation down-regulates the RNA binding function of the coat protein of potato virus A
    • Ivanov, K. I., P. Puustinen, A. Merits, M. Saarma, and K. Makinen. 2001. Phosphorylation down-regulates the RNA binding function of the coat protein of potato virus A. J. Biol. Chem. 276:13530-13540.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13530-13540
    • Ivanov, K.I.1    Puustinen, P.2    Merits, A.3    Saarma, M.4    Makinen, K.5
  • 17
    • 0028073177 scopus 로고
    • Effect of core protein phosphorylation by protein kinase C on encapsidation of RNA within core particles of hepatitis B virus
    • Kann, M., and W. H. Gerlich. 1994. Effect of core protein phosphorylation by protein kinase C on encapsidation of RNA within core particles of hepatitis B virus. J. Virol. 68:7993-8000.
    • (1994) J. Virol. , vol.68 , pp. 7993-8000
    • Kann, M.1    Gerlich, W.H.2
  • 18
    • 0033526096 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex
    • Kann, M., B. Sodeik, A. Vlachou, W. H. Gerlich, and A. Helenius. 1999. Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex. J. Cell Biol. 145:45-55.
    • (1999) J. Cell Biol. , vol.145 , pp. 45-55
    • Kann, M.1    Sodeik, B.2    Vlachou, A.3    Gerlich, W.H.4    Helenius, A.5
  • 19
    • 0042847320 scopus 로고    scopus 로고
    • Central role of a serine phosphorylation site within duck hepatitis B virus core protein for capsid trafficking and genome release
    • Kock, J., M. Kann, G. Putz, H. E. Blum, and F. Von Weizsacker. 2003. Central role of a serine phosphorylation site within duck hepatitis B virus core protein for capsid trafficking and genome release. J. Biol. Chem. 278:28123-28129.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28123-28129
    • Kock, J.1    Kann, M.2    Putz, G.3    Blum, H.E.4    Von Weizsacker, F.5
  • 20
    • 0033526794 scopus 로고    scopus 로고
    • Roles of the three major phosphorylation sites of hepatitis B virus core protein in viral replication
    • Lan, Y. T., J. Li, W. Liao, and J. Ou. 1999. Roles of the three major phosphorylation sites of hepatitis B virus core protein in viral replication. Virology 259:342-348.
    • (1999) Virology , vol.259 , pp. 342-348
    • Lan, Y.T.1    Li, J.2    Liao, W.3    Ou, J.4
  • 21
    • 0035132754 scopus 로고    scopus 로고
    • Rubella virus E2 signal peptide is required for perinuclear localization of capsid protein and virus assembly
    • Law, L. M. J., R. Duncan, A. Esmaili, H. L. Nakhasi, and T. C. Hobman. 2001. Rubella virus E2 signal peptide is required for perinuclear localization of capsid protein and virus assembly. J. Virol. 75:1978-1983.
    • (2001) J. Virol. , vol.75 , pp. 1978-1983
    • Law, L.M.J.1    Duncan, R.2    Esmaili, A.3    Nakhasi, H.L.4    Hobman, T.C.5
  • 22
    • 0037302253 scopus 로고    scopus 로고
    • Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication
    • Law, L. M. J., J. C. Everitt, M. D. Beatch, C. F. B. Holmes, and T. C. Hobman. 2003. Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication. J. Virol. 77:1764-1771.
    • (2003) J. Virol. , vol.77 , pp. 1764-1771
    • Law, L.M.J.1    Everitt, J.C.2    Beatch, M.D.3    Holmes, C.F.B.4    Hobman, T.C.5
  • 23
    • 0032889564 scopus 로고    scopus 로고
    • Nuclear targeting of the cauliflower mosaic virus coat protein
    • Leclerc, D., Y. Chapdelaine, and T. Hohn. 1999. Nuclear targeting of the cauliflower mosaic virus coat protein. J. Virol. 73:553-560.
    • (1999) J. Virol. , vol.73 , pp. 553-560
    • Leclerc, D.1    Chapdelaine, Y.2    Hohn, T.3
  • 24
    • 0029887660 scopus 로고    scopus 로고
    • Identification of domains in rubella virus genomic RNA and capsid protein necessary for specific interaction
    • Liu, Z., D. Yang, Z. Qiu, K.-T. Lim, P. Chong, and S. Gillam. 1996. Identification of domains in rubella virus genomic RNA and capsid protein necessary for specific interaction. J. Virol. 70:2184-2190.
