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Volumn 426, Issue 6, 2014, Pages 1133-1147

Recognition of herpes simplex viruses: Toll-like receptors and beyond

Author keywords

cytokine; herpes simplex virus; innate immunity; interferon; Toll like receptor

Indexed keywords

DNA DIRECTED RNA POLYMERASE III; INFLAMMASOME; INTERFERON REGULATORY FACTOR; KU ANTIGEN; PROTEIN US11; RETINOIC ACID INDUCIBLE PROTEIN I; RNA HELICASE; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 9;

EID: 84894550575     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.11.012     Document Type: Review
Times cited : (86)

References (147)
  • 1
    • 0035849323 scopus 로고    scopus 로고
    • Herpes simplex virus infections
    • R.J. Whitley, and B. Roizman Herpes simplex virus infections Lancet 357 2001 1513
    • (2001) Lancet , vol.357 , pp. 1513
    • Whitley, R.J.1    Roizman, B.2
  • 4
    • 84858000941 scopus 로고    scopus 로고
    • Sensing herpes: More than toll
    • J. Melchjorsen Sensing herpes: more than toll Rev Med Virol 22 2011 106 121
    • (2011) Rev Med Virol , vol.22 , pp. 106-121
    • Melchjorsen, J.1
  • 5
    • 53349168904 scopus 로고    scopus 로고
    • The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation
    • B. Zhong, Y. Yang, S. Li, Y.-Y. Wang, Y. Li, and F. Diao et al. The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation Immunity 29 2008 538 550
    • (2008) Immunity , vol.29 , pp. 538-550
    • Zhong, B.1    Yang, Y.2    Li, S.3    Wang, Y.-Y.4    Li, Y.5    Diao, F.6
  • 6
    • 66649109939 scopus 로고    scopus 로고
    • ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization
    • W. Sun, Y. Li, L. Chen, H. Chen, F. You, and X. Zhou et al. ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization Proc Natl Acad Sci 106 2009 8653 8658
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 8653-8658
    • Sun, W.1    Li, Y.2    Chen, L.3    Chen, H.4    You, F.5    Zhou, X.6
  • 7
    • 84876334378 scopus 로고    scopus 로고
    • Herpes simplex virus 1 infection induces activation and subsequent inhibition of the IFI16 and NLRP3 inflammasomes
    • K.E. Johnson, L. Chikoti, and B. Chandran Herpes simplex virus 1 infection induces activation and subsequent inhibition of the IFI16 and NLRP3 inflammasomes J Virol 87 2013 5005 5018
    • (2013) J Virol , vol.87 , pp. 5005-5018
    • Johnson, K.E.1    Chikoti, L.2    Chandran, B.3
  • 8
    • 37049010982 scopus 로고    scopus 로고
    • Type i interferon production during herpes simplex virus infection is controlled by cell-type-specific viral recognition through Toll-like receptor 9, the mitochondrial antiviral signaling protein pathway, and novel recognition systems
    • S.B. Rasmussen, L.N. Sorensen, L. Malmgaard, N. Ank, J.D. Baines, and Z.J. Chen et al. Type I interferon production during herpes simplex virus infection is controlled by cell-type-specific viral recognition through Toll-like receptor 9, the mitochondrial antiviral signaling protein pathway, and novel recognition systems J Virol 81 2007 13315 13324
    • (2007) J Virol , vol.81 , pp. 13315-13324
    • Rasmussen, S.B.1    Sorensen, L.N.2    Malmgaard, L.3    Ank, N.4    Baines, J.D.5    Chen, Z.J.6
  • 9
    • 3843103508 scopus 로고    scopus 로고
    • Herpes simplex virus type-1 induces IFN-(alpha) production via Toll-like receptor 9-dependent and -independent pathways
    • H. Hochrein, B. Schlatter, M. O'Keeffe, C. Wagner, F. Schmitz, and M. Schiemann et al. Herpes simplex virus type-1 induces IFN-(alpha) production via Toll-like receptor 9-dependent and -independent pathways Proc Natl Acad Sci 101 2004 11416 11421
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 11416-11421
    • Hochrein, H.1    Schlatter, B.2    O'Keeffe, M.3    Wagner, C.4    Schmitz, F.5    Schiemann, M.6
  • 10
    • 33751585824 scopus 로고    scopus 로고
    • The IFN-independent response to virus particle entry provides a first line of antiviral defense that is independent of TLRs and retinoic acid-inducible gene i
    • P. Paladino, D.T. Cummings, R.S. Noyce, and K.L. Mossman The IFN-independent response to virus particle entry provides a first line of antiviral defense that is independent of TLRs and retinoic acid-inducible gene I J Immunol 177 2006 8008 8016
    • (2006) J Immunol , vol.177 , pp. 8008-8016
    • Paladino, P.1    Cummings, D.T.2    Noyce, R.S.3    Mossman, K.L.4
  • 12
    • 70349235719 scopus 로고    scopus 로고
    • Mechanisms employed by herpes simplex virus 1 to inhibit the interferon response
    • P. Paladino, and K.L. Mossman Mechanisms employed by herpes simplex virus 1 to inhibit the interferon response J Interferon Cytokine Res 29 2009 599 608
    • (2009) J Interferon Cytokine Res , vol.29 , pp. 599-608
    • Paladino, P.1    Mossman, K.L.2
  • 13
    • 0742324860 scopus 로고    scopus 로고
    • TLR signaling pathways
    • K. Takeda, and S. Akira TLR signaling pathways Semin Immunol 16 2004 3 9
    • (2004) Semin Immunol , vol.16 , pp. 3-9
    • Takeda, K.1    Akira, S.2
  • 14
    • 31344461659 scopus 로고    scopus 로고
    • Innate immune recognition of viral infection
    • T. Kawai, and S. Akira Innate immune recognition of viral infection Nat Immunol 7 2006 131
    • (2006) Nat Immunol , vol.7 , pp. 131
    • Kawai, T.1    Akira, S.2
  • 15
    • 33748064991 scopus 로고    scopus 로고
    • Toll-like receptors, innate immunity and HSV pathogenesis
    • M.M. Herbst-Kralovetz, and R.B. Pyles Toll-like receptors, innate immunity and HSV pathogenesis Herpes 13 2006 37 41
    • (2006) Herpes , vol.13 , pp. 37-41
    • Herbst-Kralovetz, M.M.1    Pyles, R.B.2
  • 16
    • 33748696772 scopus 로고    scopus 로고
    • The role of Toll-like receptors in CNS response to microbial challenge
    • G.W. Konat, T. Kielian, and I. Marriott The role of Toll-like receptors in CNS response to microbial challenge J Neurochem 99 2006 1 12
    • (2006) J Neurochem , vol.99 , pp. 1-12
    • Konat, G.W.1    Kielian, T.2    Marriott, I.3
  • 17
    • 35649003133 scopus 로고    scopus 로고
    • Toll-like receptors in defense and damage of the central nervous system
    • R. Aravalli, P. Peterson, and J. Lokensgard Toll-like receptors in defense and damage of the central nervous system J Neuroimmune Pharmacol 2 2007 297
    • (2007) J Neuroimmune Pharmacol , vol.2 , pp. 297
    • Aravalli, R.1    Peterson, P.2    Lokensgard, J.3
  • 18
    • 84864010826 scopus 로고    scopus 로고
    • Herpes simplex virus glycoproteins gH/gL and gB bind Toll-like receptor 2, and soluble gH/gL is sufficient to activate NF-κB
    • V. Leoni, T. Gianni, S. Salvioli, and G. Campadelli-Fiume Herpes simplex virus glycoproteins gH/gL and gB bind Toll-like receptor 2, and soluble gH/gL is sufficient to activate NF-κB J Virol 86 2012 6555 6562
    • (2012) J Virol , vol.86 , pp. 6555-6562
    • Leoni, V.1    Gianni, T.2    Salvioli, S.3    Campadelli-Fiume, G.4
  • 20
    • 84873810684 scopus 로고    scopus 로고
    • The herpes simplex virus 1-encoded envelope glycoprotein B activates NF-κB through the Toll-like receptor 2 and MyD88/TRAF6-dependent signaling pathway
    • M. Cai, M. Li, K. Wang, S. Wang, Q. Lu, and J. Yan et al. The herpes simplex virus 1-encoded envelope glycoprotein B activates NF-κB through the Toll-like receptor 2 and MyD88/TRAF6-dependent signaling pathway PLoS One 8 2013 e54586
    • (2013) PLoS One , vol.8 , pp. 54586
    • Cai, M.1    Li, M.2    Wang, K.3    Wang, S.4    Lu, Q.5    Yan, J.6
  • 21
    • 0842342607 scopus 로고    scopus 로고
    • Herpes simplex virus 1 interaction with Toll-like receptor 2 contributes to lethal encephalitis
    • E.A. Kurt-Jones, M. Chan, S. Zhou, J. Wang, G. Reed, and R. Bronson et al. Herpes simplex virus 1 interaction with Toll-like receptor 2 contributes to lethal encephalitis Proc Natl Acad Sci 101 2004 1315 1320
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 1315-1320
