메뉴 건너뛰기




Volumn 88, Issue 18, 2014, Pages 10851-10863

Sequence of events in measles virus replication: Role of phosphoprotein-nucleocapsid interactions

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOCAPSID PROTEIN; PHOSPHOPROTEIN; P PROTEIN, SENDAI VIRUS; PROTEIN BINDING; VIRUS PROTEIN;

EID: 84906351352     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00664-14     Document Type: Article
Times cited : (44)

References (50)
  • 1
    • 84857998251 scopus 로고    scopus 로고
    • Mechanism of RNA synthesis initiation by the vesicular stomatitis virus polymerase
    • Morin B, Rahmeh AA, Whelan SP. 2012. Mechanism of RNA synthesis initiation by the vesicular stomatitis virus polymerase. EMBO J. 31:1320-1329. http://dx.doi.org/10.1038/emboj.2011.483.
    • (2012) EMBO J. , vol.31 , pp. 1320-1329
    • Morin, B.1    Rahmeh, A.A.2    Whelan, S.P.3
  • 3
    • 33746516378 scopus 로고    scopus 로고
    • Structure of the vesicular stomatitis virus nucleoprotein-RNA complex
    • Green TJ, Zhang X, Wertz GW, Luo M. 2006. Structure of the vesicular stomatitis virus nucleoprotein-RNA complex. Science 313:357-360. http://dx.doi.org/10.1126/science.1126953.
    • (2006) Science , vol.313 , pp. 357-360
    • Green, T.J.1    Zhang, X.2    Wertz, G.W.3    Luo, M.4
  • 5
    • 0141706544 scopus 로고    scopus 로고
    • Crystal structure of the Borna disease virus nucleoprotein
    • Rudolph MG, Kraus I, Dickmanns A, Eickmann M, Garten W, Ficner R. 2003. Crystal structure of the Borna disease virus nucleoprotein. Structure 11:1219-1226. http://dx.doi.org/10.1016/j.str.2003.08.011.
    • (2003) Structure , vol.11 , pp. 1219-1226
    • Rudolph, M.G.1    Kraus, I.2    Dickmanns, A.3    Eickmann, M.4    Garten, W.5    Ficner, R.6
  • 6
    • 1242283916 scopus 로고    scopus 로고
    • Viral RNA polymerase scanning and the gymnastics of Sendai virus RNA synthesis
    • Kolakofsky D, Le Mercier P, Iseni F, Garcin D. 2004. Viral RNA polymerase scanning and the gymnastics of Sendai virus RNA synthesis. Virology 318:463-473. http://dx.doi.org/10.1016/j.virol.2003.10.031.
    • (2004) Virology , vol.318 , pp. 463-473
    • Kolakofsky, D.1    Le Mercier, P.2    Iseni, F.3    Garcin, D.4
  • 7
    • 18744410096 scopus 로고    scopus 로고
    • Dynamics of viral RNA synthesis during measles virus infection
    • Plumet S, Duprex WP, Gerlier D. 2005. Dynamics of viral RNA synthesis during measles virus infection. J. Virol. 79:6900-6908. http://dx.doi.org/10.1128/JVI.79.11.6900-6908.2005.
    • (2005) J. Virol. , vol.79 , pp. 6900-6908
    • Plumet, S.1    Duprex, W.P.2    Gerlier, D.3
  • 8
    • 2442666665 scopus 로고    scopus 로고
    • Transcription and replication of nonsegmented negative-strand RNA viruses
    • Whelan SP, Barr JN, Wertz GW. 2004. Transcription and replication of nonsegmented negative-strand RNA viruses. Curr. Top. Microbiol. Immunol. 283:61-119.
    • (2004) Curr. Top. Microbiol. Immunol. , vol.283 , pp. 61-119
    • Whelan, S.P.1    Barr, J.N.2    Wertz, G.W.3
  • 9
    • 0242582329 scopus 로고    scopus 로고
    • Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein
    • Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, Longhi S. 2003. Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein. J. Biol. Chem. 278:44567-44573. http://dx.doi.org/10.1074/jbc.M308745200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44567-44573
    • Johansson, K.1    Bourhis, J.M.2    Campanacci, V.3    Cambillau, C.4    Canard, B.5    Longhi, S.6
  • 10
  • 11
    • 84859499620 scopus 로고    scopus 로고
    • The measles virus N(TAIL)-XD complex: an illustrative example of fuzziness
    • Longhi S. 2012. The measles virus N(TAIL)-XD complex: an illustrative example of fuzziness. Adv. Exp. Med. Biol. 725:126-141. http://dx.doi.org/10.1007/978-1-4614-0659-4_8.