    • (1996) J. Virol. , vol.70 , pp. 2184-2190
    • Liu, Z.1    Yang, D.2    Qiu, Z.3    Lim, K.-T.4    Chong, P.5    Gillam, S.6
  • 25
    • 0036385501 scopus 로고    scopus 로고
    • Phosphorylation of hepatitis C virus core protein by protein kinase a and protein kinase C
    • Lu, W., and J. H. Ou. 2002. Phosphorylation of hepatitis C virus core protein by protein kinase A and protein kinase C. Virology 300:20-30.
    • (2002) Virology , vol.300 , pp. 20-30
    • Lu, W.1    Ou, J.H.2
  • 26
    • 0034469913 scopus 로고    scopus 로고
    • Phosphorylation status of the parvovirus minute virus of mice particle: Mapping and biological relevance of the major phosphorylation sites
    • Maroto, B., J. C. Ramirez, and J. M. Almendral. 2000. Phosphorylation status of the parvovirus minute virus of mice particle: mapping and biological relevance of the major phosphorylation sites. J. Virol. 74:10892-10902.
    • (2000) J. Virol. , vol.74 , pp. 10892-10902
    • Maroto, B.1    Ramirez, J.C.2    Almendral, J.M.3
  • 27
    • 0028261083 scopus 로고
    • Expression of the rubella virus nonstructural protein ORF and demonstration of proteolytic processing
    • Marr, L. D., C. Y. Wang, and T. K. Frey. 1994. Expression of the rubella virus nonstructural protein ORF and demonstration of proteolytic processing. Virology 198:586-592.
    • (1994) Virology , vol.198 , pp. 586-592
    • Marr, L.D.1    Wang, C.Y.2    Frey, T.K.3
  • 28
    • 0025793856 scopus 로고
    • Endosomal association of a protein phosphatase with high dephosphorylating activity against a coronavirus nucleocapsid protein
    • Mohandas, D. V., and S. Dales. 1991. Endosomal association of a protein phosphatase with high dephosphorylating activity against a coronavirus nucleocapsid protein. FEBS Lett. 282:419-424.
    • (1991) FEBS Lett. , vol.282 , pp. 419-424
    • Mohandas, D.V.1    Dales, S.2
  • 29
    • 0003000404 scopus 로고
    • Togavirus morphology and morphogenesis
    • W. Schlesinger (ed.). Academic Press Inc., New York, N.Y.
    • Murphy, F. A. 1980. Togavirus morphology and morphogenesis, p. 241-326. In W. Schlesinger (ed.), The togaviruses. Academic Press Inc., New York, N.Y.
    • (1980) The Togaviruses , pp. 241-326
    • Murphy, F.A.1
  • 30
    • 0042692926 scopus 로고    scopus 로고
    • Nuclear import of hepatitis B virus capsids and release of the viral genome
    • Rabe, B., A. Vlachou, N. Pante, A. Helenius, and M. Kann. 2003. Nuclear import of hepatitis B virus capsids and release of the viral genome. Proc. Natl. Acad. Sci. USA 100:9849-9854.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9849-9854
    • Rabe, B.1    Vlachou, A.2    Pante, N.3    Helenius, A.4    Kann, M.5
  • 31
    • 0019505537 scopus 로고
    • Coronavirus JHM: A virion-associated protein kinase
    • Siddell, S. G., A. Barthel, and V. ter Meulen. 1981. Coronavirus JHM: a virion-associated protein kinase. J. Gen. Virol. 52:235-243.
    • (1981) J. Gen. Virol. , vol.52 , pp. 235-243
    • Siddell, S.G.1    Barthel, A.2    Ter Meulen, V.3
  • 32
    • 0025036502 scopus 로고
    • The E2 signal sequence of rubella virus remains part of the capsid protein and confers membrane association in vitro
    • Suomalainen, M., H. Garoff, and M. D. Baron. 1990. The E2 signal sequence of rubella virus remains part of the capsid protein and confers membrane association in vitro. J. Virol. 64:5500-5509.
