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Volumn 4, Issue DEC, 2013, Pages

Sensing microbial RNA in the cytosol

Author keywords

Cytosol; DExD H box helicases; Innate immune escape; Pathogen associated molecular patterns; Pattern recognition receptors; RIG I like receptors; RNA helicases

Indexed keywords


EID: 84892173964     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2013.00468     Document Type: Review
Times cited : (39)

References (115)
  • 1
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • doi: 10.1101/SQB.1989.054.01.003
    • Janeway CA Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol (1989) 54(Pt 1):1-13. doi: 10.1101/SQB.1989.054.01.003
    • (1989) Cold Spring Harb Symp Quant Biol , vol.54 , Issue.PART 1 , pp. 1-13
    • Janeway Jr., C.A.1
  • 2
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila toll protein signals activation of adaptive immunity
    • doi:10.1038/41131
    • Medzhitov R, Preston-Hurlburt P, Janeway CA Jr. A human homologue of the Drosophila toll protein signals activation of adaptive immunity. Nature (1997) 388:394-7. doi:10.1038/41131
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 3
    • 66949122854 scopus 로고    scopus 로고
    • Approaching the asymptote: 20 years later
    • doi:10.1016/j.immuni.2009.06.004
    • Medzhitov R. Approaching the asymptote: 20 years later. Immunity (2009) 30:766-75. doi:10.1016/j.immuni.2009.06.004
    • (2009) Immunity , vol.30 , pp. 766-775
    • Medzhitov, R.1
  • 4
    • 84857546470 scopus 로고    scopus 로고
    • Beyond pattern recognition: five immune checkpoints for scaling the microbial threat
    • doi:10.1038/nri3167
    • Blander JM, Sander LE. Beyond pattern recognition: five immune checkpoints for scaling the microbial threat. Nat Rev Immunol (2012) 12:215-25. doi:10.1038/nri3167
    • (2012) Nat Rev Immunol , vol.12 , pp. 215-225
    • Blander, J.M.1    Sander, L.E.2
  • 5
    • 0033515098 scopus 로고    scopus 로고
    • Activation of target-tissue immune-recognition molecules by double-stranded polynucleotides
    • doi:10.1073/pnas.96.5.2285
    • Suzuki K, Mori A, Ishii KJ, Saito J, Singer DS, Klinman DM, et al. Activation of target-tissue immune-recognition molecules by double-stranded polynucleotides. Proc Natl Acad Sci U S A (1999) 96:2285-90. doi:10.1073/pnas.96.5.2285
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 2285-2290
    • Suzuki, K.1    Mori, A.2    Ishii, K.J.3    Saito, J.4    Singer, D.S.5    Klinman, D.M.6
  • 6
    • 84878190840 scopus 로고    scopus 로고
    • Immune sensing of DNA
    • doi:10.1016/j.immuni.2013.05.004
    • Paludan SR, Bowie AG. Immune sensing of DNA. Immunity (2013) 38:870-80. doi:10.1016/j.immuni.2013.05.004
    • (2013) Immunity , vol.38 , pp. 870-880
    • Paludan, S.R.1    Bowie, A.G.2
  • 7
    • 79959242498 scopus 로고    scopus 로고
    • Detection of prokaryotic mRNA signifies microbial viability and promotes immunity
    • doi:10.1038/nature10072
    • Sander LE, Davis MJ, Boekschoten MV, Amsen D, Dascher CC, Ryffel B, et al. Detection of prokaryotic mRNA signifies microbial viability and promotes immunity. Nature (2011) 474:385-9. doi:10.1038/nature10072
    • (2011) Nature , vol.474 , pp. 385-389
    • Sander, L.E.1    Davis, M.J.2    Boekschoten, M.V.3    Amsen, D.4    Dascher, C.C.5    Ryffel, B.6
  • 8
    • 0003715206 scopus 로고    scopus 로고
    • 3rd ed. American Society Microbiology
    • Flint S. Principles of Virology. 3rd ed. American Society Microbiology (2009).