    • (2012) Adv. Exp. Med. Biol. , vol.725 , pp. 126-141
    • Longhi, S.1
  • 13
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive protein-protein interaction assay based on Gaussia luciferase
    • Remy I, Michnick SW. 2006. A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nat. Methods 3:977-979. http://dx.doi.org/10.1038/nmeth979.
    • (2006) Nat. Methods , vol.3 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 14
    • 33947426044 scopus 로고    scopus 로고
    • Suppression of the Sendai virus M protein through a novel short interfering RNA approach inhibits viral particle production but does not affect viral RNA synthesis
    • Mottet-Osman G, Iseni F, Pelet T, Wiznerowicz M, Garcin D, Roux L. 2007. Suppression of the Sendai virus M protein through a novel short interfering RNA approach inhibits viral particle production but does not affect viral RNA synthesis. J. Virol. 81:2861-2868. http://dx.doi.org/10.1128/JVI.02291-06.
    • (2007) J. Virol. , vol.81 , pp. 2861-2868
    • Mottet-Osman, G.1    Iseni, F.2    Pelet, T.3    Wiznerowicz, M.4    Garcin, D.5    Roux, L.6
  • 15
    • 77955663782 scopus 로고    scopus 로고
    • Sendai virus particle production: basic requirements and role of the SYWST motif present in HN cytoplasmic tail
    • Gosselin-Grenet AS, Mottet-Osman G, Roux L. 2010. Sendai virus particle production: basic requirements and role of the SYWST motif present in HN cytoplasmic tail. J. Virol. 405:439-447. http://dx.doi.org/10.1016/j.virol.2010.06.030.
    • (2010) J. Virol. , vol.405 , pp. 439-447
    • Gosselin-Grenet, A.S.1    Mottet-Osman, G.2    Roux, L.3
  • 16
    • 0038419800 scopus 로고    scopus 로고
    • Induction of an interferon response by RNAi vectors in mammalian cells
    • Bridge AJ, Pebernard S, Ducraux A, Nicoulaz AL, Iggo R. 2003. Induction of an interferon response by RNAi vectors in mammalian cells. Nat. Genet. 34:263-264. http://dx.doi.org/10.1038/ng1173.
    • (2003) Nat. Genet. , vol.34 , pp. 263-264
    • Bridge, A.J.1    Pebernard, S.2    Ducraux, A.3    Nicoulaz, A.L.4    Iggo, R.5
  • 18
    • 6344294889 scopus 로고    scopus 로고
    • Measles virus phosphoprotein gene products: conformational flexibility of the P/V protein amino-terminal domain and C protein infectivity factor function
    • Devaux P, Cattaneo R. 2004. Measles virus phosphoprotein gene products: conformational flexibility of the P/V protein amino-terminal domain and C protein infectivity factor function. J. Virol. 78:11632-11640. http://dx.doi.org/10.1128/JVI.78.21.11632-11640.2004.
    • (2004) J. Virol. , vol.78 , pp. 11632-11640
    • Devaux, P.1    Cattaneo, R.2
  • 19
    • 0034710650 scopus 로고    scopus 로고
    • SLAM (CDw150) is a cellular receptor for measles virus
    • Tatsuo H, Ono N, Tanaka K, Yanagi Y. 2000. SLAM (CDw150) is a cellular receptor for measles virus. Nature 406:893-897. http://dx.doi.org/10.1038/35022579.
    • (2000) Nature , vol.406 , pp. 893-897
    • Tatsuo, H.1    Ono, N.2    Tanaka, K.3    Yanagi, Y.4
  • 20
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini L, Blomer U, Gallay P, Ory D, Mulligan R, Gage FH, Verma IM, Trono D. 1996. In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272:263-267. http://dx.doi.org/10.1126/science.272.5259.263.
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1    Blomer, U.2    Gallay, P.3    Ory, D.4    Mulligan, R.5    Gage, F.H.6    Verma, I.M.7    Trono, D.8
  • 21
    • 0032829772 scopus 로고    scopus 로고
    • Observation of measles virus cell-to-cell spread in astrocytoma cells by using a green fluorescent protein-expressing recombinant virus
    • Duprex WP, McQuaid S, Hangartner L, Billeter MA, Rima BK. 1999. Observation of measles virus cell-to-cell spread in astrocytoma cells by using a green fluorescent protein-expressing recombinant virus. J. Virol. 73:9568-9575.