    • (1990) J. Virol. , vol.64 , pp. 5500-5509
    • Suomalainen, M.1    Garoff, H.2    Baron, M.D.3
  • 33
    • 0016260030 scopus 로고
    • Virion-bound protein kinase in Semliki Forest and Sindbis viruses
    • Tan, K. B., and F. Sokol. 1974. Virion-bound protein kinase in Semliki Forest and Sindbis viruses. J. Virol. 13:1245-1253.
    • (1974) J. Virol. , vol.13 , pp. 1245-1253
    • Tan, K.B.1    Sokol, F.2
  • 34
    • 0041888255 scopus 로고    scopus 로고
    • Complementation of a deletion in the rubella virus p150 nonstructural protein by the viral capsid protein
    • Tzeng, W. P., and T. K. Frey. 2003. Complementation of a deletion in the rubella virus p150 nonstructural protein by the viral capsid protein. J. Virol. 77:9502-9510.
    • (2003) J. Virol. , vol.77 , pp. 9502-9510
    • Tzeng, W.P.1    Frey, T.K.2
  • 35
    • 0036120574 scopus 로고    scopus 로고
    • Mapping the rubella virus subgenomic promoter
    • Tzeng, W. P., and T. K. Frey. 2002. Mapping the rubella virus subgenomic promoter. J. Virol. 76:3189-3201.
    • (2002) J. Virol. , vol.76 , pp. 3189-3201
    • Tzeng, W.P.1    Frey, T.K.2
  • 36
    • 20444385101 scopus 로고    scopus 로고
    • Rubella virus capsid protein modulation of viral genomic and subgenomic RNA synthesis
    • Tzeng, W. P., and T. K. Frey. 2005. Rubella virus capsid protein modulation of viral genomic and subgenomic RNA synthesis. Virology 337:327-334.
    • (2005) Virology , vol.337 , pp. 327-334
    • Tzeng, W.P.1    Frey, T.K.2
  • 37
    • 0015987440 scopus 로고
    • Phosphorylated proteins of Sindbis virus
    • Waite, M. R., M. Lubin, K. J. Jones, and H. R. Bose. 1974. Phosphorylated proteins of Sindbis virus. J. Virol. 13:244-246.
    • (1974) J. Virol. , vol.13 , pp. 244-246
    • Waite, M.R.1    Lubin, M.2    Jones, K.J.3    Bose, H.R.4
  • 38
    • 0036229472 scopus 로고    scopus 로고
    • Both viral transcription and replication are reduced when the rabies virus nucleoprotein is not phosphorylated
    • Wu, X., X. Gong, H. D. Foley, M. J. Schnell, and Z. F. Fu. 2002. Both viral transcription and replication are reduced when the rabies virus nucleoprotein is not phosphorylated. J. Virol. 76:4153-4161.
    • (2002) J. Virol. , vol.76 , pp. 4153-4161
    • Wu, X.1    Gong, X.2    Foley, H.D.3    Schnell, M.J.4    Fu, Z.F.5
  • 39
    • 0033057248 scopus 로고    scopus 로고
    • Mutational analysis, using a full-length rubella virus cDNA clone, of rubella virus E1 transmembrane and cytoplasmic domains required for virus release
    • Yao, J., and S. Gillam. 1999. Mutational analysis, using a full-length rubella virus cDNA clone, of rubella virus E1 transmembrane and cytoplasmic domains required for virus release. J. Virol. 73:4622-4630.
    • (1999) J. Virol. , vol.73 , pp. 4622-4630
    • Yao, J.1    Gillam, S.2
  • 40
    • 0028358552 scopus 로고
    • Multiple functions of capsid protein phosphorylation in duck hepatitis B virus replication
    • Yu, M., and J. Summers. 1994. Multiple functions of capsid protein phosphorylation in duck hepatitis B virus replication. J. Virol. 68:4341-4348.
    • (1994) J. Virol. , vol.68 , pp. 4341-4348
    • Yu, M.1    Summers, J.2
  • 41
    • 0037302292 scopus 로고    scopus 로고
    • Phosphorylated serine residues and an arginine-rich domain of the Moloney murine leukemia virus p12 protein are required for early events of viral infection
    • Yueh, A., and S. P. Goff. 2003. Phosphorylated serine residues and an arginine-rich domain of the Moloney murine leukemia virus p12 protein are required for early events of viral infection. J. Virol. 77:1820-1829.
    • (2003) J. Virol. , vol.77 , pp. 1820-1829
    • Yueh, A.1    Goff, S.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.