    • (2009) Principles of Virology
    • Flint, S.1
  • 9
    • 84874648730 scopus 로고    scopus 로고
    • Cell-to-cell transmission of viruses
    • doi:10.1016/j.coviro.2012.11.004
    • Zhong P, Agosto LM, Munro JB, Mothes W. Cell-to-cell transmission of viruses. Curr Opin Virol (2013) 3:44-50. doi:10.1016/j.coviro.2012.11.004
    • (2013) Curr Opin Virol , vol.3 , pp. 44-50
    • Zhong, P.1    Agosto, L.M.2    Munro, J.B.3    Mothes, W.4
  • 10
    • 77952127743 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells sense hepatitis C virus-infected cells, produce interferon, and inhibit infection
    • doi:10.1073/pnas.1002301107
    • Takahashi K, Asabe S, Wieland S, Garaigorta U, Gastaminza P, Isogawa M, et al. Plasmacytoid dendritic cells sense hepatitis C virus-infected cells, produce interferon, and inhibit infection. Proc Natl Acad Sci U S A (2010) 107:7431-6. doi:10.1073/pnas.1002301107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 7431-7436
    • Takahashi, K.1    Asabe, S.2    Wieland, S.3    Garaigorta, U.4    Gastaminza, P.5    Isogawa, M.6
  • 13
    • 0015114139 scopus 로고
    • Expression of animal virus genomes
    • Baltimore D. Expression of animal virus genomes. Bacteriol Rev (1971) 35:235-41.
    • (1971) Bacteriol Rev , vol.35 , pp. 235-241
    • Baltimore, D.1
  • 14
    • 34047196224 scopus 로고    scopus 로고
    • Bacterial ligands generated in a phagosome are targets of the cytosolic innate immune system
    • doi:10.1371/journal.ppat.0030051
    • Herskovits AA, Auerbuch V, Portnoy DA. Bacterial ligands generated in a phagosome are targets of the cytosolic innate immune system. PLoS Pathog (2007) 3:e51. doi:10.1371/journal.ppat.0030051
    • (2007) PLoS Pathog , vol.3
    • Herskovits, A.A.1    Auerbuch, V.2    Portnoy, D.A.3
  • 15
    • 84868569570 scopus 로고    scopus 로고
    • RIG-I detects infection with live Listeria by sensing secreted bacterial nucleic acids
    • doi:10.1038/emboj.2012.274
    • Abdullah Z, Schlee M, Roth S, Mraheil MA, Barchet W, Bottcher J, et al. RIG-I detects infection with live Listeria by sensing secreted bacterial nucleic acids. EMBO J (2012) 31:4153-64. doi:10.1038/emboj.2012.274
    • (2012) EMBO J , vol.31 , pp. 4153-4164
    • Abdullah, Z.1    Schlee, M.2    Roth, S.3    Mraheil, M.A.4    Barchet, W.5    Bottcher, J.6
  • 16
    • 84877004303 scopus 로고    scopus 로고
    • RIG-I detects triphosphorylated RNA of Listeria monocytogenes during infection in non-immune cells
    • doi:10.1371/journal.pone.0062872
    • Hagmann CA, Herzner AM, Abdullah Z, Zillinger T, Jakobs C, Schuberth C, et al. RIG-I detects triphosphorylated RNA of Listeria monocytogenes during infection in non-immune cells. PLoS One (2013) 8:e62872. doi:10.1371/journal.pone.0062872
    • (2013) PLoS One , vol.8
    • Hagmann, C.A.1    Herzner, A.M.2    Abdullah, Z.3    Zillinger, T.4    Jakobs, C.5    Schuberth, C.6
  • 17
    • 73549090166 scopus 로고    scopus 로고
    • Identification of host cytosolic sensors and bacterial factors regulating the type I interferon response to Legionella pneumophila
    • doi:10.1371/journal.ppat.1000665
    • Monroe KM, McWhirter SM, Vance RE. Identification of host cytosolic sensors and bacterial factors regulating the type I interferon response to Legionella pneumophila. PLoS Pathog (2009) 5:e1000665. doi:10.1371/journal.ppat.1000665
    • (2009) PLoS Pathog , vol.5
    • Monroe, K.M.1    McWhirter, S.M.2    Vance, R.E.3
  • 18
    • 70349459734 scopus 로고    scopus 로고
    • RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate
    • doi:10.1038/ni.1779
    • Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V. RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol (2009) 10:1065-72. doi:10.1038/ni.1779
