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Volumn 87, Issue 9, 2013, Pages 5005-5018

Herpes simplex virus 1 infection induces activation and subsequent inhibition of the IFI16 and NLRP3 inflammasomes

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS ASSOCIATED SPECK LIKE PROTEIN CONTAINING CARD; CRYOPYRIN; GAMMA INTERFERON INDUCIBLE PROTEIN 16; IMMEDIATE EARLY PROTEIN; INFLAMMASOME; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; MICROORGANISM PROTEIN; PROTEASOME; PROTEIN ICP0; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84876334378     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00082-13     Document Type: Article
Times cited : (218)

References (90)
  • 6
    • 84866156921 scopus 로고    scopus 로고
    • Encephalomyocarditis virus viroporin 2B activates NLRP3 inflammasome
    • 8:e1002857. doi: 10.1371/journal.ppat.1002857.
    • Ito M, Yanagi Y, Ichinohe T. 2012. Encephalomyocarditis virus viroporin 2B activates NLRP3 inflammasome. PLoS Pathog. 8:e1002857. doi: 10.1371/journal.ppat.1002857.
    • (2012) PLoS Pathog
    • Ito, M.1    Yanagi, Y.2    Ichinohe, T.3
  • 7
    • 78650038649 scopus 로고    scopus 로고
    • Adenovirus membrane penetration activates the NLRP3 inflammasome
    • Barlan AU, Griffin TM, McGuire KA, Wiethoff CM. 2011. Adenovirus membrane penetration activates the NLRP3 inflammasome. J. Virol. 85: 146-155.
    • (2011) J. Virol , vol.85 , pp. 146-155
    • Barlan, A.U.1    Griffin, T.M.2    McGuire, K.A.3    Wiethoff, C.M.4
  • 9
    • 51849103168 scopus 로고    scopus 로고
    • The microbial and danger signals that activate Nod-like receptors
    • Benko S, Philpott DJ, Girardin SE. 2008. The microbial and danger signals that activate Nod-like receptors. Cytokine 43:368 -373.
    • (2008) Cytokine , vol.43 , pp. 368-373
    • Benko, S.1    Philpott, D.J.2    Girardin, S.E.3
  • 10
    • 74549184092 scopus 로고    scopus 로고
    • The NLRP3 inflammasome: a sensor for metabolic danger?
    • Schroder K, Zhou R, Tschopp J. 2010. The NLRP3 inflammasome: a sensor for metabolic danger? Science 327:296 -300.
    • (2010) Science , vol.327 , pp. 296-300
    • Schroder, K.1    Zhou, R.2    Tschopp, J.3
  • 11
    • 77955039460 scopus 로고    scopus 로고
    • Fungal pathogen recognition by the NLRP3 inflammasome
    • Joly S, Sutterwala FS. 2010. Fungal pathogen recognition by the NLRP3 inflammasome. Virulence 1:276 -280.
    • (2010) Virulence , vol.1 , pp. 276-280
    • Joly, S.1    Sutterwala, F.S.2
  • 12
    • 77649179433 scopus 로고    scopus 로고
    • NLRP3 inflammasome activation: The convergence of multiple signalling pathways on ROS production?
    • Tschopp J, Schroder K. 2010. NLRP3 inflammasome activation: The convergence of multiple signalling pathways on ROS production? Nat. Rev. Immunol. 10:210 -215.
    • (2010) Nat. Rev. Immunol , vol.10 , pp. 210-215
    • Tschopp, J.1    Schroder, K.2
  • 13
    • 77954958602 scopus 로고    scopus 로고
    • Aspergillus fumigatus stimulates the NLRP3 inflammasome through a pathway requiring ROS production and the Syk tyrosine kinase
    • 5:e10008. doi:10.1371/journal.pone.0010008.
    • Said-Sadier N, Padilla E, Langsley G, Ojcius DM. 2010. Aspergillus fumigatus stimulates the NLRP3 inflammasome through a pathway requiring ROS production and the Syk tyrosine kinase. PLoS One 5:e10008. doi:10.1371/journal.pone.0010008.
    • (2010) PLoS Pathog
    • Said-Sadier, N.1    Padilla, E.2    Langsley, G.3    Ojcius, D.M.4
  • 14
    • 0030947119 scopus 로고    scopus 로고
    • Oxidants and antioxidants in viral diseases: disease mechanisms and metabolic regulation
    • Peterhans E. 1997. Oxidants and antioxidants in viral diseases: disease mechanisms and metabolic regulation. J. Nutr. 127:962S-965S.
    • (1997) J. Nutr , vol.127
    • Peterhans, E.1
  • 15
    • 0035163836 scopus 로고    scopus 로고
    • Caspase activation by adenovirus E4orf4 protein is cell line specific and is mediated by the death receptor pathway
    • Livne A, Shtrichman R, Kleinberger T. 2001. Caspase activation by adenovirus E4orf4 protein is cell line specific and is mediated by the death receptor pathway. J. Virol. 75:789 -798.