    • (1999) J. Virol. , vol.73 , pp. 9568-9575
    • Duprex, W.P.1    McQuaid, S.2    Hangartner, L.3    Billeter, M.A.4    Rima, B.K.5
  • 22
    • 24644433742 scopus 로고    scopus 로고
    • Inhibition of ubiquitination and stabilization of human ubiquitin E3 ligase PIRH2 by measles virus phosphoprotein
    • Chen M, Cortay JC, Logan IR, Sapountzi V, Robson CN, Gerlier D. 2005. Inhibition of ubiquitination and stabilization of human ubiquitin E3 ligase PIRH2 by measles virus phosphoprotein. J. Virol. 79:11824-11836. http://dx.doi.org/10.1128/JVI.79.18.11824-11836.2005.
    • (2005) J. Virol. , vol.79 , pp. 11824-11836
    • Chen, M.1    Cortay, J.C.2    Logan, I.R.3    Sapountzi, V.4    Robson, C.N.5    Gerlier, D.6
  • 23
    • 2942644452 scopus 로고    scopus 로고
    • Cell surface activation of the alternative complement pathway by the fusion protein of measles virus
    • Devaux P, Christiansen D, Plumet S, Gerlier D. 2004. Cell surface activation of the alternative complement pathway by the fusion protein of measles virus. J. Gen. Virol. 85:1665-1673. http://dx.doi.org/10.1099/vir.0.79880-0.
    • (2004) J. Gen. Virol. , vol.85 , pp. 1665-1673
    • Devaux, P.1    Christiansen, D.2    Plumet, S.3    Gerlier, D.4
  • 24
    • 84859498913 scopus 로고    scopus 로고
    • Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus
    • Shu Y, Habchi J, Costanzo S, Padilla A, Brunel J, Gerlier D, Oglesbee M, Longhi S. 2012. Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus. J. Biol. Chem. 287:11951-11967. http://dx.doi.org/10.1074/jbc.M111.333088.
    • (2012) J. Biol. Chem. , vol.287 , pp. 11951-11967
    • Shu, Y.1    Habchi, J.2    Costanzo, S.3    Padilla, A.4    Brunel, J.5    Gerlier, D.6    Oglesbee, M.7    Longhi, S.8
  • 25
    • 0033590214 scopus 로고    scopus 로고
    • Inefficient measles virus budding in murine L.CD46 fibroblasts
    • Vincent S, Spehner D, Manie S, Delorme R, Drillien R, Gerlier D. 1999. Inefficient measles virus budding in murine L.CD46 fibroblasts. Virology 265:185-195. http://dx.doi.org/10.1006/viro.1999.0064.
    • (1999) Virology , vol.265 , pp. 185-195
    • Vincent, S.1    Spehner, D.2    Manie, S.3    Delorme, R.4    Drillien, R.5    Gerlier, D.6
  • 27
    • 22144465783 scopus 로고    scopus 로고
    • Optimized SYBR green real-time PCR assay to quantify the absolute copy number of measles virus RNAs using gene specific primers
    • Plumet S, Gerlier D. 2005. Optimized SYBR green real-time PCR assay to quantify the absolute copy number of measles virus RNAs using gene specific primers. J. Virol. Methods 128:79-87. http://dx.doi.org/10.1016/j.jviromet.2005.03.020.
    • (2005) J. Virol. Methods , vol.128 , pp. 79-87
    • Plumet, S.1    Gerlier, D.2
  • 28
    • 84902482480 scopus 로고    scopus 로고
    • Coiled-coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative example
    • Blocquel D, Habchi J, Durand E, Sevajol M, Ferron F, Erales J, Papageorgiou N, Longhi S. 2014. Coiled-coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative example. Acta Crystallogr. D Biol. Crystallogr. 70:1589-1603. http://dx.doi.org/10.1016/j.virol.2010.06.030.
    • (2014) Acta Crystallogr. D Biol. Crystallogr. , vol.70 , pp. 1589-1603
    • Blocquel, D.1    Habchi, J.2    Durand, E.3    Sevajol, M.4    Ferron, F.5    Erales, J.6    Papageorgiou, N.7    Longhi, S.8
  • 30
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea EK, Klemm JD, Kim PS, Alber T. 1991. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254: 539-544. http://dx.doi.org/10.1126/science.1948029.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 31
  • 32
    • 19044381013 scopus 로고    scopus 로고
    • Phenotypic silencing of cytoplasmic genes using sequence-specific double-stranded short interfering RNA and its application in the reverse genetics of wild-type negative-strand RNA viruses
    • Bitko V, Barik S. 2001. Phenotypic silencing of cytoplasmic genes using sequence-specific double-stranded short interfering RNA and its application in the reverse genetics of wild-type negative-strand RNA viruses. BMC Microbiol. 1:34. http://dx.doi.org/10.1186/1471-2180-1-34.