    • (2009) Nat Immunol , vol.10 , pp. 1065-1072
    • Ablasser, A.1    Bauernfeind, F.2    Hartmann, G.3    Latz, E.4    Fitzgerald, K.A.5    Hornung, V.6
  • 19
    • 68049092912 scopus 로고    scopus 로고
    • RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway
    • doi:10.1016/j.cell.2009.06.015
    • Chiu YH, Macmillan JB, Chen ZJ. RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell (2009) 138:576-91. doi:10.1016/j.cell.2009.06.015
    • (2009) Cell , vol.138 , pp. 576-591
    • Chiu, Y.H.1    Macmillan, J.B.2    Chen, Z.J.3
  • 20
    • 27144440523 scopus 로고    scopus 로고
    • IPS-1, an adaptor triggering RIG-I-and Mda5-mediated type I interferon induction
    • doi:10.1038/ni1243
    • Kawai T, Takahashi K, Sato S, Coban C, Kumar H, Kato H, et al. IPS-1, an adaptor triggering RIG-I-and Mda5-mediated type I interferon induction. Nat Immunol (2005) 6:981-8. doi:10.1038/ni1243
    • (2005) Nat Immunol , vol.6 , pp. 981-988
    • Kawai, T.1    Takahashi, K.2    Sato, S.3    Coban, C.4    Kumar, H.5    Kato, H.6
  • 21
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • doi:10.1038/nature04193
    • Meylan E, Curran J, Hofmann K, Moradpour D, Binder M, Bartenschlager R, et al. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature (2005) 437:1167-72. doi:10.1038/nature04193
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5    Bartenschlager, R.6
  • 22
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3
    • doi:10.1016/j.cell.2005.08.012
    • Seth RB, Sun L, Ea CK, Chen ZJ. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell (2005) 122:669-82. doi:10.1016/j.cell.2005.08.012
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 23
    • 24944538819 scopus 로고    scopus 로고
    • VISA is an adapter protein required for virus-triggered IFN-beta signaling
    • doi:10.1016/j.molcel.2005.08.014
    • Xu LG, Wang YY, Han KJ, Li LY, Zhai Z, Shu HB. VISA is an adapter protein required for virus-triggered IFN-beta signaling. Mol Cell (2005) 19:727-40. doi:10.1016/j.molcel.2005.08.014
    • (2005) Mol Cell , vol.19 , pp. 727-740
    • Xu, L.G.1    Wang, Y.Y.2    Han, K.J.3    Li, L.Y.4    Zhai, Z.5    Shu, H.B.6
  • 24
    • 1642348822 scopus 로고    scopus 로고
    • Expression analysis and genomic characterization of human melanoma differentiation associated gene-5, mda-5: a novel type I interferon-responsive apoptosis-inducing gene
    • doi:10.1038/sj.onc.1207300
    • Kang DC, Gopalkrishnan RV, Lin L, Randolph A, Valerie K, Pestka S, et al. Expression analysis and genomic characterization of human melanoma differentiation associated gene-5, mda-5: a novel type I interferon-responsive apoptosis-inducing gene. Oncogene (2004) 23:1789-800. doi:10.1038/sj.onc.1207300
    • (2004) Oncogene , vol.23 , pp. 1789-1800
    • Kang, D.C.1    Gopalkrishnan, R.V.2    Lin, L.3    Randolph, A.4    Valerie, K.5    Pestka, S.6
  • 25
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • doi:10.1038/ni1087
    • Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T, Miyagishi M, et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat Immunol (2004) 5:730-7. doi:10.1038/ni1087
    • (2004) Nat Immunol , vol.5 , pp. 730-737
    • Yoneyama, M.1    Kikuchi, M.2    Natsukawa, T.3    Shinobu, N.4    Imaizumi, T.5    Miyagishi, M.6
  • 26
    • 33750976374 scopus 로고    scopus 로고
    • 5'-Triphosphate RNA is the ligand for RIG-I
    • doi:10.1126/science.1132505
    • Hornung V, Ellegast J, Kim S, Brzozka K, Jung A, Kato H, et al. 5'-Triphosphate RNA is the ligand for RIG-I. Science (2006) 314:994-7. doi:10.1126/science.1132505
    • (2006) Science , vol.314 , pp. 994-997
    • Hornung, V.1    Ellegast, J.2    Kim, S.3    Brzozka, K.4    Jung, A.5    Kato, H.6
  • 27
    • 33750984771 scopus 로고    scopus 로고