    • Kurt-Jones, E.A.1    Chan, M.2    Zhou, S.3    Wang, J.4    Reed, G.5    Bronson, R.6
  • 22
    • 25444448498 scopus 로고    scopus 로고
    • Cutting edge: TLR2-mediated proinflammatory cytokine and chemokine production by microglial cells in response to herpes simplex virus
    • R.N. Aravalli, S. Hu, T.N. Rowen, J.M. Palmquist, and J.R. Lokensgard Cutting edge: TLR2-mediated proinflammatory cytokine and chemokine production by microglial cells in response to herpes simplex virus J Immunol 175 2005 4189 4193
    • (2005) J Immunol , vol.175 , pp. 4189-4193
    • Aravalli, R.N.1    Hu, S.2    Rowen, T.N.3    Palmquist, J.M.4    Lokensgard, J.R.5
  • 23
    • 35148828516 scopus 로고    scopus 로고
    • Innate recognition network driving herpes simplex virus-induced corneal immunopathology: Role of the Toll pathway in early inflammatory events in stromal keratitis
    • P.P. Sarangi, B. Kim, E. Kurt-Jones, and B.T. Rouse Innate recognition network driving herpes simplex virus-induced corneal immunopathology: role of the Toll pathway in early inflammatory events in stromal keratitis J Virol 81 2007 11128 11138
    • (2007) J Virol , vol.81 , pp. 11128-11138
    • Sarangi, P.P.1    Kim, B.2    Kurt-Jones, E.3    Rouse, B.T.4
  • 24
    • 34547622158 scopus 로고    scopus 로고
    • Polymorphisms in TLR2 are associated with increased viral shedding and lesional rate in patients with genital herpes simplex virus type 2 infection
    • P.-Y. Bochud, A.S. Magaret, D.M. Koelle, A. Aderem, and A. Wald Polymorphisms in TLR2 are associated with increased viral shedding and lesional rate in patients with genital herpes simplex virus type 2 infection J Infect Dis 196 2007 505 509
    • (2007) J Infect Dis , vol.196 , pp. 505-509
    • Bochud, P.-Y.1    Magaret, A.S.2    Koelle, D.M.3    Aderem, A.4    Wald, A.5
  • 25
    • 33751206873 scopus 로고    scopus 로고
    • Dual recognition of herpes simplex viruses by TLR2 and TLR9 in dendritic cells
    • A. Sato, M.M. Linehan, and A. Iwasaki Dual recognition of herpes simplex viruses by TLR2 and TLR9 in dendritic cells Proc Natl Acad Sci 103 2006 17343 17348
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 17343-17348
    • Sato, A.1    Linehan, M.M.2    Iwasaki, A.3
  • 27
    • 78149347709 scopus 로고    scopus 로고
    • Toll-like receptor (TLR) 2 and TLR9 expressed in trigeminal ganglia are critical to viral control during herpes simplex virus 1 infection
    • G.K. Lima, G.P. Zolini, D.S. Mansur, B.H. Freire Lima, U. Wischhoff, and R.G. Astigarraga et al. Toll-like receptor (TLR) 2 and TLR9 expressed in trigeminal ganglia are critical to viral control during herpes simplex virus 1 infection Am J Pathol 177 2010 2433 2445
    • (2010) Am J Pathol , vol.177 , pp. 2433-2445
    • Lima, G.K.1    Zolini, G.P.2    Mansur, D.S.3    Freire Lima, B.H.4    Wischhoff, U.5    Astigarraga, R.G.6
  • 28
    • 0016795964 scopus 로고
    • RNA synthesis in cells infected with herpes simplex virus. X. Properties of viral symmetric transcripts and of double-stranded RNA prepared from them
    • B. Jacquemont, and B. Roizman RNA synthesis in cells infected with herpes simplex virus. X. Properties of viral symmetric transcripts and of double-stranded RNA prepared from them J Virol 15 1975 707 713
    • (1975) J Virol , vol.15 , pp. 707-713
    • Jacquemont, B.1    Roizman, B.2
  • 29
    • 33646453915 scopus 로고    scopus 로고
    • Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses
    • F. Weber, V. Wagner, S.B. Rasmussen, R. Hartmann, and S.R. Paludan Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses J Virol 80 2006 5059 5064
    • (2006) J Virol , vol.80 , pp. 5059-5064
    • Weber, F.1    Wagner, V.2    Rasmussen, S.B.3    Hartmann, R.4    Paludan, S.R.5
  • 30
    • 80555144890 scopus 로고    scopus 로고
    • Herpes simplex virus encephalitis in a patient with complete TLR3 deficiency: TLR3 is otherwise redundant in protective immunity
    • Y. Guo, M. Audry, M. Ciancanelli, L. Alsina, J. Azevedo, and M. Herman et al. Herpes simplex virus encephalitis in a patient with complete TLR3 deficiency: TLR3 is otherwise redundant in protective immunity J Exp Med 208 2011 2083 2098
    • (2011) J Exp Med , vol.208 , pp. 2083-2098
    • Guo, Y.1    Audry, M.2    Ciancanelli, M.3    Alsina, L.4    Azevedo, J.5    Herman, M.6
  • 31
  • 32
  • 33
    • 77951935483 scopus 로고    scopus 로고
    • Cutting edge: Priming of CD8 T cell immunity to herpes simplex virus type 1 requires cognate TLR3 expression in vivo
    • G.M. Davey, M. Wojtasiak, A.I. Proietto, F.R. Carbone, W.R. Heath, and S. Bedoui Cutting edge: priming of CD8 T cell immunity to herpes simplex virus type 1 requires cognate TLR3 expression in vivo J Immunol 184 2010 2243 2246
    • (2010) J Immunol , vol.184 , pp. 2243-2246
    • Davey, G.M.1    Wojtasiak, M.2    Proietto, A.I.3    Carbone, F.R.4    Heath, W.R.5    Bedoui, S.6
  • 34
    • 84859716889 scopus 로고    scopus 로고
    • TLR3 deficiency renders astrocytes permissive to herpes simplex virus infection and facilitates establishment of CNS infection in mice
    • L.S. Reinert, L. Harder, C.K. Holm, M.B. Iversen, K.A. Horan, and F. Dagnaes-Hansen et al. TLR3 deficiency renders astrocytes permissive to herpes simplex virus infection and facilitates establishment of CNS infection in mice J Clin Invest 122 2012 1368 1376
    • (2012) J Clin Invest , vol.122 , pp. 1368-1376
    • Reinert, L.S.1    Harder, L.2    Holm, C.K.3    Iversen, M.B.4    Horan, K.A.5    Dagnaes-Hansen, F.6
  • 35
    • 9144257930 scopus 로고    scopus 로고
    • Viral activation of macrophages through TLR-dependent and -independent pathways
    • L. Malmgaard, J. Melchjorsen, A.G. Bowie, S.C. Mogensen, and S.R. Paludan Viral activation of macrophages through TLR-dependent and -independent pathways J Immunol 173 2004 6890 6898
    • (2004) J Immunol , vol.173 , pp. 6890-6898
    • Malmgaard, L.1    Melchjorsen, J.2    Bowie, A.G.3    Mogensen, S.C.4    Paludan, S.R.5
  • 36
    • 77957018085 scopus 로고    scopus 로고
    • Human TRAF3 adaptor molecule deficiency leads to impaired Toll-like receptor 3 response and susceptibility to herpes simplex encephalitis
    • R. Pérez de Diego, V. Sancho-Shimizu, L. Lorenzo, A. Puel, S. Plancoulaine, and C. Picard et al. Human TRAF3 adaptor molecule deficiency leads to impaired Toll-like receptor 3 response and susceptibility to herpes simplex encephalitis Immunity 33 2010 400 411
    • (2010) Immunity , vol.33 , pp. 400-411
    • Pérez De Diego, R.1    Sancho-Shimizu, V.2    Lorenzo, L.3    Puel, A.4    Plancoulaine, S.5    Picard, C.6
  • 38
    • 84866393226 scopus 로고    scopus 로고
    • Heterozygous TBK1 mutations impair TLR3 immunity and underlie herpes simplex encephalitis of childhood
    • M. Herman, M. Ciancanelli, Y.-H. Ou, L. Lorenzo, M. Klaudel-Dreszler, and E. Pauwels et al. Heterozygous TBK1 mutations impair TLR3 immunity and underlie herpes simplex encephalitis of childhood J Exp Med 209 2012 1567 1582
    • (2012) J Exp Med , vol.209 , pp. 1567-1582
    • Herman, M.1    Ciancanelli, M.2    Ou, Y.-H.3    Lorenzo, L.4    Klaudel-Dreszler, M.5    Pauwels, E.6
  • 39
    • 0042123694 scopus 로고    scopus 로고
    • Toll-like receptor 9-mediated recognition of herpes simplex virus-2 by plasmacytoid dendritic cells
    • J. Lund, A. Sato, S. Akira, R. Medzhitov, and A. Iwasaki Toll-like receptor 9-mediated recognition of herpes simplex virus-2 by plasmacytoid dendritic cells J Exp Med 198 2003 513 520
    • (2003) J Exp Med , vol.198 , pp. 513-520
    • Lund, J.1    Sato, A.2    Akira, S.3    Medzhitov, R.4    Iwasaki, A.5
  • 40
    • 0842328805 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 activates murine natural interferon-producing cells through toll-like receptor 9