    • (2001) BMC Microbiol. , vol.1 , pp. 34
    • Bitko, V.1    Barik, S.2
  • 33
    • 0345059128 scopus 로고    scopus 로고
    • Measles virus protein interactions in yeast: new findings and caveats
    • Chen M, Cortay JC, Gerlier D. 2003. Measles virus protein interactions in yeast: new findings and caveats. Virus Res. 98:123-129. http://dx.doi.org/10.1016/j.virusres.2003.09.003.
    • (2003) Virus Res. , vol.98 , pp. 123-129
    • Chen, M.1    Cortay, J.C.2    Gerlier, D.3
  • 34
    • 38649127553 scopus 로고    scopus 로고
    • Nonsegmented negative-strand RNA virus RNA synthesis in vivo
    • Curran J, Kolakofsky D. 2008. Nonsegmented negative-strand RNA virus RNA synthesis in vivo. Virology 371:227-230. http://dx.doi.org/10.1016/j.virol.2007.11.022.
    • (2008) Virology , vol.371 , pp. 227-230
    • Curran, J.1    Kolakofsky, D.2
  • 35
    • 35048818442 scopus 로고    scopus 로고
    • Measles virus minigenomes encoding two autofluorescent proteins reveal cell-to-cell variation in reporter expression dependent on viral sequences between the transcription units
    • Rennick LJ, Duprex WP, Rima BK. 2007. Measles virus minigenomes encoding two autofluorescent proteins reveal cell-to-cell variation in reporter expression dependent on viral sequences between the transcription units. J. Gen. Virol. 88:2710-2718. http://dx.doi.org/10.1099/vir.0.83106-0.
    • (2007) J. Gen. Virol. , vol.88 , pp. 2710-2718
    • Rennick, L.J.1    Duprex, W.P.2    Rima, B.K.3
  • 37
    • 70350289940 scopus 로고    scopus 로고
    • Ribose 2=-O methylation of the vesicular stomatitis virus mRNA cap precedes and facilitates subsequent guanine-N-7 methylation by the large polymerase protein
    • Rahmeh AA, Li J, Kranzusch PJ, Whelan SP. 2009. Ribose 2=-O methylation of the vesicular stomatitis virus mRNA cap precedes and facilitates subsequent guanine-N-7 methylation by the large polymerase protein. J. Virol. 83:11043-11050. http://dx.doi.org/10.1128/JVI.01426-09.
    • (2009) J. Virol. , vol.83 , pp. 11043-11050
    • Rahmeh, A.A.1    Li, J.2    Kranzusch, P.J.3    Whelan, S.P.4
  • 38
    • 35148849601 scopus 로고    scopus 로고
    • Vesicular stomatitis virus mRNA capping machinery requires specific cis-acting signals in the RNA
    • Wang JT, McElvain LE, Whelan SP. 2007. Vesicular stomatitis virus mRNA capping machinery requires specific cis-acting signals in the RNA. J. Virol. 81:11499-11506. http://dx.doi.org/10.1128/JVI.01057-07.
    • (2007) J. Virol. , vol.81 , pp. 11499-11506
    • Wang, J.T.1    McElvain, L.E.2    Whelan, S.P.3
  • 39
    • 47749090176 scopus 로고    scopus 로고
    • Formation of guanosine(5=)tetraphospho(5=) adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus
    • Ogino T, Banerjee AK. 2008. Formation of guanosine(5=)tetraphospho(5=) adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus. J. Virol. 82:7729-7734. http://dx.doi.org/10.1128/JVI.00326-08.
    • (2008) J. Virol. , vol.82 , pp. 7729-7734
    • Ogino, T.1    Banerjee, A.K.2
  • 40
    • 84877997305 scopus 로고    scopus 로고
    • Creation of a completely helper cell-dependent recombinant morbillivirus
    • Baron J, Baron MD. 2013. Creation of a completely helper cell-dependent recombinant morbillivirus. J. Gen. Virol. 94(Pt 6):1195-1199. http://dx.doi.org/10.1099/vir.0.050872-0.
    • (2013) J. Gen. Virol. , vol.94 , Issue.PART 6 , pp. 1195-1199
    • Baron, J.1    Baron, M.D.2
  • 41
    • 37049027944 scopus 로고    scopus 로고
    • De novo synthesis of N and P proteins as a key step in Sendai virus gene expression
    • Wiegand MA, Bossow S, Schlecht S, Neubert WJ. 2007. De novo synthesis of N and P proteins as a key step in Sendai virus gene expression. J. Virol. 81:13835-13844. http://dx.doi.org/10.1128/JVI.00914-07.