    • RIG-I-mediated antiviral responses to single-stranded RNA bearing 5'-phosphates
    • doi:10.1126/science.1132998
    • Pichlmair A, Schulz O, Tan CP, Naslund TI, Liljestrom P, Weber F, et al. RIG-I-mediated antiviral responses to single-stranded RNA bearing 5'-phosphates. Science (2006) 314:997-1001. doi:10.1126/science.1132998
    • (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
  • 28
    • 68049089651 scopus 로고    scopus 로고
    • Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus
    • doi:10.1016/j.immuni.2009.05.008
    • Schlee M, Roth A, Hornung V, Hagmann CA, Wimmenauer V, Barchet W, et al. Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus. Immunity (2009) 31:25-34. doi:10.1016/j.immuni.2009.05.008
    • (2009) Immunity , vol.31 , pp. 25-34
    • Schlee, M.1    Roth, A.2    Hornung, V.3    Hagmann, C.A.4    Wimmenauer, V.5    Barchet, W.6
  • 29
    • 67749133995 scopus 로고    scopus 로고
    • 5'-Triphosphate RNA requires base-paired structures to activate antiviral signaling via RIG-I
    • doi:10.1073/pnas.0900971106
    • Schmidt A, Schwerd T, Hamm W, Hellmuth JC, Cui S, Wenzel M, et al. 5'-Triphosphate RNA requires base-paired structures to activate antiviral signaling via RIG-I. Proc Natl Acad Sci U S A (2009) 106:12067-72. doi:10.1073/pnas.0900971106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 12067-12072
    • Schmidt, A.1    Schwerd, T.2    Hamm, W.3    Hellmuth, J.C.4    Cui, S.5    Wenzel, M.6
  • 30
    • 81555204380 scopus 로고    scopus 로고
    • Structural basis of RNA recognition and activation by innate immune receptor RIG-I
    • doi:10.1038/nature10537
    • Jiang F, Ramanathan A, Miller MT, Tang GQ, Gale M Jr, Patel SS, et al. Structural basis of RNA recognition and activation by innate immune receptor RIG-I. Nature (2011) 479:423-7. doi:10.1038/nature10537
    • (2011) Nature , vol.479 , pp. 423-427
    • Jiang, F.1    Ramanathan, A.2    Miller, M.T.3    Tang, G.Q.4    Gale Jr., M.5    Patel, S.S.6
  • 31
    • 80054703126 scopus 로고    scopus 로고
    • Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA
    • doi:10.1016/j.cell.2011.09.039
    • Kowalinski E, Lunardi T, McCarthy AA, Louber J, Brunel J, Grigorov B, et al. Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. Cell (2011) 147:423-35. doi:10.1016/j.cell.2011.09.039
    • (2011) Cell , vol.147 , pp. 423-435
    • Kowalinski, E.1    Lunardi, T.2    McCarthy, A.A.3    Louber, J.4    Brunel, J.5    Grigorov, B.6
  • 32
    • 80054685883 scopus 로고    scopus 로고
    • Structural insights into RNA recognition by RIG-I
    • doi:10.1016/j.cell.2011.09.023
    • Luo D, Ding SC, Vela A, Kohlway A, Lindenbach BD, Pyle AM. Structural insights into RNA recognition by RIG-I. Cell (2011) 147:409-22. doi:10.1016/j.cell.2011.09.023
    • (2011) Cell , vol.147 , pp. 409-422
    • Luo, D.1    Ding, S.C.2    Vela, A.3    Kohlway, A.4    Lindenbach, B.D.5    Pyle, A.M.6
  • 33
    • 79960990301 scopus 로고    scopus 로고
    • Molecular mechanism of signal perception and integration by the innate immune sensor retinoic acid-inducible gene-I (RIG-I)
    • doi:10.1074/jbc.M111.256974
    • Binder M, Eberle F, Seitz S, Mucke N, Huber CM, Kiani N, et al. Molecular mechanism of signal perception and integration by the innate immune sensor retinoic acid-inducible gene-I (RIG-I). J Biol Chem (2011) 286:27278-87. doi:10.1074/jbc.M111.256974
    • (2011) J Biol Chem , vol.286 , pp. 27278-27287
    • Binder, M.1    Eberle, F.2    Seitz, S.3    Mucke, N.4    Huber, C.M.5    Kiani, N.6
  • 34
    • 33646561864 scopus 로고    scopus 로고
    • A structural basis for discriminating between self and nonself double-stranded RNAs in mammalian cells
    • doi:10.1038/nbt1205