    • (2001) J. Virol , vol.75 , pp. 789-798
    • Livne, A.1    Shtrichman, R.2    Kleinberger, T.3
  • 16
    • 72649083760 scopus 로고    scopus 로고
    • Oxidative damage to neurons caused by the induction of microglial NADPH oxidase in encephalomyocarditis virus infection
    • Ano Y, Sakudo A, Kimata T, Uraki R, Sugiura K, Onodera T. 2010. Oxidative damage to neurons caused by the induction of microglial NADPH oxidase in encephalomyocarditis virus infection. Neurosci. Lett. 469:39-43.
    • (2010) Neurosci. Lett , vol.469 , pp. 39-43
    • Ano, Y.1    Sakudo, A.2    Kimata, T.3    Uraki, R.4    Sugiura, K.5    Onodera, T.6
  • 18
    • 0032809592 scopus 로고    scopus 로고
    • Transcription and growth regulatory functions of the HIN-200 family of proteins
    • Johnstone RW, Trapani JA. 1999. Transcription and growth regulatory functions of the HIN-200 family of proteins. Mol. Cell. Biol. 19:5833-5838.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 5833-5838
    • Johnstone, R.W.1    Trapani, J.A.2
  • 19
    • 22144490446 scopus 로고    scopus 로고
    • The HIN-200 family: more than interferon-inducible genes
    • Ludlow LE, Johnstone RW, Clarke CJ. 2005. The HIN-200 family: more than interferon-inducible genes? Exp. Cell Res. 308:1-17.
    • (2005) Exp. Cell Res , vol.308 , pp. 1-17
    • Ludlow, L.E.1    Johnstone, R.W.2    Clarke, C.J.3
  • 20
    • 38449105062 scopus 로고    scopus 로고
    • Interferon-inducible IFI16 protein in human cancers and autoimmune diseases
    • Choubey D, Deka R, Ho SM. 2008. Interferon-inducible IFI16 protein in human cancers and autoimmune diseases. Front. Biosci. 13:598-608.
    • (2008) Front. Biosci , vol.13 , pp. 598-608
    • Choubey, D.1    Deka, R.2    Ho, S.M.3
  • 21
    • 38449122879 scopus 로고    scopus 로고
    • Role of IFI16 in DNA damage and checkpoint
    • Ouchi M, Ouchi T. 2008. Role of IFI16 in DNA damage and checkpoint. Front. Biosci. 13:236 -239.
    • (2008) Front. Biosci , vol.13 , pp. 236-239
    • Ouchi, M.1    Ouchi, T.2
  • 22
    • 77951485147 scopus 로고    scopus 로고
    • The interferon-inducible HIN-200 gene family in apoptosis and inflammation: implication for autoimmunity
    • Mondini M, Costa S, Sponza S, Gugliesi F, Gariglio M, Landolfo S. 2010. The interferon-inducible HIN-200 gene family in apoptosis and inflammation: implication for autoimmunity. Autoimmunity 43:226-231.
    • (2010) Autoimmunity , vol.43 , pp. 226-231
    • Mondini, M.1    Costa, S.2    Sponza, S.3    Gugliesi, F.4    Gariglio, M.5    Landolfo, S.6
  • 23
    • 0032479176 scopus 로고    scopus 로고
    • The human interferoninducible protein, IFI 16, is a repressor of transcription
    • Johnstone RW, Kerry JA, Trapani JA. 1998. The human interferoninducible protein, IFI 16, is a repressor of transcription. J. Biol. Chem. 273:17172-17177.
    • (1998) J. Biol. Chem , vol.273 , pp. 17172-17177
    • Johnstone, R.W.1    Kerry, J.A.2    Trapani, J.A.3
  • 25
    • 79956061094 scopus 로고    scopus 로고
    • IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi sarcoma-associated herpesvirus infection
    • Kerur N, Veettil MV, Sharma-Walia N, Bottero V, Sadagopan S, Otageri P, Chandran B. 2011. IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi sarcoma-associated herpesvirus infection. Cell Host Microbe 9:363-375.
    • (2011) Cell Host Microbe , vol.9 , pp. 363-375
    • Kerur, N.1    Veettil, M.V.2    Sharma-Walia, N.3    Bottero, V.4    Sadagopan, S.5    Otageri, P.6    Chandran, B.7
  • 26
    • 84862976171 scopus 로고    scopus 로고
    • Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16
    • Li T, Diner BA, Chen J, Cristea IM. 2012. Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16. Proc. Natl. Acad. Sci. U. S. A. 109:10558 -10563.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 10558-10563
    • Li, T.1    Diner, B.A.2    Chen, J.3    Cristea, I.M.4
  • 27
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • Fernandes-Alnemri T, Yu JW, Datta P, Wu J, Alnemri ES. 2009. AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 458:509 -513.
    • (2009) Nature , vol.458 , pp. 509-513
    • Fernandes-Alnemri, T.1    Yu, J.W.2    Datta, P.3    Wu, J.4    Alnemri, E.S.5
  • 32
    • 3543054546 scopus 로고    scopus 로고
    • Herpes simplex virus 1 has multiple mechanisms for blocking virus-induced interferon production
    • Melroe GT, DeLuca NA, Knipe DM. 2004. Herpes simplex virus 1 has multiple mechanisms for blocking virus-induced interferon production. J. Virol. 78:8411-8420.
    • (2004) J. Virol , vol.78 , pp. 8411-8420
    • Melroe, G.T.1    DeLuca, N.A.2    Knipe, D.M.3
  • 33
    • 33947627724 scopus 로고    scopus 로고
    • Recruitment of activated IRF-3 and CBP/p300 to herpes simplex virus ICP0 nuclear foci: Potential role in blocking IFN-beta induction
    • Melroe GT, Silva L, Schaffer PA, Knipe DM. 2007. Recruitment of activated IRF-3 and CBP/p300 to herpes simplex virus ICP0 nuclear foci: Potential role in blocking IFN-beta induction. Virology 360:305-321.
    • (2007) Virology , vol.360 , pp. 305-321
    • Melroe, G.T.1    Silva, L.2    Schaffer, P.A.3    Knipe, D.M.4
  • 34
    • 84868095535 scopus 로고    scopus 로고
    • Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein
    • Orzalli MH, Deluca NA, Knipe DM. 2012. Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein. Proc. Natl. Acad. Sci. U. S. A. 109:E3008 -3017.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109
    • Orzalli, M.H.1    Deluca, N.A.2    Knipe, D.M.3
  • 35
    • 0035919636 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 suppresses the interferon signaling pathway by inhibiting phosphorylation of STATs and Janus kinases during an early infection stage
    • Yokota S, Yokosawa N, Kubota T, Suzutani T, Yoshida I, Miura S, Jimbow K, Fujii N. 2001. Herpes simplex virus type 1 suppresses the interferon signaling pathway by inhibiting phosphorylation of STATs and Janus kinases during an early infection stage. Virology 286:119-124.
    • (2001) Virology , vol.286 , pp. 119-124
    • Yokota, S.1    Yokosawa, N.2    Kubota, T.3    Suzutani, T.4    Yoshida, I.5    Miura, S.6    Jimbow, K.7    Fujii, N.8
  • 36
    • 1842484070 scopus 로고    scopus 로고
    • Herpes simplex virus 1 gene products occlude the interferon signaling pathway at multiple sites
    • Chee AV, Roizman B. 2004. Herpes simplex virus 1 gene products occlude the interferon signaling pathway at multiple sites. J. Virol. 78:4185-4196.
    • (2004) J. Virol , vol.78 , pp. 4185-4196
    • Chee, A.V.1    Roizman, B.2
  • 37
    • 42649143255 scopus 로고    scopus 로고
    • Role for herpes simplex virus 1 ICP27 in the inhibition of type I interferon signaling
    • Johnson KE, Song B, Knipe DM. 2008. Role for herpes simplex virus 1 ICP27 in the inhibition of type I interferon signaling. Virology 374:487-494.
    • (2008) Virology , vol.374 , pp. 487-494
    • Johnson, K.E.1    Song, B.2    Knipe, D.M.3
  • 38
    • 0030793170 scopus 로고    scopus 로고
    • Suppression of the phenotype of γ1134.5 herpes simplex virus 1: failure of activated RNA-dependent protein kinase to shut off protein synthesis is associated with a deletion in the domain of the α47 gene
    • He B, Chou J, Brandimarti R, Mohr I, Gluzman Y, Roizman B. 1997. Suppression of the phenotype of γ1134.5 herpes simplex virus 1: failure of activated RNA-dependent protein kinase to shut off protein synthesis is associated with a deletion in the domain of the α47 gene. J. Virol. 71:6049-6054.
    • (1997) J. Virol , vol.71 , pp. 6049-6054
    • He, B.1    Chou, J.2    Brandimarti, R.3    Mohr, I.4    Gluzman, Y.5    Roizman, B.6
  • 39
    • 84873340673 scopus 로고    scopus 로고
    • HSV-1-induced chemokine expression via IFI16-dependent and IFI16-independent pathways in human monocyte-derived macrophages
    • doi: 10.1186/2042-4280-3-6
    • Soby S, Laursen RR, Ostergaard L, Melchjorsen J. 2012. HSV-1-induced chemokine expression via IFI16-dependent and IFI16-independent pathways in human monocyte-derived macrophages. Herpesviridae 3:6. doi: 10.1186/2042-4280-3-6.
    • (2012) Herpesviridae , vol.3 , Issue.2
    • Soby, S.1    Laursen, R.R.2    Ostergaard, L.3    Melchjorsen, J.4
  • 42
    • 34548490485 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha and interleukin-1 beta play a critical role in the resistance against lethal herpes simplex virus encephalitis
    • Sergerie Y, Rivest S, Boivin G. 2007. Tumor necrosis factor-alpha and interleukin-1 beta play a critical role in the resistance against lethal herpes simplex virus encephalitis. J. Infect. Dis. 196:853-860.
    • (2007) J. Infect. Dis , vol.196 , pp. 853-860
    • Sergerie, Y.1    Rivest, S.2    Boivin, G.3
  • 43
    • 0032981470 scopus 로고    scopus 로고
    • Interleukin-18 protects mice against acute herpes simplex virus type 1 infection
    • Fujioka N, Akazawa R, Ohashi K, Fujii M, Ikeda M, Kurimoto M. 1999. Interleukin-18 protects mice against acute herpes simplex virus type 1 infection. J. Virol. 73:2401-2409.
    • (1999) J. Virol , vol.73 , pp. 2401-2409
    • Fujioka, N.1    Akazawa, R.2    Ohashi, K.3    Fujii, M.4    Ikeda, M.5    Kurimoto, M.6
  • 44
    • 0019973281 scopus 로고
    • Definition of a series of stages in the association of two herpesviral proteins with the cell nucleus
    • Knipe DM, Spang AE. 1982. Definition of a series of stages in the association of two herpesviral proteins with the cell nucleus. J. Virol. 43:314-324.
    • (1982) J. Virol , vol.43 , pp. 314-324
    • Knipe, D.M.1    Spang, A.E.2
  • 45
    • 0031947861 scopus 로고    scopus 로고
    • Persistence and expression of the herpes simplex virus genome in the absence of immediateearly proteins
    • Samaniego LA, Neiderhiser L, DeLuca NA. 1998. Persistence and expression of the herpes simplex virus genome in the absence of immediateearly proteins. J. Virol. 72:3307-3320.
    • (1998) J. Virol , vol.72 , pp. 3307-3320
    • Samaniego, L.A.1    Neiderhiser, L.2    DeLuca, N.A.3
  • 46
    • 1842509993 scopus 로고    scopus 로고
    • Concurrent expression of latent and a limited number of lytic genes with immune modulation and antiapoptotic function by Kaposi's sarcoma-associated herpesvirus early during infection of primary endothelial and fibroblast cells and subsequent decline of lytic gene expression
    • Krishnan HH, Naranatt PP, Smith MS, Zeng L, Bloomer C, Chandran B. 2004. Concurrent expression of latent and a limited number of lytic genes with immune modulation and antiapoptotic function by Kaposi's sarcoma-associated herpesvirus early during infection of primary endothelial and fibroblast cells and subsequent decline of lytic gene expression. J. Virol. 78:3601-3620.
    • (2004) J. Virol , vol.78 , pp. 3601-3620
    • Krishnan, H.H.1    Naranatt, P.P.2    Smith, M.S.3    Zeng, L.4    Bloomer, C.5    Chandran, B.6
  • 47
    • 23244461927 scopus 로고    scopus 로고
    • ERK1/2 and MEK1/2 induced by Kaposi's sarcomaassociated herpesvirus (human herpesvirus 8) early during infection of target cells are essential for expression of viral genes and for establishment of infection
    • Sharma-Walia N, Krishnan HH, Naranatt PP, Zeng L, Smith MS, Chandran B. 2005. ERK1/2 and MEK1/2 induced by Kaposi's sarcomaassociated herpesvirus (human herpesvirus 8) early during infection of target cells are essential for expression of viral genes and for establishment of infection. J. Virol. 79:10308-10329.
    • (2005) J. Virol , vol.79 , pp. 10308-10329
    • Sharma-Walia, N.1    Krishnan, H.H.2    Naranatt, P.P.3    Zeng, L.4    Smith, M.S.5    Chandran, B.6
  • 48
    • 0023094009 scopus 로고
    • Antigenic crossreactions among herpes simplex virus types 1 and 2, Epstein-Barr virus, and cytomegalovirus
    • Balachandran N, Oba DE, Hutt-Fletcher LM. 1987. Antigenic crossreactions among herpes simplex virus types 1 and 2, Epstein-Barr virus, and cytomegalovirus. J. Virol. 61:1125-1135.
    • (1987) J. Virol , vol.61 , pp. 1125-1135
    • Balachandran, N.1    Oba, D.E.2    Hutt-Fletcher, L.M.3
  • 50
    • 1342310841 scopus 로고    scopus 로고
    • The roles of Rab27 and its effectors in the regulated secretory pathways
    • Izumi T, Gomi H, Kasai K, Mizutani S, Torii S. 2003. The roles of Rab27 and its effectors in the regulated secretory pathways. Cell Struct. Funct. 28:465-474.
    • (2003) Cell Struct. Funct , vol.28 , pp. 465-474
    • Izumi, T.1    Gomi, H.2    Kasai, K.3    Mizutani, S.4    Torii, S.5
  • 51
    • 36148964750 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 infection induces oxidative stress and the release of bioactive lipid peroxidation by-products in mouse P19N neural cell cultures
    • Kavouras JH, Prandovszky E, Valyi-Nagy K, Kovacs SK, Tiwari V, Kovacs M, Shukla D, Valyi-Nagy T. 2007. Herpes simplex virus type 1 infection induces oxidative stress and the release of bioactive lipid peroxidation by-products in mouse P19N neural cell cultures. J. Neurovirol. 13:416-425.
    • (2007) J. Neurovirol , vol.13 , pp. 416-425
    • Kavouras, J.H.1    Prandovszky, E.2    Valyi-Nagy, K.3    Kovacs, S.K.4    Tiwari, V.5    Kovacs, M.6    Shukla, D.7    Valyi-Nagy, T.8
  • 54
    • 84862279094 scopus 로고    scopus 로고
    • Preferential binding of IFI16 protein to cruciform structure and superhelical DNA
    • Brazda V, Coufal J, Liao JC, Arrowsmith CH. 2012. Preferential binding of IFI16 protein to cruciform structure and superhelical DNA. Biochem. Biophys. Res. Commun. 422:716-720.
    • (2012) Biochem. Biophys. Res. Commun , vol.422 , pp. 716-720
    • Brazda, V.1    Coufal, J.2    Liao, J.C.3    Arrowsmith, C.H.4
  • 55
    • 0032534802 scopus 로고    scopus 로고
    • A viral activator of gene expression functions via the ubiquitin-proteasome pathway
    • Everett RD, Orr A, Preston CM. 1998. A viral activator of gene expression functions via the ubiquitin-proteasome pathway. EMBO J. 17:7161-7169.
    • (1998) EMBO J , vol.17 , pp. 7161-7169
    • Everett, R.D.1    Orr, A.2    Preston, C.M.3
  • 56
    • 0033559253 scopus 로고    scopus 로고
    • Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110
    • Everett RD, Earnshaw WC, Findlay J, Lomonte P. 1999. Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110. EMBO J. 18: 1526-1538.
    • (1999) EMBO J , vol.18 , pp. 1526-1538
    • Everett, R.D.1    Earnshaw, W.C.2    Findlay, J.3    Lomonte, P.4
  • 57
    • 0035937114 scopus 로고    scopus 로고
    • Degradation of nucleosomeassociated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0
    • Lomonte P, Sullivan KF, Everett RD. 2001. Degradation of nucleosomeassociated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0. J. Biol. Chem. 276:5829-5835.
    • (2001) J. Biol. Chem , vol.276 , pp. 5829-5835
    • Lomonte, P.1    Sullivan, K.F.2    Everett, R.D.3
  • 58
    • 0033779805 scopus 로고    scopus 로고
    • Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins
    • Parkinson J, Everett RD. 2000. Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins. J. Virol. 74:10006-10017.
    • (2000) J. Virol , vol.74 , pp. 10006-10017
    • Parkinson, J.1    Everett, R.D.2
  • 59
    • 0032889431 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein Vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase
    • Parkinson J, Lees-Miller SP, Everett RD. 1999. Herpes simplex virus type 1 immediate-early protein Vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase. J. Virol. 73:650-657.
    • (1999) J. Virol , vol.73 , pp. 650-657
    • Parkinson, J.1    Lees-Miller, S.P.2    Everett, R.D.3
  • 60
    • 79959848568 scopus 로고    scopus 로고
    • The intrinsic antiviral defense to incoming HSV-1 genomes includes specificDNArepair proteins and is counteracted by the viral protein ICP0
    • 7:e1002084. doi:10.1371/journal.ppat.1002084
    • Lilley CE, Chaurushiya MS, Boutell C, Everett RD, Weitzman MD. 2011 The intrinsic antiviral defense to incoming HSV-1 genomes includes specificDNArepair proteins and is counteracted by the viral protein ICP0. PLoS Pathog. 7:e1002084. doi:10.1371/journal.ppat.1002084.
    • (2011) PLoS Pathog
    • Lilley, C.E.1    Chaurushiya, M.S.2    Boutell, C.3    Everett, R.D.4    Weitzman, M.D.5
  • 61
    • 41149153281 scopus 로고    scopus 로고
    • Cellular proteasome activity facilitates herpes simplex virus entry at a postpenetration step
    • Delboy MG, Roller DG, Nicola AV. 2008. Cellular proteasome activity facilitates herpes simplex virus entry at a postpenetration step. J. Virol. 82:3381-3390.
    • (2008) J. Virol , vol.82 , pp. 3381-3390
    • Delboy, M.G.1    Roller, D.G.2    Nicola, A.V.3
  • 62
    • 33845604018 scopus 로고    scopus 로고
    • Antiviral activity of proteasome inhibitors in herpes simplex virus-1 infection: role of nuclear factor-kB
    • La Frazia S, Amici C, Santoro MG. 2006. Antiviral activity of proteasome inhibitors in herpes simplex virus-1 infection: role of nuclear factor-kB. Antivir. Ther. 11:995-1004.
    • (2006) Antivir. Ther , vol.11 , pp. 995-1004
    • La Frazia, S.1    Amici, C.2    Santoro, M.G.3
  • 63
    • 67651172779 scopus 로고    scopus 로고
    • Dynamics of macrophage polarization reveal new mechanism to inhibit IL-1β release through pyrophosphates
    • Pelegrin P, Surprenant A. 2009. Dynamics of macrophage polarization reveal new mechanism to inhibit IL-1β release through pyrophosphates. EMBO J. 28:2114-2127.
    • (2009) EMBO J , vol.28 , pp. 2114-2127
    • Pelegrin, P.1    Surprenant, A.2
  • 64
    • 0022658383 scopus 로고
    • Organization of cytoskeleton elements during herpes simplex virus type 1 infection of human fibroblasts: an immunofluorescence study
    • Norrild B, Lehto VP, Virtanen I. 1986. Organization of cytoskeleton elements during herpes simplex virus type 1 infection of human fibroblasts: an immunofluorescence study. J. Gen. Virol. 67:97-105.
    • (1986) J. Gen. Virol , vol.67 , pp. 97-105
    • Norrild, B.1    Lehto, V.P.2    Virtanen, I.3
  • 65
    • 0022526952 scopus 로고
    • Involvement of actincontaining microfilaments in HSV-induced cytopathology and the influence of inhibitors of glycosylation
    • Heeg U, Dienes HP, Muller S, Falke D. 1986. Involvement of actincontaining microfilaments in HSV-induced cytopathology and the influence of inhibitors of glycosylation. Arch. Virol. 91:257-270.
    • (1986) Arch. Virol , vol.91 , pp. 257-270
    • Heeg, U.1    Dienes, H.P.2    Muller, S.3    Falke, D.4
  • 66
    • 71949107259 scopus 로고    scopus 로고
    • Viral entry mechanisms: cellular and viral mediators of herpes simplex virus entry
    • Akhtar J, Shukla D. 2009. Viral entry mechanisms: cellular and viral mediators of herpes simplex virus entry. FEBS J. 276:7228-7236.
    • (2009) FEBS J , vol.276 , pp. 7228-7236
    • Akhtar, J.1    Shukla, D.2
  • 67
    • 80055045773 scopus 로고    scopus 로고
    • IFI16 protein mediates the anti-inflammatory actions of the type-I interferons through suppression of activation of caspase-1 by inflammasomes
    • 6:e27040. doi:10.1371/journal.pone.0027040.
    • Veeranki S, Duan X, Panchanathan R, Liu H, Choubey D. 2011. IFI16 protein mediates the anti-inflammatory actions of the type-I interferons through suppression of activation of caspase-1 by inflammasomes. PLoS One 6:e27040. doi:10.1371/journal.pone.0027040.
    • (2011) PLoS One
    • Veeranki, S.1    Duan, X.2    Panchanathan, R.3    Liu, H.4    Choubey, D.5
  • 69
    • 0027435961 scopus 로고
    • Demonstration of circularization of herpes simplex virus DNA following infection using pulsed field gel electrophoresis
    • Garber DA, Beverley SM, Coen DM. 1993. Demonstration of circularization of herpes simplex virus DNA following infection using pulsed field gel electrophoresis. Virology 197:459-462.
    • (1993) Virology , vol.197 , pp. 459-462
    • Garber, D.A.1    Beverley, S.M.2    Coen, D.M.3
  • 70
    • 57349146688 scopus 로고    scopus 로고
    • Herpes simplex virus ICP0 promotes both histone removal and acetylation on viral DNA during lytic infection
    • Cliffe AR, Knipe DM. 2008. Herpes simplex virus ICP0 promotes both histone removal and acetylation on viral DNA during lytic infection. J. Virol. 82:12030-12038.
    • (2008) J. Virol , vol.82 , pp. 12030-12038
    • Cliffe, A.R.1    Knipe, D.M.2
  • 71
    • 0029153276 scopus 로고
    • The interferon-inducible autoantigen, IFI 16: localization to the nucleolus and identification of a DNA-binding domain
    • Dawson MJ, Trapani JA. 1995. The interferon-inducible autoantigen, IFI
    • (1995) Biochem. Biophys. Res. Commun , vol.214 , pp. 152-162
    • Dawson, M.J.1    Trapani, J.A.2
  • 72
    • 0034619772 scopus 로고    scopus 로고
    • Functional interaction between p53 and the interferon-inducible nucleoprotein IFI 16
    • Johnstone RW, Wei W, Greenway A, Trapani JA. 2000. Functional interaction between p53 and the interferon-inducible nucleoprotein IFI 16. Oncogene 19:6033-6042.
    • (2000) Oncogene , vol.19 , pp. 6033-6042
    • Johnstone, R.W.1    Wei, W.2    Greenway, A.3    Trapani, J.A.4
  • 74
    • 84876345677 scopus 로고    scopus 로고
    • DNA sensingindependent inhibition of herpes simplex virus type-1 replication by DAI/ ZBP1
    • Pham TH, Kwon KM, Kim YE, Kim KK, Ahn JH. 2013. DNA sensingindependent inhibition of herpes simplex virus type-1 replication by DAI/ ZBP1. J. Virol. 87:3076-3086.
    • (2013) J. Virol , vol.87 , pp. 3076-3086
    • Pham, T.H.1    Kwon, K.M.2    Kim, Y.E.3    Kim, K.K.4    Ahn, J.H.5
  • 75
    • 79955961661 scopus 로고    scopus 로고
    • Varicella-zoster virus infection triggers formation of an interleukin-1β (IL-1β)-processing inflammasome complex
    • Nour AM, Reichelt M, Ku CC, Ho MY, Heineman TC, Arvin AM. 2011. Varicella-zoster virus infection triggers formation of an interleukin-1β (IL-1β)-processing inflammasome complex. J. Biol. Chem. 286:17921-17933.
    • (2011) J. Biol. Chem , vol.286 , pp. 17921-17933
    • Nour, A.M.1    Reichelt, M.2    Ku, C.C.3    Ho, M.Y.4    Heineman, T.C.5    Arvin, A.M.6
  • 76
    • 0001642851 scopus 로고
    • The etiologic agents of varicella and herpes zoster; isolation, propagation, and cultural characteristics in vitro
    • Weller TH, Witton HM, Bell EJ. 1958. The etiologic agents of varicella and herpes zoster; isolation, propagation, and cultural characteristics in vitro. J. Exp. Med. 108:843-868.
    • (1958) J. Exp. Med , vol.108 , pp. 843-868
    • Weller, T.H.1    Witton, H.M.2    Bell, E.J.3
  • 78
    • 0035082275 scopus 로고    scopus 로고
    • Requirements for the nuclearcytoplasmic translocation of infected-cell protein 0 of herpes simplex virus 1
    • Lopez P, Van Sant C, Roizman B. 2001. Requirements for the nuclearcytoplasmic translocation of infected-cell protein 0 of herpes simplex virus 1. J. Virol. 75:3832-3840.
    • (2001) J. Virol , vol.75 , pp. 3832-3840
    • Lopez, P.1    Van Sant, C.2    Roizman, B.3
  • 79
    • 77749319322 scopus 로고    scopus 로고
    • ICP0 antagonizes ICP4-dependent silencing of the herpes simplex virus ICP0 gene
    • 5:e8837. doi:10.1371/journal.pone.0008837.
    • Liu M, Rakowski B, Gershburg E, Weisend CM, Lucas O, Schmidt EE, Halford WP. 2010. ICP0 antagonizes ICP4-dependent silencing of the herpes simplex virus ICP0 gene. PLoS One 5:e8837. doi:10.1371/journal.pone.0008837.
    • (2010) PLoS One
    • Liu, M.1    Rakowski, B.2    Gershburg, E.3    Weisend, C.M.4    Lucas, O.5    Schmidt, E.E.6    Halford, W.P.7
  • 80
    • 45149095793 scopus 로고    scopus 로고
    • Hsc70 focus formation at the periphery of HSV-1 transcription sites requires ICP27
    • 3:e1491. doi:10.1371/journal.pone.0001491.
    • Li L, Johnson LA, Dai-Ju JQ, Sandri-Goldin RM. 2008. Hsc70 focus formation at the periphery of HSV-1 transcription sites requires ICP27. PLoS One 3:e1491. doi:10.1371/journal.pone.0001491.
    • (2008) PLoS One
    • Li, L.1    Johnson, L.A.2    Dai-Ju, J.Q.3    Sandri-Goldin, R.M.4
  • 81
    • 84858142724 scopus 로고    scopus 로고
    • HECT and RING finger families of E3 ubiquitin ligases at a glance
    • Metzger MB, Hristova VA, Weissman AM. 2012. HECT and RING finger families of E3 ubiquitin ligases at a glance. J. Cell Sci. 125:531-537.
    • (2012) J. Cell Sci , vol.125 , pp. 531-537
    • Metzger, M.B.1    Hristova, V.A.2    Weissman, A.M.3
  • 82
    • 30044437590 scopus 로고    scopus 로고
    • Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases
    • Ozkan E, Yu H, Deisenhofer J. 2005. Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases. Proc. Natl. Acad. Sci. U. S. A. 102:18890-18895.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18890-18895
    • Ozkan, E.1    Yu, H.2    Deisenhofer, J.3
  • 83
    • 77954485440 scopus 로고    scopus 로고
    • Human cytomegalovirus pUL83 stimulates activity of the viral immediate-early promoter through its interaction with the cellular IFI16 protein
    • Cristea IM, Moorman NJ, Terhune SS, Cuevas CD, O'Keefe ES, Rout MP, Chait BT, Shenk T. 2010. Human cytomegalovirus pUL83 stimulates activity of the viral immediate-early promoter through its interaction with the cellular IFI16 protein. J. Virol. 84:7803-7814.
    • (2010) J. Virol , vol.84 , pp. 7803-7814
    • Cristea, I.M.1    Moorman, N.J.2    Terhune, S.S.3    Cuevas, C.D.4    O'Keefe, E.S.5    Rout, M.P.6    Chait, B.T.7    Shenk, T.8
  • 84
    • 84875506475 scopus 로고    scopus 로고
    • Alphaherpesviral US3 kinase induces cofilin dephosphorylation to reorganize the actin cytoskeleton
    • 30 January, doi:10.1128/JVI.03107-12.
    • Jacob T, Van den Broeke C, van Troys M, Waterschoot D, Ampe C, Favoreel HW. 30 January 2013. Alphaherpesviral US3 kinase induces cofilin dephosphorylation to reorganize the actin cytoskeleton. J. Virol. doi:10.1128/JVI.03107-12.
    • (2013) J. Virol
    • Jacob, T.1    Van den Broeke, C.2    Van Troys, M.3    Waterschoot, D.4    Ampe, C.5    Favoreel, H.W.6
  • 85
    • 33746190699 scopus 로고    scopus 로고
    • Functional genomic analysis of herpes simplex virus type 1 counteraction of the host innate response
    • Pasieka TJ, Baas T, Carter VS, Proll SC, Katze MG, Leib DA. 2006. Functional genomic analysis of herpes simplex virus type 1 counteraction of the host innate response. J. Virol. 80:7600-7612.
    • (2006) J. Virol , vol.80 , pp. 7600-7612
    • Pasieka, T.J.1    Baas, T.2    Carter, V.S.3    Proll, S.C.4    Katze, M.G.5    Leib, D.A.6
  • 86
    • 0033919629 scopus 로고    scopus 로고
    • The role of the UL41 gene of herpes simplex virus type 1 in evasion of non-specific host defence mechanisms during primary infection
    • Suzutani T, Nagamine M, Shibaki T, Ogasawara M, Yoshida I, Daikoku T, Nishiyama Y, Azuma M. 2000. The role of the UL41 gene of herpes simplex virus type 1 in evasion of non-specific host defence mechanisms during primary infection. J. Gen. Virol. 81:1763-1771.
    • (2000) J. Gen. Virol , vol.81 , pp. 1763-1771
    • Suzutani, T.1    Nagamine, M.2    Shibaki, T.3    Ogasawara, M.4    Yoshida, I.5    Daikoku, T.6    Nishiyama, Y.7    Azuma, M.8
  • 87
    • 84869232621 scopus 로고    scopus 로고
    • Global secretome characterization of herpes simplex virus 1-infected human primary macrophages
    • Miettinen JJ, Matikainen S, Nyman TA. 2012. Global secretome characterization of herpes simplex virus 1-infected human primary macrophages. J. Virol. 86:12770-12778.
    • (2012) J. Virol , vol.86 , pp. 12770-12778
    • Miettinen, J.J.1    Matikainen, S.2    Nyman, T.A.3
  • 88
    • 77956845138 scopus 로고    scopus 로고
    • Myosin Va enhances secretion of herpes simplex virus 1 virions and cell surface expression of viral glycoproteins
    • Roberts KL, Baines JD. 2010. Myosin Va enhances secretion of herpes simplex virus 1 virions and cell surface expression of viral glycoproteins. J. Virol. 84:9889-9896.
    • (2010) J. Virol , vol.84 , pp. 9889-9896
    • Roberts, K.L.1    Baines, J.D.2
  • 89
    • 84868587398 scopus 로고    scopus 로고
    • Endocytic tubules regulated by Rab GTPases 5 and 11 are used for envelopment of herpes simplex virus
    • Hollinshead M, Johns HL, Sayers CL, Gonzalez-Lopez C, Smith GL, Elliott G. 2012. Endocytic tubules regulated by Rab GTPases 5 and 11 are used for envelopment of herpes simplex virus. EMBO J. 31:4204-4220.
    • (2012) EMBO J , vol.31 , pp. 4204-4220
    • Hollinshead, M.1    Johns, H.L.2    Sayers, C.L.3    Gonzalez-Lopez, C.4    Smith, G.L.5    Elliott, G.6
  • 90
    • 84869110305 scopus 로고    scopus 로고
    • Role of the small GTPase Rab27a during Herpes simplex virus infection of oligodendrocytic cells
    • doi:10.1186/1471-2180-12-265.
    • Bello-Morales R, Crespillo AJ, Fraile-Ramos A, Tabares E, Alcina A, Lopez-Guerrero JA. 2012. Role of the small GTPase Rab27a during Herpes simplex virus infection of oligodendrocytic cells. BMC Microbiol. 12: 265. doi:10.1186/1471-2180-12-265.
    • (2012) BMC Microbiol , vol.12 , pp. 265
    • Bello-Morales, R.1    Crespillo, A.J.2    Fraile-Ramos, A.3    Tabares, E.4    Alcina, A.5    Lopez-Guerrero, J.A.6


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