    • A. Krug, G.D. Luker, W. Barchet, D.A. Leib, S. Akira, and M. Colonna Herpes simplex virus type 1 activates murine natural interferon-producing cells through toll-like receptor 9 Blood 103 2004 1433 1437
    • (2004) Blood , vol.103 , pp. 1433-1437
    • Krug, A.1    Luker, G.D.2    Barchet, W.3    Leib, D.A.4    Akira, S.5    Colonna, M.6
  • 41
    • 77950822768 scopus 로고    scopus 로고
    • Expression of type III interferon (IFN) in the vaginal mucosa is mediated primarily by dendritic cells and displays stronger dependence on NF-κB than type i IFNs
    • M.B. Iversen, N. Ank, J. Melchjorsen, and S.R. Paludan Expression of type III interferon (IFN) in the vaginal mucosa is mediated primarily by dendritic cells and displays stronger dependence on NF-κB than type I IFNs J Virol 84 2010 4579 4586
    • (2010) J Virol , vol.84 , pp. 4579-4586
    • Iversen, M.B.1    Ank, N.2    Melchjorsen, J.3    Paludan, S.R.4
  • 42
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • O. Takeuchi, and S. Akira Pattern recognition receptors and inflammation Cell 140 2010 805 820
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 43
    • 46949097299 scopus 로고    scopus 로고
    • Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5
    • H. Kato, O. Takeuchi, E. Mikamo-Satoh, R. Hirai, T. Kawai, and K. Matsushita et al. Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5 J Exp Med 205 2008 1601 1610
    • (2008) J Exp Med , vol.205 , pp. 1601-1610
    • Kato, H.1    Takeuchi, O.2    Mikamo-Satoh, E.3    Hirai, R.4    Kawai, T.5    Matsushita, K.6
  • 45
    • 33750984771 scopus 로고    scopus 로고
    • RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates
    • A. Pichlmair, O. Schulz, C.P. Tan, T.I. Naslund, P. Liljestrom, and F. Weber et al. RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates Science 314 2006 997 1001
    • (2006) Science , vol.314 , pp. 997-1001
    • Pichlmair, A.1    Schulz, O.2    Tan, C.P.3    Naslund, T.I.4    Liljestrom, P.5    Weber, F.6
  • 46
    • 70349728538 scopus 로고    scopus 로고
    • Activation of MDA5 requires higher-order RNA structures generated during virus infection
    • A. Pichlmair, O. Schulz, C.-P. Tan, J. Rehwinkel, H. Kato, and O. Takeuchi et al. Activation of MDA5 requires higher-order RNA structures generated during virus infection J Virol 83 2009 10761 10769
    • (2009) J Virol , vol.83 , pp. 10761-10769
    • Pichlmair, A.1    Schulz, O.2    Tan, C.-P.3    Rehwinkel, J.4    Kato, H.5    Takeuchi, O.6
  • 47
    • 34547434301 scopus 로고    scopus 로고
    • Double-stranded DNA and double-stranded RNA induce a common antiviral signaling pathway in human cells
    • G. Cheng, J. Zhong, J. Chung, and F.V. Chisari Double-stranded DNA and double-stranded RNA induce a common antiviral signaling pathway in human cells Proc Natl Acad Sci 104 2007 9035 9040
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 9035-9040
    • Cheng, G.1    Zhong, J.2    Chung, J.3    Chisari, F.V.4
  • 48
    • 59849100923 scopus 로고    scopus 로고
    • Herpes simplex virus infection is sensed by both Toll-like receptors and retinoic acid-inducible gene-like receptors, which synergize to induce type i interferon production
    • S.B. Rasmussen, S.B. Jensen, C. Nielsen, E. Quartin, H. Kato, and Z.J. Chen et al. Herpes simplex virus infection is sensed by both Toll-like receptors and retinoic acid-inducible gene-like receptors, which synergize to induce type I interferon production J Gen Virol 90 2009 74 78
    • (2009) J Gen Virol , vol.90 , pp. 74-78
    • Rasmussen, S.B.1    Jensen, S.B.2    Nielsen, C.3    Quartin, E.4    Kato, H.5    Chen, Z.J.6
  • 49
    • 81255163730 scopus 로고    scopus 로고
    • The virion host shutoff protein of herpes simplex virus 1 blocks the replication-independent activation of NF-κB in dendritic cells in the absence of type i interferon signaling
    • C.R. Cotter, W.-k Kim, M.L. Nguyen, J.S. Yount, C.B. López, and J.A. Blaho et al. The virion host shutoff protein of herpes simplex virus 1 blocks the replication-independent activation of NF-κB in dendritic cells in the absence of type I interferon signaling J Virol 85 2011 12662 12672
    • (2011) J Virol , vol.85 , pp. 12662-12672
    • Cotter, C.R.1    Kim, W.-K.2    Nguyen, M.L.3    Yount, J.S.4    López, C.B.5    Blaho, J.A.6
  • 50
    • 77957958023 scopus 로고    scopus 로고
    • Early innate recognition of herpes simplex virus in human primary macrophages is mediated via the MDA5/MAVS-dependent and MDA5/MAVS/RNA polymerase III-independent pathways
    • J. Melchjorsen, J. Rintahaka, S. Søby, K.A. Horan, A. Poltajainen, and L. ∅stergaard et al. Early innate recognition of herpes simplex virus in human primary macrophages is mediated via the MDA5/MAVS-dependent and MDA5/MAVS/RNA polymerase III-independent pathways J Virol 84 2010 11350 11358
    • (2010) J Virol , vol.84 , pp. 11350-11358
    • Melchjorsen, J.1    Rintahaka, J.2    Søby, S.3    Horan, K.A.4    Poltajainen, A.5    Stergaard, L.6
  • 51
    • 79959344720 scopus 로고    scopus 로고
    • DDX1, DDX21, and DHX36 helicases form a complex with the adaptor molecule TRIF to sense dsRNA in dendritic cells
    • Z. Zhang, T. Kim, M. Bao, V. Facchinetti, S.Y. Jung, and A.A. Ghaffari et al. DDX1, DDX21, and DHX36 helicases form a complex with the adaptor molecule TRIF to sense dsRNA in dendritic cells Immunity 34 2011 866 878
    • (2011) Immunity , vol.34 , pp. 866-878
    • Zhang, Z.1    Kim, T.2    Bao, M.3    Facchinetti, V.4    Jung, S.Y.5    Ghaffari, A.A.6
  • 52
    • 80555133355 scopus 로고    scopus 로고
    • DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells
    • Z. Zhang, B. Yuan, N. Lu, V. Facchinetti, and Y.-J. Liu DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells J Immunol 187 2011 4501 4508
    • (2011) J Immunol , vol.187 , pp. 4501-4508
    • Zhang, Z.1    Yuan, B.2    Lu, N.3    Facchinetti, V.4    Liu, Y.-J.5
  • 53
    • 29244471275 scopus 로고    scopus 로고
    • A Toll-like receptor-independent antiviral response induced by double-stranded B-form DNA
    • K. Ishii, C. Coban, H. Kato, K. Takahashi, Y. Torii, and F. Takeshita A Toll-like receptor-independent antiviral response induced by double-stranded B-form DNA Nat Immunol 7 2006 40 48
    • (2006) Nat Immunol , vol.7 , pp. 40-48
    • Ishii, K.1    Coban, C.2    Kato, H.3    Takahashi, K.4    Torii, Y.5    Takeshita, F.6
  • 54
    • 30444450839 scopus 로고    scopus 로고
    • Recognition of cytosolic DNA activates an IRF3-dependent innate immune response
    • D. Stetson, and R. Medzhitov Recognition of cytosolic DNA activates an IRF3-dependent innate immune response Immunity 24 2006 93 103
    • (2006) Immunity , vol.24 , pp. 93-103
    • Stetson, D.1    Medzhitov, R.2
  • 55
    • 53349178089 scopus 로고    scopus 로고
    • STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
    • H. Ishikawa, and G.N. Barber STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling Nature 455 2008 674 678
    • (2008) Nature , vol.455 , pp. 674-678
    • Ishikawa, H.1    Barber, G.N.2
  • 56
    • 70349943834 scopus 로고    scopus 로고
    • STING regulates intracellular DNA-mediated, type i interferon-dependent innate immunity
    • H. Ishikawa, Z. Ma, and G.N. Barber STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity Nature 461 2009 788 792
    • (2009) Nature , vol.461 , pp. 788-792
    • Ishikawa, H.1    Ma, Z.2    Barber, G.N.3
  • 57
    • 34547143110 scopus 로고    scopus 로고
    • DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response
    • A. Takaoka, Z. Wang, M.K. Choi, H. Yanai, H. Negishi, and T. Ban et al. DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response Nature 448 2007 501 505
    • (2007) Nature , vol.448 , pp. 501-505
    • Takaoka, A.1    Wang, Z.2    Choi, M.K.3    Yanai, H.4    Negishi, H.5    Ban, T.6
  • 58
    • 84873711885 scopus 로고    scopus 로고
    • Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type i interferon pathway
    • L. Sun, J. Wu, F. Du, X. Chen, and Z.J. Chen Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway Science 339 2013 786 791
    • (2013) Science , vol.339 , pp. 786-791
    • Sun, L.1    Wu, J.2    Du, F.3    Chen, X.4    Chen, Z.J.5
  • 60
    • 80052969639 scopus 로고    scopus 로고
    • The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells
    • Z. Zhang, B. Yuan, M. Bao, N. Lu, T. Kim, and Y.-J. Liu The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells Nat Immunol 12 2011 959 965
    • (2011) Nat Immunol , vol.12 , pp. 959-965
    • Zhang, Z.1    Yuan, B.2    Bao, M.3    Lu, N.4    Kim, T.5    Liu, Y.-J.6
  • 61
    • 84875224757 scopus 로고    scopus 로고
    • DNA-PK is a DNA sensor for IRF-3-dependent innate immunity
    • B.J. Ferguson, D.S. Mansur, N.E. Peters, H. Ren, and G.L. Smith DNA-PK is a DNA sensor for IRF-3-dependent innate immunity eLife 1 2012 e00047
    • (2012) ELife , vol.1 , pp. 00047
    • Ferguson, B.J.1    Mansur, D.S.2    Peters, N.E.3    Ren, H.4    Smith, G.L.5
  • 62
    • 84874278336 scopus 로고    scopus 로고
    • DNA damage sensor MRE11 recognizes cytosolic double-stranded DNA and induces type i interferon by regulating STING trafficking
    • T. Kondo, J. Kobayashi, T. Saitoh, K. Maruyama, K.J. Ishii, and G.N. Barber et al. DNA damage sensor MRE11 recognizes cytosolic double-stranded DNA and induces type I interferon by regulating STING trafficking Proc Natl Acad Sci U S A 110 2013 2969 2974
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 2969-2974
    • Kondo, T.1    Kobayashi, J.2    Saitoh, T.3    Maruyama, K.4    Ishii, K.J.5    Barber, G.N.6
  • 63
    • 68049092912 scopus 로고    scopus 로고
    • RNA polymerase III detects cytosolic DNA and induces type i interferons through the RIG-I pathway
    • Y.-H. Chiu, J.B. MacMillan, and Z.J. Chen RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway Cell 138 2009 576 591
    • (2009) Cell , vol.138 , pp. 576-591
    • Chiu, Y.-H.1    Macmillan, J.B.2    Chen, Z.J.3
  • 64
    • 70349459734 scopus 로고    scopus 로고
    • RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate
    • A. Ablasser, F. Bauernfeind, G. Hartmann, E. Latz, K. Fitzgerald, and V. Hornung RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate Nat Immunol 10 2009 1065 1072
    • (2009) Nat Immunol , vol.10 , pp. 1065-1072
    • Ablasser, A.1    Bauernfeind, F.2    Hartmann, G.3    Latz, E.4    Fitzgerald, K.5    Hornung, V.6
  • 65
    • 77952566304 scopus 로고    scopus 로고
    • The cytosolic nucleic acid sensor LRRFIP1 mediates the production of type i interferon via a beta-catenin-dependent pathway
    • P. Yang, H. An, X. Liu, M. Wen, Y. Zheng, and Y. Rui et al. The cytosolic nucleic acid sensor LRRFIP1 mediates the production of type I interferon via a beta-catenin-dependent pathway Nat Immunol 11 2010 487 494
    • (2010) Nat Immunol , vol.11 , pp. 487-494
    • Yang, P.1    An, H.2    Liu, X.3    Wen, M.4    Zheng, Y.5    Rui, Y.6
  • 66
    • 77957009390 scopus 로고    scopus 로고
    • Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A helicases sense microbial DNA in human plasmacytoid dendritic cells
    • T. Kim, S. Pazhoor, M. Bao, Z. Zhang, S. Hanabuchi, and V. Facchinetti et al. Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A helicases sense microbial DNA in human plasmacytoid dendritic cells Proc Natl Acad Sci 107 2010 15181 15186
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 15181-15186
    • Kim, T.1    Pazhoor, S.2    Bao, M.3    Zhang, Z.4    Hanabuchi, S.5    Facchinetti, V.6
  • 67
    • 79955004696 scopus 로고    scopus 로고
    • Cutting edge: Ku70 is a novel cytosolic DNA sensor that induces type III rather than type i IFN
    • X. Zhang, T.W. Brann, M. Zhou, J. Yang, R.M. Oguariri, and K.B. Lidie et al. Cutting edge: Ku70 is a novel cytosolic DNA sensor that induces type III rather than type I IFN J Immunol 186 2011 4541 4545
    • (2011) J Immunol , vol.186 , pp. 4541-4545
    • Zhang, X.1    Brann, T.W.2    Zhou, M.3    Yang, J.4    Oguariri, R.M.5    Lidie, K.B.6
  • 68
    • 44449157593 scopus 로고    scopus 로고
    • Regulation of innate immune responses by DAI (DLM-1/ZBP1) and other DNA-sensing molecules
    • Z. Wang, M.K. Choi, T. Ban, H. Yanai, H. Negishi, and Y. Lu et al. Regulation of innate immune responses by DAI (DLM-1/ZBP1) and other DNA-sensing molecules Proc Natl Acad Sci 105 2008 5477 5482
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 5477-5482
    • Wang, Z.1    Choi, M.K.2    Ban, T.3    Yanai, H.4    Negishi, H.5    Lu, Y.6
  • 69
    • 68249113997 scopus 로고    scopus 로고
    • DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-(kappa)B
    • M. Rebsamen, L.X. Heinz, E. Meylan, M.-C. Michallet, K. Schroder, and K. Hofmann et al. DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-(kappa)B EMBO Rep 10 2009 916 922
    • (2009) EMBO Rep , vol.10 , pp. 916-922
    • Rebsamen, M.1    Heinz, L.X.2    Meylan, E.3    Michallet, M.-C.4    Schroder, K.5    Hofmann, K.6
  • 70
    • 38949093002 scopus 로고    scopus 로고
    • TANK-binding kinase-1 delineates innate and adaptive immune responses to DNA vaccines
    • K.J. Ishii, T. Kawagoe, S. Koyama, K. Matsui, H. Kumar, and T. Kawai et al. TANK-binding kinase-1 delineates innate and adaptive immune responses to DNA vaccines Nature 451 2008 725
    • (2008) Nature , vol.451 , pp. 725
    • Ishii, K.J.1    Kawagoe, T.2    Koyama, S.3    Matsui, K.4    Kumar, H.5    Kawai, T.6
  • 71
    • 80051583481 scopus 로고    scopus 로고
    • A role for DNA-dependent activator of interferon regulatory factor in the recognition of herpes simplex virus type 1 by glial cells
    • S. Furr, V. Chauhan, M. Moerdyk-Schauwecker, and I. Marriott A role for DNA-dependent activator of interferon regulatory factor in the recognition of herpes simplex virus type 1 by glial cells J Neuroinflammation 8 2011 99
    • (2011) J Neuroinflammation , vol.8 , pp. 99
    • Furr, S.1    Chauhan, V.2    Moerdyk-Schauwecker, M.3    Marriott, I.4
  • 72
    • 84876345677 scopus 로고    scopus 로고
    • DNA sensing-independent inhibition of herpes simplex virus 1 replication by DAI/ZBP1
    • T.H. Pham, K.M. Kwon, Y.-E. Kim, K.K. Kim, and J.-H. Ahn DNA sensing-independent inhibition of herpes simplex virus 1 replication by DAI/ZBP1 J Virol 87 2013 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
  • 73
    • 84858420051 scopus 로고    scopus 로고
    • DAI/ZBP1/DLM-1 complexes with RIP3 to mediate virus-induced programmed necrosis that is targeted by murine cytomegalovirus vIRA
    • J.W. Upton, W.J. Kaiser, and E.S. Mocarski DAI/ZBP1/DLM-1 complexes with RIP3 to mediate virus-induced programmed necrosis that is targeted by murine cytomegalovirus vIRA Cell Host Microbe 11 2012 290 297
    • (2012) Cell Host Microbe , vol.11 , pp. 290-297
    • Upton, J.W.1    Kaiser, W.J.2    Mocarski, E.S.3
  • 74
    • 80052152283 scopus 로고    scopus 로고
    • The PYHIN protein family as mediators of host defenses
    • S.A. Schattgen, and K.A. Fitzgerald The PYHIN protein family as mediators of host defenses Immunol Rev 243 2011 109 118
    • (2011) Immunol Rev , vol.243 , pp. 109-118
    • Schattgen, S.A.1    Fitzgerald, K.A.2
  • 75
    • 49149114140 scopus 로고    scopus 로고
    • The DEAD-box helicase DDX3X is a critical component of the TANK-binding kinase 1-dependent innate immune response
    • D. Soulat, T. Burckstummer, S. Westermayer, A. Goncalves, A. Bauch, and A. Stefanovic et al. The DEAD-box helicase DDX3X is a critical component of the TANK-binding kinase 1-dependent innate immune response EMBO J 27 2008 2135 2146
    • (2008) EMBO J , vol.27 , pp. 2135-2146
    • Soulat, D.1    Burckstummer, T.2    Westermayer, S.3    Goncalves, A.4    Bauch, A.5    Stefanovic, A.6
  • 76
    • 49149113373 scopus 로고    scopus 로고
    • Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKK(epsiv)-mediated IRF activation
    • M. Schroder, M. Baran, and A.G. Bowie Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKK(epsiv)-mediated IRF activation EMBO J 27 2008 2147 2157
    • (2008) EMBO J , vol.27 , pp. 2147-2157
    • Schroder, M.1    Baran, M.2    Bowie, A.G.3
  • 77
    • 84863116708 scopus 로고    scopus 로고
    • Resistance to HSV-1 infection in the epithelium resides with the novel innate sensor, IFI-16
    • C.D. Conrady, M. Zheng, K.A. Fitzgerald, C. Liu, and D.J.J. Carr Resistance to HSV-1 infection in the epithelium resides with the novel innate sensor, IFI-16 Mucosal Immunol 5 2012 173 183
    • (2012) Mucosal Immunol , vol.5 , pp. 173-183
    • Conrady, C.D.1    Zheng, M.2    Fitzgerald, K.A.3    Liu, C.4    Carr, D.J.J.5
  • 78
    • 84655165036 scopus 로고    scopus 로고
    • Interferon-inducible p200-family protein IFI16, an innate immune sensor for cytosolic and nuclear double-stranded DNA: Regulation of subcellular localization
    • S. Veeranki, and D. Choubey Interferon-inducible p200-family protein IFI16, an innate immune sensor for cytosolic and nuclear double-stranded DNA: regulation of subcellular localization Mol Immunol 49 2012 567 571
    • (2012) Mol Immunol , vol.49 , pp. 567-571
    • Veeranki, S.1    Choubey, D.2
  • 79
    • 84862976171 scopus 로고    scopus 로고
    • Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16
    • T. Li, B.A. Diner, J. Chen, and I.M. Cristea Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16 Proc Natl Acad Sci 109 2012 10558 10563
    • (2012) Proc Natl Acad Sci , vol.109 , pp. 10558-10563
    • Li, T.1    Diner, B.A.2    Chen, J.3    Cristea, I.M.4
  • 80
    • 84874246480 scopus 로고    scopus 로고
    • Proteasomal degradation of herpes simplex virus capsids in macrophages releases DNA to the cytosol for recognition by DNA sensors
    • K.A. Horan, K. Hansen, M.R. Jakobsen, C.K. Holm, S. Søby, and L. Unterholzner et al. Proteasomal degradation of herpes simplex virus capsids in macrophages releases DNA to the cytosol for recognition by DNA sensors J Immunol 190 2013 2311 2319
    • (2013) J Immunol , vol.190 , pp. 2311-2319
    • Horan, K.A.1    Hansen, K.2    Jakobsen, M.R.3    Holm, C.K.4    Søby, S.5    Unterholzner, L.6
  • 81
    • 84868095535 scopus 로고    scopus 로고
    • Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein
    • M.H. Orzalli, N.A. DeLuca, and D.M. Knipe Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein Proc Natl Acad Sci 109 2012 E3008 E3017
    • (2012) Proc Natl Acad Sci , vol.109
    • Orzalli, M.H.1    Deluca, N.A.2    Knipe, D.M.3
  • 82
    • 79956061094 scopus 로고    scopus 로고
    • IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi Sarcoma-associated herpesvirus infection
    • N. Kerur, M.V. Veettil, N. Sharma-Walia, V. Bottero, S. Sadagopan, and P. Otageri et al. IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi Sarcoma-associated herpesvirus infection Cell Host Microbe 9 2011 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
  • 83
    • 84866324649 scopus 로고    scopus 로고
    • DNA viruses and the cellular DNA-damage response
    • A.S. Turnell, and R.J. Grand DNA viruses and the cellular DNA-damage response J Gen Virol 93 2012 2076 2097
    • (2012) J Gen Virol , vol.93 , pp. 2076-2097
    • Turnell, A.S.1    Grand, R.J.2
  • 85
    • 84873724533 scopus 로고    scopus 로고
    • Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA
    • J. Wu, L. Sun, X. Chen, F. Du, H. Shi, and C. Chen et al. Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA Science 339 2013 826 830
    • (2013) Science , vol.339 , pp. 826-830
    • Wu, J.1    Sun, L.2    Chen, X.3    Du, F.4    Shi, H.5    Chen, C.6
  • 86
    • 80054966060 scopus 로고    scopus 로고
    • Membrane perturbation elicits an IRF3-dependent, interferon-independent antiviral response
    • R.S. Noyce, K. Taylor, M. Ciechonska, S.E. Collins, R. Duncan, and K.L. Mossman Membrane perturbation elicits an IRF3-dependent, interferon-independent antiviral response J Virol 85 2011 10926 10931
    • (2011) J Virol , vol.85 , pp. 10926-10931
    • Noyce, R.S.1    Taylor, K.2    Ciechonska, M.3    Collins, S.E.4    Duncan, R.5    Mossman, K.L.6
  • 88
    • 0034844014 scopus 로고    scopus 로고
    • Activation of interferon response factor-3 in human cells infected with herpes simplex virus type 1 or human cytomegalovirus
    • C.M. Preston, A.N. Harman, and M.J. Nicholl Activation of interferon response factor-3 in human cells infected with herpes simplex virus type 1 or human cytomegalovirus J Virol 75 2001 8909 8916
    • (2001) J Virol , vol.75 , pp. 8909-8916
    • Preston, C.M.1    Harman, A.N.2    Nicholl, M.J.3
  • 89
    • 0842304532 scopus 로고    scopus 로고
    • Innate cellular response to virus particle entry requires IRF3 but not virus replication
    • S.E. Collins, R.S. Noyce, and K.L. Mossman Innate cellular response to virus particle entry requires IRF3 but not virus replication J Virol 78 2004 1706 1717
    • (2004) J Virol , vol.78 , pp. 1706-1717
    • Collins, S.E.1    Noyce, R.S.2    Mossman, K.L.3
  • 90
    • 33645989466 scopus 로고    scopus 로고
    • Identification of a novel pathway essential for the immediate-early, interferon-independent antiviral response to enveloped virions
    • R.S. Noyce, S.E. Collins, and K.L. Mossman Identification of a novel pathway essential for the immediate-early, interferon-independent antiviral response to enveloped virions J Virol 80 2006 226 235
    • (2006) J Virol , vol.80 , pp. 226-235
    • Noyce, R.S.1    Collins, S.E.2    Mossman, K.L.3
  • 91
    • 79952073161 scopus 로고    scopus 로고
    • Innate immune sensing of DNA viruses
    • V.A. Rathinam, and K.A. Fitzgerald Innate immune sensing of DNA viruses Virology 411 2011 153 162
    • (2011) Virology , vol.411 , pp. 153-162
    • Rathinam, V.A.1    Fitzgerald, K.A.2
  • 92
    • 79955961661 scopus 로고    scopus 로고
    • Varicella-zoster virus infection triggers formation of an interleukin-1 (IL-1)-processing inflammasome complex
    • A.M. Nour, M. Reichelt, C.C. Ku, M.Y. Ho, T.C. Heineman, and A.M. Arvin Varicella-zoster virus infection triggers formation of an interleukin-1 (IL-1)-processing inflammasome complex J Biol Chem 286 2011 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
  • 93
    • 84880617721 scopus 로고    scopus 로고
    • Constitutive interferon-inducible protein 16-inflammasome activation during Epstein-Barr virus latency I, II, and III in B and epithelial cells
    • M.A. Ansari, V.V. Singh, S. Dutta, M.V. Veettil, D. Dutta, and L. Chikoti et al. Constitutive interferon-inducible protein 16-inflammasome activation during Epstein-Barr virus latency I, II, and III in B and epithelial cells J Virol 87 2013 8606 8623
    • (2013) J Virol , vol.87 , pp. 8606-8623
    • Ansari, M.A.1    Singh, V.V.2    Dutta, S.3    Veettil, M.V.4    Dutta, D.5    Chikoti, L.6
  • 94
    • 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
    • S. Veeranki, X. Duan, R. Panchanathan, H. Liu, and D. Choubey IFI16 protein mediates the anti-inflammatory actions of the type-I interferons through suppression of activation of caspase-1 by inflammasomes PLoS One 6 2011 e27040
    • (2011) PLoS One , vol.6 , pp. 27040
    • Veeranki, S.1    Duan, X.2    Panchanathan, R.3    Liu, H.4    Choubey, D.5
  • 95
    • 40449097257 scopus 로고    scopus 로고
    • The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response
    • D.A. Muruve, V. Petrilli, A.K. Zaiss, L.R. White, S.A. Clark, and P.J. Ross et al. The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response Nature 452 2008 103 107
    • (2008) Nature , vol.452 , pp. 103-107
    • Muruve, D.A.1    Petrilli, V.2    Zaiss, A.K.3    White, L.R.4    Clark, S.A.5    Ross, P.J.6
  • 96
    • 77951269392 scopus 로고    scopus 로고
    • The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
    • V.A.K. Rathinam, Z. Jiang, S.N. Waggoner, S. Sharma, L.E. Cole, and L. Waggoner et al. The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses Nat Immunol 11 2010 395 402
    • (2010) Nat Immunol , vol.11 , pp. 395-402
    • Rathinam, V.A.K.1    Jiang, Z.2    Waggoner, S.N.3    Sharma, S.4    Cole, L.E.5    Waggoner, L.6
  • 97
    • 84865511926 scopus 로고    scopus 로고
    • Novel role of PKR in inflammasome activation and HMGB1 release
    • B. Lu, T. Nakamura, K. Inouye, J. Li, Y. Tang, and P. Lundback et al. Novel role of PKR in inflammasome activation and HMGB1 release Nature 488 2012 670 674
    • (2012) Nature , vol.488 , pp. 670-674
    • Lu, B.1    Nakamura, T.2    Inouye, K.3    Li, J.4    Tang, Y.5    Lundback, P.6
  • 98
    • 84858677223 scopus 로고    scopus 로고
    • Sensing and reacting to microbes through the inflammasomes
    • L. Franchi, R. Munoz-Planillo, and G. Nunez Sensing and reacting to microbes through the inflammasomes Nat Immunol 13 2012 325 332
    • (2012) Nat Immunol , vol.13 , pp. 325-332
    • Franchi, L.1    Munoz-Planillo, R.2    Nunez, G.3
  • 99
    • 79953046719 scopus 로고    scopus 로고
    • The inflammasome NLRs in immunity, inflammation, and associated diseases
    • B.K. Davis, H. Wen, and J.P.-Y. Ting The inflammasome NLRs in immunity, inflammation, and associated diseases Annu Rev Immunol 29 2011 707 735
    • (2011) Annu Rev Immunol , vol.29 , pp. 707-735
    • Davis, B.K.1    Wen, H.2    Ting, J.P.-Y.3
  • 100
    • 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
    • J. Kavouras, E. Prandovszky, K. Valyi-Nagy, S.K. Kovacs, V. Tiwari, and M. Kovacs et al. 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 2007 416 425
    • (2007) J Neurovirol , vol.13 , pp. 416-425
    • Kavouras, J.1    Prandovszky, E.2    Valyi-Nagy, K.3    Kovacs, S.K.4    Tiwari, V.5    Kovacs, M.6
  • 101
    • 0031017382 scopus 로고    scopus 로고
    • The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase
    • B. He, M. Gross, and B. Roizman The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase Proc Natl Acad Sci U S A 94 1997 843 848
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 102
    • 0036150004 scopus 로고    scopus 로고
    • Herpes simplex virus ICP0 and ICP34.5 counteract distinct interferon-induced barriers to virus replication
    • K.L. Mossman, and J.R. Smiley Herpes simplex virus ICP0 and ICP34.5 counteract distinct interferon-induced barriers to virus replication J Virol 76 2002 1995 1998
    • (2002) J Virol , vol.76 , pp. 1995-1998
    • Mossman, K.L.1    Smiley, J.R.2
  • 103
    • 0036174361 scopus 로고    scopus 로고
    • Expression of herpes simplex virus ICP0 inhibits the induction of interferon-stimulated genes by viral infection
    • K.M. Eidson, W.E. Hobbs, B.J. Manning, P. Carlson, and N.A. DeLuca Expression of herpes simplex virus ICP0 inhibits the induction of interferon-stimulated genes by viral infection J Virol 76 2002 2180 2191
    • (2002) J Virol , vol.76 , pp. 2180-2191
    • Eidson, K.M.1    Hobbs, W.E.2    Manning, B.J.3    Carlson, P.4    Deluca, N.A.5
  • 104
    • 0842326034 scopus 로고    scopus 로고
    • The herpes simplex virus ICP0 RING finger domain inhibits IRF3- and IRF7-mediated activation of interferon-stimulated genes
    • R. Lin, R.S. Noyce, S.E. Collins, R.D. Everett, and K.L. Mossman The herpes simplex virus ICP0 RING finger domain inhibits IRF3- and IRF7-mediated activation of interferon-stimulated genes J Virol 78 2004 1675 1684
    • (2004) J Virol , vol.78 , pp. 1675-1684
    • Lin, R.1    Noyce, R.S.2    Collins, S.E.3    Everett, R.D.4    Mossman, K.L.5
  • 105
    • 3543054546 scopus 로고    scopus 로고
    • Herpes simplex virus 1 has multiple mechanisms for blocking virus-induced interferon production
    • G.T. Melroe, N.A. DeLuca, and D.M. Knipe Herpes simplex virus 1 has multiple mechanisms for blocking virus-induced interferon production J Virol 78 2004 8411 8420
    • (2004) J Virol , vol.78 , pp. 8411-8420
    • Melroe, G.T.1    Deluca, N.A.2    Knipe, D.M.3
  • 106
    • 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
    • G.T. Melroe, L. Silva, P.A. Schaffer, and D.M. Knipe Recruitment of activated IRF-3 and CBP/p300 to herpes simplex virus ICP0 nuclear foci: potential role in blocking IFN-(beta) induction Virology 360 2007 305
    • (2007) Virology , vol.360 , pp. 305
    • Melroe, G.T.1    Silva, L.2    Schaffer, P.A.3    Knipe, D.M.4
  • 107
    • 77956398377 scopus 로고    scopus 로고
    • Cellular localization of the herpes simplex virus ICP0 protein dictates its ability to block IRF3-mediated innate immune responses
    • P. Paladino, S.E. Collins, and K.L. Mossman Cellular localization of the herpes simplex virus ICP0 protein dictates its ability to block IRF3-mediated innate immune responses PLoS One 5 2010 e10428
    • (2010) PLoS One , vol.5 , pp. 10428
    • Paladino, P.1    Collins, S.E.2    Mossman, K.L.3
  • 108
    • 65349175161 scopus 로고    scopus 로고
    • HSV ICP0 recruits USP7 to modulate TLR-mediated innate response
    • S. Daubeuf, D. Singh, Y. Tan, H. Liu, H.J. Federoff, and W.J. Bowers et al. HSV ICP0 recruits USP7 to modulate TLR-mediated innate response Blood 113 2009 3264 3275
    • (2009) Blood , vol.113 , pp. 3264-3275
    • Daubeuf, S.1    Singh, D.2    Tan, Y.3    Liu, H.4    Federoff, H.J.5    Bowers, W.J.6
  • 109
    • 77957203288 scopus 로고    scopus 로고
    • Herpes simplex virus immediate-early ICP0 protein inhibits Toll-like receptor 2-dependent inflammatory responses and NF-κB signaling
    • A.L. van Lint, M.R. Murawski, R.E. Goodbody, M. Severa, K.A. Fitzgerald, and R.W. Finberg et al. Herpes simplex virus immediate-early ICP0 protein inhibits Toll-like receptor 2-dependent inflammatory responses and NF-κB signaling J Virol 84 2010 10802 10811
    • (2010) J Virol , vol.84 , pp. 10802-10811
    • Van Lint, A.L.1    Murawski, M.R.2    Goodbody, R.E.3    Severa, M.4    Fitzgerald, K.A.5    Finberg, R.W.6
  • 110
    • 2442708973 scopus 로고    scopus 로고
    • Suppression of proinflammatory cytokine expression by herpes simplex virus type 1
    • T.H. Mogensen, J. Melchjorsen, L. Malmgaard, A. Casola, and S.R. Paludan Suppression of proinflammatory cytokine expression by herpes simplex virus type 1 J Virol 78 2004 5883 5890
    • (2004) J Virol , vol.78 , pp. 5883-5890
    • Mogensen, T.H.1    Melchjorsen, J.2    Malmgaard, L.3    Casola, A.4    Paludan, S.R.5
  • 111
    • 33646131843 scopus 로고    scopus 로고
    • Induction of cytokine expression by herpes simplex virus in human monocyte-derived macrophages and dendritic cells is dependent on virus replication and is counteracted by ICP27 targeting NF-(kappa)B and IRF-3
    • J. Melchjorsen, J. Siren, I. Julkunen, S.R. Paludan, and S. Matikainen Induction of cytokine expression by herpes simplex virus in human monocyte-derived macrophages and dendritic cells is dependent on virus replication and is counteracted by ICP27 targeting NF-(kappa)B and IRF-3 J Gen Virol 87 2006 1099 1108
    • (2006) J Gen Virol , vol.87 , pp. 1099-1108
    • Melchjorsen, J.1    Siren, J.2    Julkunen, I.3    Paludan, S.R.4    Matikainen, S.5
  • 112
    • 45549087796 scopus 로고    scopus 로고
    • HSV-1 ICP27 suppresses NF-(kappa)B activity by stabilizing I(kappa)B(alpha)
    • J.C. Kim, S.Y. Lee, S.Y. Kim, J.K. Kim, H.J. Kim, and H.M. Lee et al. HSV-1 ICP27 suppresses NF-(kappa)B activity by stabilizing I(kappa)B(alpha) FEBS Lett 582 2008 2371
    • (2008) FEBS Lett , vol.582 , pp. 2371
    • Kim, J.C.1    Lee, S.Y.2    Kim, S.Y.3    Kim, J.K.4    Kim, H.J.5    Lee, H.M.6
  • 113
    • 0022655615 scopus 로고
    • The terminal a sequence of the herpes simplex virus genome contains the promoter of a gene located in the repeat sequences of the L component
    • J. Chou, and B. Roizman The terminal a sequence of the herpes simplex virus genome contains the promoter of a gene located in the repeat sequences of the L component J Virol 57 1986 629 637
    • (1986) J Virol , vol.57 , pp. 629-637
    • Chou, J.1    Roizman, B.2
  • 114
    • 0027527821 scopus 로고
    • The herpes simplex virus type 1 strain 17 open reading frame RL1 encodes a polypeptide of apparent M(r) 37K equivalent to ICP34.5 of herpes simplex virus type 1 strain F
    • E.M. McKay, B. McVey, H.S. Marsden, S.M. Brown, and A.R. MacLean The herpes simplex virus type 1 strain 17 open reading frame RL1 encodes a polypeptide of apparent M(r) 37K equivalent to ICP34.5 of herpes simplex virus type 1 strain F J Gen Virol 74 1993 2493 2497
    • (1993) J Gen Virol , vol.74 , pp. 2493-2497
    • McKay, E.M.1    McVey, B.2    Marsden, H.S.3    Brown, S.M.4    Maclean, A.R.5
  • 115
    • 59449109932 scopus 로고    scopus 로고
    • Control of TANK-binding kinase 1-mediated signaling by the (gamma)134.5 protein of herpes simplex virus 1
    • D. Verpooten, Y. Ma, S. Hou, Z. Yan, and B. He Control of TANK-binding kinase 1-mediated signaling by the (gamma)134.5 protein of herpes simplex virus 1 J Biol Chem 284 2009 1097 1105
    • (2009) J Biol Chem , vol.284 , pp. 1097-1105
    • Verpooten, D.1    Ma, Y.2    Hou, S.3    Yan, Z.4    He, B.5
  • 116
    • 0032516518 scopus 로고    scopus 로고
    • The gamma(1)34.5 protein of herpes simplex virus 1 has the structural and functional attributes of a protein phosphatase 1 regulatory subunit and is present in a high molecular weight complex with the enzyme in infected cells
    • B. He, M. Gross, and B. Roizman The gamma(1)34.5 protein of herpes simplex virus 1 has the structural and functional attributes of a protein phosphatase 1 regulatory subunit and is present in a high molecular weight complex with the enzyme in infected cells J Biol Chem 273 1998 20737 20743
    • (1998) J Biol Chem , vol.273 , pp. 20737-20743
    • He, B.1    Gross, M.2    Roizman, B.3
  • 117
    • 0035841360 scopus 로고    scopus 로고
    • 134.5 protein of herpes simplex virus 1 are required for viral resistance to interferon-α/β
    • 134.5 protein of herpes simplex virus 1 are required for viral resistance to interferon-α/β Virology 290 2001 115
    • (2001) Virology , vol.290 , pp. 115
    • Cheng, G.1    Brett, M.-E.2    He, B.3
  • 119
    • 70450208398 scopus 로고    scopus 로고
    • Dephosphorylation of eIF2(alpha) mediated by the (gamma)134.5 protein of herpes simplex virus 1 facilitates viral neuroinvasion
    • D. Verpooten, Z. Feng, T. Valyi-Nagy, Y. Ma, H. Jin, and Z. Yan et al. Dephosphorylation of eIF2(alpha) mediated by the (gamma)134.5 protein of herpes simplex virus 1 facilitates viral neuroinvasion J Virol 83 2009 12626 12630
    • (2009) J Virol , vol.83 , pp. 12626-12630
    • Verpooten, D.1    Feng, Z.2    Valyi-Nagy, T.3    Ma, Y.4    Jin, H.5    Yan, Z.6
  • 120
    • 0035036952 scopus 로고    scopus 로고
    • 134.5 second-site suppressor mutant that exhibits enhanced growth in cultured glioblastoma cells is severely attenuated in animals
    • 134.5 second-site suppressor mutant that exhibits enhanced growth in cultured glioblastoma cells is severely attenuated in animals J Virol 75 2001 5189 5196
    • (2001) J Virol , vol.75 , pp. 5189-5196
    • Mohr, I.1    Sternberg, D.2    Ward, S.3    Leib, D.4    Mulvey, M.5    Gluzman, Y.6
  • 121
    • 0345701493 scopus 로고    scopus 로고
    • In vivo replication of an ICP34.5 second-site suppressor mutant following corneal infection correlates with in vitro regulation of eIF2α phosphorylation
    • S.L. Ward, D. Scheuner, J. Poppers, R.J. Kaufman, I. Mohr, and D.A. Leib In vivo replication of an ICP34.5 second-site suppressor mutant following corneal infection correlates with in vitro regulation of eIF2α phosphorylation J Virol 77 2003 4626 4634
    • (2003) J Virol , vol.77 , pp. 4626-4634
    • Ward, S.L.1    Scheuner, D.2    Poppers, J.3    Kaufman, R.J.4    Mohr, I.5    Leib, D.A.6
  • 122
    • 0036145269 scopus 로고    scopus 로고
    • Second-site mutation outside of the U(S)10-12 domain of Deltagamma(1)34.5 herpes simplex virus 1 recombinant blocks the shutoff of protein synthesis induced by activated protein kinase R and partially restores neurovirulence
    • K.A. Cassady, M. Gross, G.Y. Gillespie, and B. Roizman Second-site mutation outside of the U(S)10-12 domain of Deltagamma(1)34.5 herpes simplex virus 1 recombinant blocks the shutoff of protein synthesis induced by activated protein kinase R and partially restores neurovirulence J Virol 76 2002 942 949
    • (2002) J Virol , vol.76 , pp. 942-949
    • Cassady, K.A.1    Gross, M.2    Gillespie, G.Y.3    Roizman, B.4
  • 123
    • 33746190699 scopus 로고    scopus 로고
    • Functional genomic analysis of herpes simplex virus type 1 counteraction of the host innate response
    • T.J. Pasieka, T. Baas, V.S. Carter, S.C. Proll, M.G. Katze, and D.A. Leib Functional genomic analysis of herpes simplex virus type 1 counteraction of the host innate response J Virol 80 2006 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
  • 124
    • 84863127174 scopus 로고    scopus 로고
    • Inhibition of TANK binding kinase 1 by herpes simplex virus 1 facilitates productive infection
    • Y. Ma, H. Jin, T. Valyi-Nagy, Y. Cao, Z. Yan, and B. He Inhibition of TANK binding kinase 1 by herpes simplex virus 1 facilitates productive infection J Virol 86 2012 2188 2196
    • (2012) J Virol , vol.86 , pp. 2188-2196
    • Ma, Y.1    Jin, H.2    Valyi-Nagy, T.3    Cao, Y.4    Yan, Z.5    He, B.6
  • 125
    • 79952583971 scopus 로고    scopus 로고
    • A herpesvirus virulence factor inhibits dendritic cell maturation through protein phosphatase 1 and IκB kinase
    • H. Jin, Z. Yan, Y. Ma, Y. Cao, and B. He A herpesvirus virulence factor inhibits dendritic cell maturation through protein phosphatase 1 and IκB kinase J Virol 85 2011 3397 3407
    • (2011) J Virol , vol.85 , pp. 3397-3407
    • Jin, H.1    Yan, Z.2    Ma, Y.3    Cao, Y.4    He, B.5
  • 126
    • 65349167768 scopus 로고    scopus 로고
    • The (gamma)134.5 protein of herpes simplex virus 1 is required to interfere with dendritic cell maturation during productive infection
    • H. Jin, Y. Ma, B.S. Prabhakar, Z. Feng, T. Valyi-Nagy, and Z. Yan et al. The (gamma)134.5 protein of herpes simplex virus 1 is required to interfere with dendritic cell maturation during productive infection J Virol 83 2009 4984 4994
    • (2009) J Virol , vol.83 , pp. 4984-4994
    • Jin, H.1    Ma, Y.2    Prabhakar, B.S.3    Feng, Z.4    Valyi-Nagy, T.5    Yan, Z.6
  • 127
    • 2642604294 scopus 로고
    • Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs
    • A.D. Kwong, and N. Frenkel Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs Proc Natl Acad Sci U S A 84 1987 1926 1930
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 1926-1930
    • Kwong, A.D.1    Frenkel, N.2
  • 128
    • 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
    • T. Suzutani, M. Nagamine, T. Shibaki, M. Ogasawara, I. Yoshida, and T. Daikoku et al. 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 2000 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
  • 129
    • 0041888287 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 virion host shutoff protein regulates alpha/beta interferon but not adaptive immune responses during primary infection in vivo
    • J.A. Murphy, R.J. Duerst, T.J. Smith, and L.A. Morrison Herpes simplex virus type 2 virion host shutoff protein regulates alpha/beta interferon but not adaptive immune responses during primary infection in vivo J Virol 77 2003 9337 9345
    • (2003) J Virol , vol.77 , pp. 9337-9345
    • Murphy, J.A.1    Duerst, R.J.2    Smith, T.J.3    Morrison, L.A.4
  • 130
    • 1942421835 scopus 로고    scopus 로고
    • Herpes simplex virus 2 virion host shutoff protein interferes with type i interferon production and responsiveness
    • R.J. Duerst, and L.A. Morrison Herpes simplex virus 2 virion host shutoff protein interferes with type I interferon production and responsiveness Virology 322 2004 158
    • (2004) Virology , vol.322 , pp. 158
    • Duerst, R.J.1    Morrison, L.A.2
  • 131
    • 43949120109 scopus 로고    scopus 로고
    • Herpes simplex virus virion host shutoff attenuates establishment of the antiviral state
    • T.J. Pasieka, B. Lu, S.D. Crosby, K.M. Wylie, L.A. Morrison, and D.E. Alexander et al. Herpes simplex virus virion host shutoff attenuates establishment of the antiviral state J Virol 82 2008 5527 5535
    • (2008) J Virol , vol.82 , pp. 5527-5535
    • Pasieka, T.J.1    Lu, B.2    Crosby, S.D.3    Wylie, K.M.4    Morrison, L.A.5    Alexander, D.E.6
  • 132
    • 1842484070 scopus 로고    scopus 로고
    • Herpes simplex virus 1 gene products occlude the interferon signaling pathway at multiple sites
    • A.V. Chee, and B. Roizman Herpes simplex virus 1 gene products occlude the interferon signaling pathway at multiple sites J Virol 78 2004 4185 4196
    • (2004) J Virol , vol.78 , pp. 4185-4196
    • Chee, A.V.1    Roizman, B.2
  • 133
    • 80051748552 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 virion host shutoff protein suppresses innate dsRNA antiviral pathways in human vaginal epithelial cells
    • X.-D. Yao, and K.L. Rosenthal Herpes simplex virus type 2 virion host shutoff protein suppresses innate dsRNA antiviral pathways in human vaginal epithelial cells J Gen Virol 92 2011 1981 1993
    • (2011) J Gen Virol , vol.92 , pp. 1981-1993
    • Yao, X.-D.1    Rosenthal, K.L.2
  • 134
    • 77949534318 scopus 로고    scopus 로고
    • The virion host shut-off (vhs) protein blocks a TLR-independent pathway of herpes simplex virus type 1 recognition in human and mouse dendritic cells
    • C.R. Cotter, M.L. Nguyen, J.S. Yount, C.B. López, J.A. Blaho, and T.M. Moran The virion host shut-off (vhs) protein blocks a TLR-independent pathway of herpes simplex virus type 1 recognition in human and mouse dendritic cells PLoS One 5 2010 e8684
    • (2010) PLoS One , vol.5 , pp. 8684
    • Cotter, C.R.1    Nguyen, M.L.2    Yount, J.S.3    López, C.B.4    Blaho, J.A.5    Moran, T.M.6
  • 135
    • 78651254479 scopus 로고    scopus 로고
    • Keep it in the subfamily: The conserved alphaherpesvirus US3 protein kinase
    • M.J. Deruelle, and H.W. Favoreel Keep it in the subfamily: the conserved alphaherpesvirus US3 protein kinase J Gen Virol 92 2011 18 30
    • (2011) J Gen Virol , vol.92 , pp. 18-30
    • Deruelle, M.J.1    Favoreel, H.W.2
  • 137
    • 58149086118 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 Us3 gene deletion influences Toll-like receptor responses in cultured monocytic cells
    • P. Peri, R. Mattila, H. Kantola, E. Broberg, H. Karttunen, and M. Waris et al. Herpes simplex virus type 1 Us3 gene deletion influences Toll-like receptor responses in cultured monocytic cells Virol J 5 2008 140
    • (2008) Virol J , vol.5 , pp. 140
    • Peri, P.1    Mattila, R.2    Kantola, H.3    Broberg, E.4    Karttunen, H.5    Waris, M.6
  • 138
    • 84875808016 scopus 로고    scopus 로고
    • Herpes simplex virus US3 tegument protein inhibits Toll-like receptor 2 signaling at or before TRAF6 ubiquitination
    • J. Sen, X. Liu, R. Roller, and D.M. Knipe Herpes simplex virus US3 tegument protein inhibits Toll-like receptor 2 signaling at or before TRAF6 ubiquitination Virology 439 2013 65 73
    • (2013) Virology , vol.439 , pp. 65-73
    • Sen, J.1    Liu, X.2    Roller, R.3    Knipe, D.M.4
  • 139
    • 0029841340 scopus 로고    scopus 로고
    • A herpesvirus genetic element which affects translation in the absence of the viral GADD34 function
    • I. Mohr, and Y. Gluzman A herpesvirus genetic element which affects translation in the absence of the viral GADD34 function EMBO J 15 1996 4759 4766
    • (1996) EMBO J , vol.15 , pp. 4759-4766
    • Mohr, I.1    Gluzman, Y.2
  • 140
    • 0034469630 scopus 로고    scopus 로고
    • Inhibition of PKR activation by the proline-rich RNA binding domain of the herpes simplex virus type 1 Us11 protein
    • J. Poppers, M. Mulvey, D. Khoo, and I. Mohr Inhibition of PKR activation by the proline-rich RNA binding domain of the herpes simplex virus type 1 Us11 protein J Virol 74 2000 11215 11221
    • (2000) J Virol , vol.74 , pp. 11215-11221
    • Poppers, J.1    Mulvey, M.2    Khoo, D.3    Mohr, I.4
  • 141
    • 0036168638 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 US11 protein interacts with protein kinase R in infected cells and requires a 30-amino-acid sequence adjacent to a kinase substrate domain
    • K.A. Cassady, and M. Gross The herpes simplex virus type 1 US11 protein interacts with protein kinase R in infected cells and requires a 30-amino-acid sequence adjacent to a kinase substrate domain J Virol 76 2002 2029 2035
    • (2002) J Virol , vol.76 , pp. 2029-2035
    • Cassady, K.A.1    Gross, M.2
  • 142
    • 33947357710 scopus 로고    scopus 로고
    • Inhibition of cellular 2′-5′ oligoadenylate synthetase by the herpes simplex virus type 1 Us11 protein
    • R. Sáanchez, and I. Mohr Inhibition of cellular 2′-5′ oligoadenylate synthetase by the herpes simplex virus type 1 Us11 protein J Virol 81 2007 3455 3464
    • (2007) J Virol , vol.81 , pp. 3455-3464
    • Sáanchez, R.1    Mohr, I.2
  • 143
    • 4444319171 scopus 로고    scopus 로고
    • Full resistance of herpes simplex virus type 1-infected primary human cells to alpha interferon requires both the Us11 and gamma(1)34.5 gene products
    • M. Mulvey, V. Camarena, and I. Mohr Full resistance of herpes simplex virus type 1-infected primary human cells to alpha interferon requires both the Us11 and gamma(1)34.5 gene products J Virol 78 2004 10193 10196
    • (2004) J Virol , vol.78 , pp. 10193-10196
    • Mulvey, M.1    Camarena, V.2    Mohr, I.3
  • 144
    • 84861320795 scopus 로고    scopus 로고
    • Herpes simplex virus 1 tegument protein US11 downmodulates the RLR signaling pathway via direct interaction with RIG-I and MDA-5
    • J. Xing, S. Wang, R. Lin, K.L. Mossman, and C. Zheng Herpes simplex virus 1 tegument protein US11 downmodulates the RLR signaling pathway via direct interaction with RIG-I and MDA-5 J Virol 86 2012 3528 3540
    • (2012) J Virol , vol.86 , pp. 3528-3540
    • Xing, J.1    Wang, S.2    Lin, R.3    Mossman, K.L.4    Zheng, C.5
  • 145
    • 34548490485 scopus 로고    scopus 로고
    • Tumor necrosis factor-α and interleukin-1β play a critical role in the resistance against lethal herpes simplex virus encephalitis
    • Y. Sergerie, S. Rivest, and G. Boivin Tumor necrosis factor-α and interleukin-1β play a critical role in the resistance against lethal herpes simplex virus encephalitis J Infect Dis 196 2007 853 860
    • (2007) J Infect Dis , vol.196 , pp. 853-860
    • Sergerie, Y.1    Rivest, S.2    Boivin, G.3
  • 146
    • 0032981470 scopus 로고    scopus 로고
    • Interleukin-18 protects mice against acute herpes simplex virus type 1 infection
    • N. Fujioka, R. Akazawa, K. Ohashi, M. Fujii, M. Ikeda, and M. Kurimoto Interleukin-18 protects mice against acute herpes simplex virus type 1 infection J Virol 73 1999 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
  • 147
    • 84869232621 scopus 로고    scopus 로고
    • Global secretome characterization of herpes simplex virus 1-infected human primary macrophages
    • J.J. Miettinen, S. Matikainen, and T.A. Nyman Global secretome characterization of herpes simplex virus 1-infected human primary macrophages J Virol 86 2012 12770 12778
    • (2012) J Virol , vol.86 , pp. 12770-12778
    • Miettinen, J.J.1    Matikainen, S.2    Nyman, T.A.3


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