    • Marques JT, Devosse T, Wang D, Zamanian-Daryoush M, Serbinowski P, Hartmann R, et al. A structural basis for discriminating between self and nonself double-stranded RNAs in mammalian cells. Nat Biotechnol (2006) 24:559-65. doi:10.1038/nbt1205
    • (2006) Nat Biotechnol , vol.24 , pp. 559-565
    • Marques, J.T.1    Devosse, T.2    Wang, D.3    Zamanian-Daryoush, M.4    Serbinowski, P.5    Hartmann, R.6
  • 35
    • 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
    • doi:10.1084/jem.20080091
    • Kato H, Takeuchi O, Mikamo-Satoh E, Hirai R, Kawai T, Matsushita K, 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 (2008) 205:1601-10. doi:10.1084/jem.20080091
    • (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
  • 36
    • 39649092731 scopus 로고    scopus 로고
    • Nonself RNA-sensing mechanism of RIG-I helicase and activation of anti-viral immune responses
    • doi:10.1016/j.molcel.2007.11.028
    • Takahasi K, Yoneyama M, Nishihori T, Hirai R, Kumeta H, Narita R, et al. Nonself RNA-sensing mechanism of RIG-I helicase and activation of anti-viral immune responses. Mol Cell (2008) 29:428-40. doi:10.1016/j.molcel.2007.11.028
    • (2008) Mol Cell , vol.29 , pp. 428-440
    • Takahasi, K.1    Yoneyama, M.2    Nishihori, T.3    Hirai, R.4    Kumeta, H.5    Narita, R.6
  • 37
    • 84869765600 scopus 로고    scopus 로고
    • The thermodynamic basis for viral RNA detection by the RIG-I innate immune sensor
    • doi:10.1074/jbc.M112.385146
    • Vela A, Fedorova O, Ding SC, Pyle AM. The thermodynamic basis for viral RNA detection by the RIG-I innate immune sensor. J Biol Chem (2012) 287:42564-73. doi:10.1074/jbc.M112.385146
    • (2012) J Biol Chem , vol.287 , pp. 42564-42573
    • Vela, A.1    Fedorova, O.2    Ding, S.C.3    Pyle, A.M.4
  • 38
    • 75749140581 scopus 로고    scopus 로고
    • RIG-I detects viral genomic RNA during negative-strand RNA virus infection
    • doi:10.1016/j.cell.2010.01.020
    • Rehwinkel J, Tan CP, Goubau D, Schulz O, Pichlmair A, Bier K, et al. RIG-I detects viral genomic RNA during negative-strand RNA virus infection. Cell (2010) 140:397-408. doi:10.1016/j.cell.2010.01.020
    • (2010) Cell , vol.140 , pp. 397-408
    • Rehwinkel, J.1    Tan, C.P.2    Goubau, D.3    Schulz, O.4    Pichlmair, A.5    Bier, K.6
  • 39
    • 84875167118 scopus 로고    scopus 로고
    • Incoming RNA virus nucleocapsids containing a 5'-triphosphorylated genome activate RIG-I and antiviral signaling
    • doi:10.1016/j.chom.2013.01.012
    • Weber M, Gawanbacht A, Habjan M, Rang A, Borner C, Schmidt AM, et al. Incoming RNA virus nucleocapsids containing a 5'-triphosphorylated genome activate RIG-I and antiviral signaling. Cell Host Microbe (2013) 13:336-46. doi:10.1016/j.chom.2013.01.012
    • (2013) Cell Host Microbe , vol.13 , pp. 336-346
    • Weber, M.1    Gawanbacht, A.2    Habjan, M.3    Rang, A.4    Borner, C.5    Schmidt, A.M.6
  • 40
    • 33646342149 scopus 로고    scopus 로고
    • Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
    • doi:10.1038/nature04734
    • Kato H, Takeuchi O, Sato S, Yoneyama M, Yamamoto M, Matsui K, et al. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature (2006) 441:101-5. doi:10.1038/nature04734
    • (2006) Nature , vol.441 , pp. 101-105
    • Kato, H.1    Takeuchi, O.2    Sato, S.3    Yoneyama, M.4    Yamamoto, M.5    Matsui, K.6
  • 41
    • 47949092573 scopus 로고    scopus 로고
    • Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA
    • doi:10.1038/nature07106
    • Saito T, Owen DM, Jiang F, Marcotrigiano J, Gale M Jr. Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA. Nature (2008) 454:523-7. doi:10.1038/nature07106
    • (2008) Nature , vol.454 , pp. 523-527
    • Saito, T.1    Owen, D.M.2    Jiang, F.3    Marcotrigiano, J.4    Gale Jr., M.5
  • 42
    • 77957997708 scopus 로고    scopus 로고
    • Preference of RIG-I for short viral RNA molecules in infected cells revealed by next-generation sequencing
    • doi:10.1073/pnas.1005077107
    • Baum A, Sachidanandam R, Garcia-Sastre A. Preference of RIG-I for short viral RNA molecules in infected cells revealed by next-generation sequencing. Proc Natl Acad Sci U S A (2010) 107:16303-8. doi:10.1073/pnas.1005077107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 16303-16308
    • Baum, A.1    Sachidanandam, R.2    Garcia-Sastre, A.3
  • 43
    • 47049129929 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded small RNA induces IL-10 through RIG-I-mediated IRF-3 signaling
    • doi:10.1038/onc.2008.75
    • Samanta M, Iwakiri D, Takada K. Epstein-Barr virus-encoded small RNA induces IL-10 through RIG-I-mediated IRF-3 signaling. Oncogene (2008) 27:4150-60. doi:10.1038/onc.2008.75
    • (2008) Oncogene , vol.27 , pp. 4150-4160
    • Samanta, M.1    Iwakiri, D.2    Takada, K.3
  • 44
    • 79952836011 scopus 로고    scopus 로고
    • Adenovirus virus-associated RNAs induce type I interferon expression through a RIG-I-mediated pathway
    • doi:10.1128/JVI.02160-10
    • Minamitani T, Iwakiri D, Takada K. Adenovirus virus-associated RNAs induce type I interferon expression through a RIG-I-mediated pathway. J Virol (2011) 85:4035-40. doi:10.1128/JVI.02160-10
    • (2011) J Virol , vol.85 , pp. 4035-4040
    • Minamitani, T.1    Iwakiri, D.2    Takada, K.3
  • 45
    • 0027528568 scopus 로고
    • The 5' ends of RNA oligonucleotides in Escherichia coli and mRNA degradation
    • doi:10.1111/j.1432-1033.1993.tb17761.x
    • Cannistraro VJ, Kennell D. The 5' ends of RNA oligonucleotides in Escherichia coli and mRNA degradation. Eur J Biochem (1993) 213:285-93. doi:10.1111/j.1432-1033.1993.tb17761.x
    • (1993) Eur J Biochem , vol.213 , pp. 285-293
    • Cannistraro, V.J.1    Kennell, D.2
  • 46
    • 66149110970 scopus 로고    scopus 로고
    • Extracellular and intracellular pattern recognition receptors cooperate in the recognition of Helicobacter pylori
    • doi:10.1053/j.gastro.2009.02.066
    • Rad R, Ballhorn W, Voland P, Eisenacher K, Mages J, Rad L, et al. Extracellular and intracellular pattern recognition receptors cooperate in the recognition of Helicobacter pylori. Gastroenterology (2009) 136:2247-57. doi:10.1053/j.gastro.2009.02.066
    • (2009) Gastroenterology , vol.136 , pp. 2247-2257
    • Rad, R.1    Ballhorn, W.2    Voland, P.3    Eisenacher, K.4    Mages, J.5    Rad, L.6
  • 47
    • 84866151928 scopus 로고    scopus 로고
    • IFNgamma inhibits the cytosolic replication of Shigella flexneri via the cytoplasmic RNA sensor RIG-I
    • doi:10.1371/journal.ppat.1002809
    • Jehl SP, Nogueira CV, Zhang X, Starnbach MN. IFNgamma inhibits the cytosolic replication of Shigella flexneri via the cytoplasmic RNA sensor RIG-I. PLoS Pathog (2012) 8:e1002809. doi:10.1371/journal.ppat.1002809
    • (2012) PLoS Pathog , vol.8
    • Jehl, S.P.1    Nogueira, C.V.2    Zhang, X.3    Starnbach, M.N.4
  • 48
    • 33744791510 scopus 로고    scopus 로고
    • Essential role of mda-5 in type I IFN responses to polyriboinosinic:polyribocytidylic acid and encephalomyocarditis picornavirus
    • doi:10.1073/pnas.0603082103
    • Gitlin L, Barchet W, Gilfillan S, Cella M, Beutler B, Flavell RA, et al. Essential role of mda-5 in type I IFN responses to polyriboinosinic:polyribocytidylic acid and encephalomyocarditis picornavirus. Proc Natl Acad Sci U S A (2006) 103:8459-64. doi:10.1073/pnas.0603082103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8459-8464
    • Gitlin, L.1    Barchet, W.2    Gilfillan, S.3    Cella, M.4    Beutler, B.5    Flavell, R.A.6
  • 49
    • 84872604349 scopus 로고    scopus 로고
    • Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5
    • doi:10.1016/j.cell.2012.11.048
    • Wu B, Peisley A, Richards C, Yao H, Zeng X, Lin C, et al. Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5. Cell (2013) 152:276-89. doi:10.1016/j.cell.2012.11.048
    • (2013) Cell , vol.152 , pp. 276-289
    • Wu, B.1    Peisley, A.2    Richards, C.3    Yao, H.4    Zeng, X.5    Lin, C.6
  • 50
    • 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
    • doi:10.1128/JVI.80.10.5059-5064.2006
    • Weber F, Wagner V, Rasmussen SB, Hartmann R, Paludan SR. 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 (2006) 80:5059-64. doi:10.1128/JVI.80.10.5059-5064.2006
    • (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
  • 51
    • 70349728538 scopus 로고    scopus 로고
    • Activation of MDA5 requires higher-order RNA structures generated during virus infection
    • doi:10.1128/JVI.00770-09
    • Pichlmair A, Schulz O, Tan CP, Rehwinkel J, Kato H, Takeuchi O, et al. Activation of MDA5 requires higher-order RNA structures generated during virus infection. J Virol (2009) 83:10761-9. doi:10.1128/JVI.00770-09
    • (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
  • 52
    • 84870476784 scopus 로고    scopus 로고
    • MDA5 detects the double-stranded RNA replicative form in picornavirus-infected cells
    • doi:10.1016/j.celrep.2012.10.005
    • Feng Q, Hato SV, Langereis MA, Zoll J, Virgen-Slane R, Peisley A, et al. MDA5 detects the double-stranded RNA replicative form in picornavirus-infected cells. Cell Rep (2012) 2:1187-96. doi:10.1016/j.celrep.2012.10.005
    • (2012) Cell Rep , vol.2 , pp. 1187-1196
    • Feng, Q.1    Hato, S.V.2    Langereis, M.A.3    Zoll, J.4    Virgen-Slane, R.5    Peisley, A.6
  • 53
    • 84878781543 scopus 로고    scopus 로고
    • Innate immune response after adenoviral gene delivery into skin is mediated by AIM2, NALP3, DAI and mda5
    • doi:10.1186/2193-1801-2-234
    • Schulte M, Sorkin M, Al-Benna S, Stupka J, Hirsch T, Daigeler A, et al. Innate immune response after adenoviral gene delivery into skin is mediated by AIM2, NALP3, DAI and mda5. Springerplus (2013) 2:234. doi:10.1186/2193-1801-2-234
    • (2013) Springerplus , vol.2 , pp. 234
    • Schulte, M.1    Sorkin, M.2    Al-Benna, S.3    Stupka, J.4    Hirsch, T.5    Daigeler, A.6
  • 54
    • 84883491208 scopus 로고    scopus 로고
    • Visualisation of direct interaction of MDA5 and the dsRNA replicative intermediate form of positive strand RNA viruses
    • doi:10.1242/jcs.103887
    • Triantafilou K, Vakakis E, Kar S, Richer E, Evans GL, Triantafilou M. Visualisation of direct interaction of MDA5 and the dsRNA replicative intermediate form of positive strand RNA viruses. J Cell Sci (2012) 125:4761-9. doi:10.1242/jcs.103887
    • (2012) J Cell Sci , vol.125 , pp. 4761-4769
    • Triantafilou, K.1    Vakakis, E.2    Kar, S.3    Richer, E.4    Evans, G.L.5    Triantafilou, M.6
  • 55
    • 79952125382 scopus 로고    scopus 로고
    • Activation of IFN-β expression by a viral mRNA through RNase L and MDA5
    • doi:10.1073/pnas.1012409108
    • Luthra P, Sun D, Silverman RH, He B. Activation of IFN-β expression by a viral mRNA through RNase L and MDA5. Proc Natl Acad Sci U S A (2011) 108:2118-23. doi:10.1073/pnas.1012409108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2118-2123
    • Luthra, P.1    Sun, D.2    Silverman, R.H.3    He, B.4
  • 56
    • 78651484480 scopus 로고    scopus 로고
    • New insights into the role of RNase L in innate immunity
    • doi:10.1089/jir.2010.0120
    • Chakrabarti A, Jha BK, Silverman RH. New insights into the role of RNase L in innate immunity. J Interferon Cytokine Res (2011) 31:49-57. doi:10.1089/jir.2010.0120
    • (2011) J Interferon Cytokine Res , vol.31 , pp. 49-57
    • Chakrabarti, A.1    Jha, B.K.2    Silverman, R.H.3
  • 57
    • 78751637122 scopus 로고    scopus 로고
    • Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5
    • doi:10.1038/ni.1979
    • Zust R, Cervantes-Barragan L, Habjan M, Maier R, Neuman BW, Ziebuhr J, et al. Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5. Nat Immunol (2011) 12:137-43. doi:10.1038/ni.1979
    • (2011) Nat Immunol , vol.12 , pp. 137-143
    • Zust, R.1    Cervantes-Barragan, L.2    Habjan, M.3    Maier, R.4    Neuman, B.W.5    Ziebuhr, J.6
  • 58
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • doi:10.1016/j.cell.2011.06.041
    • Hou F, Sun L, Zheng H, Skaug B, Jiang QX, Chen ZJ. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell (2011) 146:448-61. doi:10.1016/j.cell.2011.06.041
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1    Sun, L.2    Zheng, H.3    Skaug, B.4    Jiang, Q.X.5    Chen, Z.J.6
  • 59
    • 84876698263 scopus 로고    scopus 로고
    • Intracellular pathogen detection by RIG-I-like receptors
    • doi:10.1016/B978-0-12-410524-9.00004-9
    • Dixit E, Kagan JC. Intracellular pathogen detection by RIG-I-like receptors. Adv Immunol (2013) 117:99-125. doi:10.1016/B978-0-12-410524-9.00004-9
    • (2013) Adv Immunol , vol.117 , pp. 99-125
    • Dixit, E.1    Kagan, J.C.2
  • 60
    • 84876237736 scopus 로고    scopus 로고
    • The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation
    • doi:10.1016/j.cell.2013.02.054
    • Subramanian N, Natarajan K, Clatworthy MR, Wang Z, Germain RN. The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation. Cell (2013) 153:348-61. doi:10.1016/j.cell.2013.02.054
    • (2013) Cell , vol.153 , pp. 348-361
    • Subramanian, N.1    Natarajan, K.2    Clatworthy, M.R.3    Wang, Z.4    Germain, R.N.5
  • 61
    • 74049126045 scopus 로고    scopus 로고
    • Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1 beta production
    • doi:10.1038/ni.1824
    • Poeck H, Bscheider M, Gross O, Finger K, Roth S, Rebsamen M, et al. Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1 beta production. Nat Immunol (2010) 11:63-9. doi:10.1038/ni.1824
    • (2010) Nat Immunol , vol.11 , pp. 63-69
    • Poeck, H.1    Bscheider, M.2    Gross, O.3    Finger, K.4    Roth, S.5    Rebsamen, M.6
  • 62
    • 84876833883 scopus 로고    scopus 로고
    • Type I IFN triggers RIG-I/TLR3/NLRP3-dependent inflammasome activation in influenza A virus infected cells
    • doi:10.1371/journal.ppat.1003256
    • Pothlichet J, Meunier I, Davis BK, Ting JP, Skamene E, von Messling V, et al. Type I IFN triggers RIG-I/TLR3/NLRP3-dependent inflammasome activation in influenza A virus infected cells. PLoS Pathog (2013) 9:e1003256. doi:10.1371/journal.ppat.1003256
    • (2013) PLoS Pathog , vol.9
    • Pothlichet, J.1    Meunier, I.2    Davis, B.K.3    Ting, J.P.4    Skamene, E.5    von Messling, V.6
  • 63
    • 67649413594 scopus 로고    scopus 로고
    • The RIG-I-like receptor LGP2 recognizes the termini of double-stranded RNA
    • doi:10.1074/jbc.M900818200
    • Li X, Ranjith-Kumar CT, Brooks MT, Dharmaiah S, Herr AB, Kao C, et al. The RIG-I-like receptor LGP2 recognizes the termini of double-stranded RNA. J Biol Chem (2009) 284:13881-91. doi:10.1074/jbc.M900818200
    • (2009) J Biol Chem , vol.284 , pp. 13881-13891
    • Li, X.1    Ranjith-Kumar, C.T.2    Brooks, M.T.3    Dharmaiah, S.4    Herr, A.B.5    Kao, C.6
  • 64
    • 64549126847 scopus 로고    scopus 로고
    • The regulatory domain of the RIG-I family ATPase LGP2 senses double-stranded RNA
    • doi:10.1093/nar/gkp059
    • Pippig DA, Hellmuth JC, Cui S, Kirchhofer A, Lammens K, Lammens A, et al. The regulatory domain of the RIG-I family ATPase LGP2 senses double-stranded RNA. