메뉴 건너뛰기




Volumn 20, Issue 12, 2012, Pages 570-576

Cytopathic effects: Virus-modulated manifestations of innate immunity?

Author keywords

Picornaviruses; Virus induced apoptosis; Virus induced necrosis

Indexed keywords

RNA DIRECTED RNA POLYMERASE; VIRUS PROTEIN;

EID: 84869489300     PISSN: 0966842X     EISSN: 18784380     Source Type: Journal    
DOI: 10.1016/j.tim.2012.09.003     Document Type: Review
Times cited : (32)

References (55)
  • 1
    • 84870967885 scopus 로고    scopus 로고
    • Persistent infection
    • ASM Press, E. Ehrenfeld (Ed.)
    • Colbère-Garapin F., Lipton H.L. Persistent infection. The Picornaviruses 2010, 321-335. ASM Press. E. Ehrenfeld (Ed.).
    • (2010) The Picornaviruses , pp. 321-335
    • Colbère-Garapin, F.1    Lipton, H.L.2
  • 2
    • 78449303073 scopus 로고    scopus 로고
    • Viral security proteins: counteracting host defences
    • Agol V.I., Gmyl A.P. Viral security proteins: counteracting host defences. Nat. Rev. Microbiol. 2010, 8:867-878.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 867-878
    • Agol, V.I.1    Gmyl, A.P.2
  • 3
    • 67650424325 scopus 로고    scopus 로고
    • Antiapoptotic activity of the cardiovirus leader protein, a viral "security" protein
    • Romanova L.I., et al. Antiapoptotic activity of the cardiovirus leader protein, a viral "security" protein. J. Virol. 2009, 83:7273-7284.
    • (2009) J. Virol. , vol.83 , pp. 7273-7284
    • Romanova, L.I.1
  • 4
    • 84861314633 scopus 로고    scopus 로고
    • Suppression of injuries caused by a lytic RNA virus (mengovirus) and their uncoupling from viral reproduction by mutual cell/virus disarmament
    • Mikitas O.V., et al. Suppression of injuries caused by a lytic RNA virus (mengovirus) and their uncoupling from viral reproduction by mutual cell/virus disarmament. J. Virol. 2012, 86:5574-5583.
    • (2012) J. Virol. , vol.86 , pp. 5574-5583
    • Mikitas, O.V.1
  • 5
    • 0037213915 scopus 로고    scopus 로고
    • Poliovirus-induced apoptosis is reduced in cells expressing a mutant CD155 selected during persistent poliovirus infection in neuroblastoma cells
    • Gosselin A.S., et al. Poliovirus-induced apoptosis is reduced in cells expressing a mutant CD155 selected during persistent poliovirus infection in neuroblastoma cells. J. Virol. 2003, 77:790-798.
    • (2003) J. Virol. , vol.77 , pp. 790-798
    • Gosselin, A.S.1
  • 6
    • 18144414234 scopus 로고    scopus 로고
    • Apoptotic events induced by human rhinovirus infection
    • Deszcz L., et al. Apoptotic events induced by human rhinovirus infection. J. Gen. Virol. 2005, 86:1379-1389.
    • (2005) J. Gen. Virol. , vol.86 , pp. 1379-1389
    • Deszcz, L.1
  • 7
    • 10644270663 scopus 로고    scopus 로고
    • Dendritic cells and macrophages are productively infected by poliovirus
    • Wahid R., et al. Dendritic cells and macrophages are productively infected by poliovirus. J. Virol. 2005, 79:401-409.
    • (2005) J. Virol. , vol.79 , pp. 401-409
    • Wahid, R.1
  • 8
    • 0028977987 scopus 로고
    • Apoptosis-inducing and apoptosis-preventing functions of poliovirus
    • Tolskaya E.A., et al. Apoptosis-inducing and apoptosis-preventing functions of poliovirus. J. Virol. 1995, 69:1181-1189.