    • (2007) J. Virol. , vol.81 , pp. 13835-13844
    • Wiegand, M.A.1    Bossow, S.2    Schlecht, S.3    Neubert, W.J.4
  • 42
    • 70349311591 scopus 로고    scopus 로고
    • Parainfluenza virus 5 genomes are located in viral cytoplasmic bodies whilst the virus dismantles the interferon-induced antiviral state of cells
    • Carlos TS, Young DF, Schneider M, Simas JP, Randall RE. 2009. Parainfluenza virus 5 genomes are located in viral cytoplasmic bodies whilst the virus dismantles the interferon-induced antiviral state of cells. J. Gen. Virol. 90:2147-2156. http://dx.doi.org/10.1099/vir.0.012047-0.
    • (2009) J. Gen. Virol. , vol.90 , pp. 2147-2156
    • Carlos, T.S.1    Young, D.F.2    Schneider, M.3    Simas, J.P.4    Randall, R.E.5
  • 43
    • 67749104678 scopus 로고    scopus 로고
    • Functional characterization of Negri bodies (NBs) in rabies virusinfected cells: evidence that NBs are sites of viral transcription and replication
    • Lahaye X, Vidy A, Pomier C, Obiang L, Harper F, Gaudin Y, Blondel D. 2009. Functional characterization of Negri bodies (NBs) in rabies virusinfected cells: evidence that NBs are sites of viral transcription and replication. J. Virol. 83:7948-7958. http://dx.doi.org/10.1128/JVI.00554-09.
    • (2009) J. Virol. , vol.83 , pp. 7948-7958
    • Lahaye, X.1    Vidy, A.2    Pomier, C.3    Obiang, L.4    Harper, F.5    Gaudin, Y.6    Blondel, D.7
  • 44
    • 84892160896 scopus 로고    scopus 로고
    • Mutation of the TYTLE motif in the cytoplasmic tail of the Sendai virus fusion protein deeply affects viral assembly and particle production
    • Essaidi-Laziosi M, Shevtsova A, Gerlier D, Roux L. 2013. Mutation of the TYTLE motif in the cytoplasmic tail of the Sendai virus fusion protein deeply affects viral assembly and particle production. PLoS One 8:e78074. http://dx.doi.org/10.1371/journal.pone.0078074.
    • (2013) PLoS One , vol.8
    • Essaidi-Laziosi, M.1    Shevtsova, A.2    Gerlier, D.3    Roux, L.4
  • 45
    • 84864651001 scopus 로고    scopus 로고
    • Protein activity regulation by conformational entropy
    • Tzeng SR, Kalodimos CG. 2012. Protein activity regulation by conformational entropy. Nature 488:236-240. http://dx.doi.org/10.1038/nature11271.
    • (2012) Nature , vol.488 , pp. 236-240
    • Tzeng, S.R.1    Kalodimos, C.G.2
  • 47
    • 2942520968 scopus 로고    scopus 로고
    • Conformational flexibility in recombinant measles virus nucleocapsids visualized by cryo-negative stain electron microscopy and real-space helical reconstruction
    • Bhella D, Ralph A, Yeo RP. 2004. Conformational flexibility in recombinant measles virus nucleocapsids visualized by cryo-negative stain electron microscopy and real-space helical reconstruction. J. Mol. Biol. 340: 319-331. http://dx.doi.org/10.1016/j.jmb.2004.05.015.
    • (2004) J. Mol. Biol. , vol.340 , pp. 319-331
    • Bhella, D.1    Ralph, A.2    Yeo, R.P.3
  • 48
    • 78651394593 scopus 로고    scopus 로고
    • Nucleoprotein-RNA orientation in the measles virus nucleocapsid by three-dimensional electron microscopy
    • Desfosses A, Goret G, Farias Estrozi L, Ruigrok RW, Gutsche I. 2011. Nucleoprotein-RNA orientation in the measles virus nucleocapsid by three-dimensional electron microscopy. J. Virol. 85:1391-1395. http://dx.doi.org/10.1128/JVI.01459-10.
    • (2011) J. Virol. , vol.85 , pp. 1391-1395
    • Desfosses, A.1    Goret, G.2    Farias Estrozi, L.3    Ruigrok, R.W.4    Gutsche, I.5
  • 50
    • 84885648103 scopus 로고    scopus 로고
    • The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity.
    • Krumm SA, Takeda M, Plemper RK. 2013. The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity. J. Biol. Chem. 288:29943-29953. http://dx.doi.org/10.1074/jbc.M113.503862.
    • (2013) J. Biol. Chem. , vol.288 , pp. 29943-29953
    • Krumm, S.A.1    Takeda, M.2    Plemper, R.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.