    • (1995) J. Virol. , vol.69 , pp. 1181-1189
    • Tolskaya, E.A.1
  • 9
    • 33846964621 scopus 로고    scopus 로고
    • Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak
    • Willis S.N., et al. Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak. Science 2007, 315:856-859.
    • (2007) Science , vol.315 , pp. 856-859
    • Willis, S.N.1
  • 10
    • 10644268336 scopus 로고    scopus 로고
    • VP1 of foot-and-mouth disease virus induces apoptosis via the Akt signaling pathway
    • Peng J.M., et al. VP1 of foot-and-mouth disease virus induces apoptosis via the Akt signaling pathway. J. Biol. Chem. 2004, 279:52168-52174.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52168-52174
    • Peng, J.M.1
  • 11
    • 35649003113 scopus 로고    scopus 로고
    • Induction of immature dendritic cell apoptosis by foot and mouth disease virus is an integrin receptor mediated event before viral infection
    • Jin H., et al. Induction of immature dendritic cell apoptosis by foot and mouth disease virus is an integrin receptor mediated event before viral infection. J. Cell. Biochem. 2007, 102:980-991.
    • (2007) J. Cell. Biochem. , vol.102 , pp. 980-991
    • Jin, H.1
  • 12
    • 77952716030 scopus 로고    scopus 로고
    • A single coxsackievirus B2 capsid residue controls cytolysis and apoptosis in rhabdomyosarcoma cells
    • Gullberg M., et al. A single coxsackievirus B2 capsid residue controls cytolysis and apoptosis in rhabdomyosarcoma cells. J. Virol. 2010, 84:5868-5879.
    • (2010) J. Virol. , vol.84 , pp. 5868-5879
    • Gullberg, M.1
  • 13
    • 63849210692 scopus 로고    scopus 로고
    • Apoptotic signaling cascades operating in poliovirus-infected cells
    • Blondel B., et al. Apoptotic signaling cascades operating in poliovirus-infected cells. Front. Biosci. 2009, 14:2181-2192.
    • (2009) Front. Biosci. , vol.14 , pp. 2181-2192
    • Blondel, B.1
  • 14
    • 0035201806 scopus 로고    scopus 로고
    • Suppression of apoptotic and necrotic cell death by poliovirus
    • Koyama A.H., et al. Suppression of apoptotic and necrotic cell death by poliovirus. J. Gen. Virol. 2001, 82:2965-2972.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2965-2972
    • Koyama, A.H.1
  • 15
    • 33745197325 scopus 로고    scopus 로고
    • Coxsackievirus protein 2BC blocks host cell apoptosis by inhibiting caspase-3
    • Salako M.A., et al. Coxsackievirus protein 2BC blocks host cell apoptosis by inhibiting caspase-3. J. Biol. Chem. 2006, 281:16296-16304.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16296-16304
    • Salako, M.A.1
  • 16
    • 0034795061 scopus 로고    scopus 로고
    • Poliovirus protein 3A inhibits tumor necrosis factor (TNF)-induced apoptosis by eliminating the TNF receptor from the cell surface
    • Neznanov N., et al. Poliovirus protein 3A inhibits tumor necrosis factor (TNF)-induced apoptosis by eliminating the TNF receptor from the cell surface. J. Virol. 2001, 75:10409-10420.
    • (2001) J. Virol. , vol.75 , pp. 10409-10420
    • Neznanov, N.1
  • 17
    • 79952040396 scopus 로고    scopus 로고
    • Interference with cellular gene expression
    • ASM Press, E. Ehrenfeld (Ed.)
    • Dougherty J.D., et al. Interference with cellular gene expression. The Picornaviruses 2010, 165-180. ASM Press. E. Ehrenfeld (Ed.).
    • (2010) The Picornaviruses , pp. 165-180
    • Dougherty, J.D.1
  • 18
    • 0012848648 scopus 로고    scopus 로고
    • Picornavirus protease-mediated shutoff of host translation: direct cleavage of a cellular initiation factor
    • ASM Press, B.L. Semler, E. Wimmer (Eds.)
    • Kuechler E., et al. Picornavirus protease-mediated shutoff of host translation: direct cleavage of a cellular initiation factor. Molecular Biology of Picornaviruses 2002, 301-311. ASM Press. B.L. Semler, E. Wimmer (Eds.).
    • (2002) Molecular Biology of Picornaviruses , pp. 301-311
    • Kuechler, E.1
  • 19
    • 0142042113 scopus 로고    scopus 로고
    • Effects of picornavirus proteinases on host cell transcription
    • ASM Press, B.L. Semler, E. Wimmer (Eds.)
    • Dasgupta A., et al. Effects of picornavirus proteinases on host cell transcription. Molecular Biology of Picornaviruses 2002, 321-335. ASM Press. B.L. Semler, E. Wimmer (Eds.).
    • (2002) Molecular Biology of Picornaviruses , pp. 321-335
    • Dasgupta, A.1
  • 20
    • 0031800940 scopus 로고    scopus 로고
    • Rapamycin and wortmannin enhance replication of a defective encephalomyocarditis virus
    • Svitkin Y.V., et al. Rapamycin and wortmannin enhance replication of a defective encephalomyocarditis virus. J. Virol. 1998, 72:5811-5819.
    • (1998) J. Virol. , vol.72 , pp. 5811-5819
    • Svitkin, Y.V.1
  • 21
    • 77951051592 scopus 로고    scopus 로고
    • Variability in inhibition of host RNA synthesis by entero- and cardioviruses
    • Krupina K.A., et al. Variability in inhibition of host RNA synthesis by entero- and cardioviruses. J. Gen. Virol. 2010, 91:1239-1244.
    • (2010) J. Gen. Virol. , vol.91 , pp. 1239-1244
    • Krupina, K.A.1
  • 22
    • 0142091700 scopus 로고    scopus 로고
    • Encephalomyocarditis virus (EMCV) proteins 2A and 3BCD localize to nuclei and inhibit cellular mRNA transcription but not rRNA transcription
    • Aminev A.G., et al. Encephalomyocarditis virus (EMCV) proteins 2A and 3BCD localize to nuclei and inhibit cellular mRNA transcription but not rRNA transcription. Virus Res. 2003, 95:59-73.
    • (2003) Virus Res. , vol.95 , pp. 59-73
    • Aminev, A.G.1
  • 23
    • 78650797340 scopus 로고    scopus 로고
    • Mutational analysis of the EMCV 2A protein identifies a nuclear localization signal and an eIF4E binding site
    • Groppo R., et al. Mutational analysis of the EMCV 2A protein identifies a nuclear localization signal and an eIF4E binding site. Virology 2011, 410:257-267.
    • (2011) Virology , vol.410 , pp. 257-267
    • Groppo, R.1
  • 24
    • 0034734764 scopus 로고    scopus 로고
    • Early alteration of nucleo-cytoplasmic traffic induced by some RNA viruses
    • Belov G.A., et al. Early alteration of nucleo-cytoplasmic traffic induced by some RNA viruses. Virology 2000, 275:244-248.
    • (2000) Virology , vol.275 , pp. 244-248
    • Belov, G.A.1
  • 25
    • 33644748242 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic traffic disorder induced by cardioviruses
    • Lidsky P.V., et al. Nucleo-cytoplasmic traffic disorder induced by cardioviruses. J. Virol. 2006, 80:2705-2717.
    • (2006) J. Virol. , vol.80 , pp. 2705-2717
    • Lidsky, P.V.1
  • 26
    • 4444274231 scopus 로고    scopus 로고
    • Bidirectional increase in permeability of nuclear envelope upon poliovirus infection and accompanying alterations of nuclear pores
    • Belov G.A., et al. Bidirectional increase in permeability of nuclear envelope upon poliovirus infection and accompanying alterations of nuclear pores. J. Virol. 2004, 78:10166-10177.
    • (2004) J. Virol. , vol.78 , pp. 10166-10177
    • Belov, G.A.1
  • 27
    • 70350367733 scopus 로고    scopus 로고
    • RNA nuclear export is blocked by poliovirus 2A protease and is concomitant with nucleoporin cleavage
    • Castelló A., et al. RNA nuclear export is blocked by poliovirus 2A protease and is concomitant with nucleoporin cleavage. J. Cell Sci. 2009, 122:3799-3809.
    • (2009) J. Cell Sci. , vol.122 , pp. 3799-3809
    • Castelló, A.1
  • 28
    • 77956511212 scopus 로고    scopus 로고
    • Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease
    • Park N., et al. Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease. J. Biol. Chem. 2010, 285:28796-28805.
    • (2010) J. Biol. Chem. , vol.285 , pp. 28796-28805
    • Park, N.1
  • 29
    • 63149173682 scopus 로고    scopus 로고
    • Mengovirus-induced rearrangement of the nuclear pore complex: hijacking cellular phosphorylation machinery
    • Bardina M.V., et al. Mengovirus-induced rearrangement of the nuclear pore complex: hijacking cellular phosphorylation machinery. J. Virol. 2009, 83:3150-3161.
    • (2009) J. Virol. , vol.83 , pp. 3150-3161
    • Bardina, M.V.1
  • 30
    • 59649088827 scopus 로고    scopus 로고
    • Leader-induced phosphorylation of nucleoporins correlates with nuclear trafficking inhibition by cardioviruses
    • Porter F.W., Palmenberg A.C. Leader-induced phosphorylation of nucleoporins correlates with nuclear trafficking inhibition by cardioviruses. J. Virol. 2009, 83:1941-1951.
    • (2009) J. Virol. , vol.83 , pp. 1941-1951
    • Porter, F.W.1    Palmenberg, A.C.2
  • 31
    • 79952039623 scopus 로고    scopus 로고
    • Remodeling cellular membranes
    • ASM Press, E. Ehrenfeld (Ed.)
    • van Kuppeveld F., et al. Remodeling cellular membranes. The Picornaviruses 2010, 181-193. ASM Press. E. Ehrenfeld (Ed.).
    • (2010) The Picornaviruses , pp. 181-193
    • van Kuppeveld, F.1
  • 32
    • 35948982216 scopus 로고    scopus 로고
    • The mengovirus leader protein blocks interferon-α/β gene transcription and inhibits activation of interferon regulatory factor 3
    • Hato S.V., et al. The mengovirus leader protein blocks interferon-α/β gene transcription and inhibits activation of interferon regulatory factor 3. Cell. Microbiol. 2007, 9:2921-2930.
    • (2007) Cell. Microbiol. , vol.9 , pp. 2921-2930
    • Hato, S.V.1
  • 33
    • 80052443081 scopus 로고    scopus 로고
    • The leader protein of cardioviruses inhibits stress granule assembly
    • Borghese F., Michiels T. The leader protein of cardioviruses inhibits stress granule assembly. J. Virol. 2011, 85:9614-9622.
    • (2011) J. Virol. , vol.85 , pp. 9614-9622
    • Borghese, F.1    Michiels, T.2
  • 34
    • 84255210700 scopus 로고    scopus 로고
    • Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012
    • Galluzzi L., et al. Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012. Cell Death Differ. 2012, 19:107-120.
    • (2012) Cell Death Differ. , vol.19 , pp. 107-120
    • Galluzzi, L.1
  • 35
    • 79960921946 scopus 로고    scopus 로고
    • The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs
    • Tenev T., et al. The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. Mol. Cell 2011, 43:432-448.
    • (2011) Mol. Cell , vol.43 , pp. 432-448
    • Tenev, T.1
  • 36
    • 79960922705 scopus 로고    scopus 로고
    • CIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms
    • Feoktistova M., et al. cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol. Cell 2011, 43:449-463.
    • (2011) Mol. Cell , vol.43 , pp. 449-463
    • Feoktistova, M.1
  • 37
    • 81255195542 scopus 로고    scopus 로고
    • Programmed necrosis: backup to and competitor with apoptosis in the immune system
    • Han J., et al. Programmed necrosis: backup to and competitor with apoptosis in the immune system. Nat. Immunol. 2011, 12:1143-1149.
    • (2011) Nat. Immunol. , vol.12 , pp. 1143-1149
    • Han, J.1
  • 38
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-α
    • He S., et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-α. Cell 2009, 137:1100-1111.
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1
  • 39
    • 0034120437 scopus 로고    scopus 로고
    • Competing death programs in poliovirus-infected cells: commitment switch in the mid of infectious cycle
    • Agol V.I., et al. Competing death programs in poliovirus-infected cells: commitment switch in the mid of infectious cycle. J. Virol. 2000, 74:5534-5541.
    • (2000) J. Virol. , vol.74 , pp. 5534-5541
    • Agol, V.I.1
  • 40
    • 0037213269 scopus 로고    scopus 로고
    • The major apoptotic pathway activated and suppressed by poliovirus
    • Belov G.A., et al. The major apoptotic pathway activated and suppressed by poliovirus. J. Virol. 2003, 77:45-56.
    • (2003) J. Virol. , vol.77 , pp. 45-56
    • Belov, G.A.1
  • 41
    • 70349266011 scopus 로고    scopus 로고
    • Bypass suppression of small-plaque phenotypes by a mutation in poliovirus 2A that enhances apoptosis
    • Burgon T.B., et al. Bypass suppression of small-plaque phenotypes by a mutation in poliovirus 2A that enhances apoptosis. J. Virol. 2009, 83:10129-10139.
    • (2009) J. Virol. , vol.83 , pp. 10129-10139
    • Burgon, T.B.1
  • 42
    • 77952692073 scopus 로고    scopus 로고
    • 2A protease is not a prerequisite for poliovirus replication
    • Igarashi H., et al. 2A protease is not a prerequisite for poliovirus replication. J. Virol. 2010, 84:5947-5957.
    • (2010) J. Virol. , vol.84 , pp. 5947-5957
    • Igarashi, H.1
  • 43
    • 84856160569 scopus 로고    scopus 로고
    • Caspase 8 inhibits programmed necrosis by processing CYLD
    • O'Donnell M.A., et al. Caspase 8 inhibits programmed necrosis by processing CYLD. Nat. Cell Biol. 2011, 13:1437-1442.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1437-1442
    • O'Donnell, M.A.1
  • 44
    • 84856231635 scopus 로고    scopus 로고
    • Viral infection and the evolution of caspase 8-regulated apoptotic and necrotic death pathways
    • Mocarski E.S., et al. Viral infection and the evolution of caspase 8-regulated apoptotic and necrotic death pathways. Nat. Rev. Immunol. 2012, 12:79-88.
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 79-88
    • Mocarski, E.S.1
  • 45
    • 0030465346 scopus 로고    scopus 로고
    • A final s{cyrillic}heckpoint in the drug-promoted and poliovirus-promoted apoptosis is under post-translational control by growth factors
    • Tolskaya E.A., et al. A final s{cyrillic}heckpoint in the drug-promoted and poliovirus-promoted apoptosis is under post-translational control by growth factors. J. Cell. Biochem. 1996, 63:422-431.
    • (1996) J. Cell. Biochem. , vol.63 , pp. 422-431
    • Tolskaya, E.A.1
  • 46
    • 0029814501 scopus 로고    scopus 로고
    • Theiler's murine encephalomyelitis virus kills restrictive but not permissive cells by apoptosis
    • Jelachich M.L., Lipton H.L. Theiler's murine encephalomyelitis virus kills restrictive but not permissive cells by apoptosis. J. Virol. 1996, 70:6856-6861.
    • (1996) J. Virol. , vol.70 , pp. 6856-6861
    • Jelachich, M.L.1    Lipton, H.L.2
  • 47
    • 0343090469 scopus 로고    scopus 로고
    • Poliovirus induces apoptosis in the human U937 promonocytic cell line
    • Lopez-Guerrero J.A., et al. Poliovirus induces apoptosis in the human U937 promonocytic cell line. Virology 2000, 272:250-256.
    • (2000) Virology , vol.272 , pp. 250-256
    • Lopez-Guerrero, J.A.1
  • 48
    • 0032809437 scopus 로고    scopus 로고
    • Poliovirus infection induces apoptosis in CaCo-2 cells
    • Ammendolia M.G., et al. Poliovirus infection induces apoptosis in CaCo-2 cells. J. Med. Virol. 1999, 59:122-129.
    • (1999) J. Med. Virol. , vol.59 , pp. 122-129
    • Ammendolia, M.G.1
  • 49
    • 0031596337 scopus 로고    scopus 로고
    • NF-κB-mediated inhibition of apoptosis is required for encephalomyocarditis virus virulence: a mechanism of resistance in p50 knockout mice
    • Schwarz E.M., et al. NF-κB-mediated inhibition of apoptosis is required for encephalomyocarditis virus virulence: a mechanism of resistance in p50 knockout mice. J. Virol. 1998, 72:5654-5660.
    • (1998) J. Virol. , vol.72 , pp. 5654-5660
    • Schwarz, E.M.1
  • 50
    • 19944426505 scopus 로고    scopus 로고
    • Variability in apoptotic response to poliovirus infection
    • Romanova L.I., et al. Variability in apoptotic response to poliovirus infection. Virology 2005, 331:292-306.
    • (2005) Virology , vol.331 , pp. 292-306
    • Romanova, L.I.1
  • 51
    • 84857081648 scopus 로고    scopus 로고
    • The anti-apoptotic Mcl-1 protein controls the type of cell death in Theiler's virus-infected BHK-21 cells
    • Arslan S.Y., et al. The anti-apoptotic Mcl-1 protein controls the type of cell death in Theiler's virus-infected BHK-21 cells. J. Virol. 2012, 86:1922-1929.
    • (2012) J. Virol. , vol.86 , pp. 1922-1929
    • Arslan, S.Y.1
  • 52
    • 84858081250 scopus 로고    scopus 로고
    • The origin and diversity of the HIV-1 pandemic
    • Hemelaar J. The origin and diversity of the HIV-1 pandemic. Trends Mol. Med. 2012, 18:182-192.
    • (2012) Trends Mol. Med. , vol.18 , pp. 182-192
    • Hemelaar, J.1
  • 53
    • 27344438916 scopus 로고    scopus 로고
    • Bats are natural reservoirs of SARS-like coronaviruses
    • Li W., et al. Bats are natural reservoirs of SARS-like coronaviruses. Science 2005, 310:676-679.
    • (2005) Science , vol.310 , pp. 676-679
    • Li, W.1
  • 54
    • 84857424101 scopus 로고    scopus 로고
    • Myxomatosis in Australia and Europe: a model for emerging infectious diseases
    • Kerr P.J. Myxomatosis in Australia and Europe: a model for emerging infectious diseases. Antiviral Res. 2012, 93:387-415.
    • (2012) Antiviral Res. , vol.93 , pp. 387-415
    • Kerr, P.J.1
  • 55
    • 79952039453 scopus 로고    scopus 로고
    • Genome organization and encoded proteins
    • ASM Press, E. Ehrenfeld (Ed.)
    • Palmenberg A., et al. Genome organization and encoded proteins. The Picornaviruses 2010, 3-17. ASM Press. E. Ehrenfeld (Ed.).
    • (2010) The Picornaviruses , pp. 3-17
    • Palmenberg, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.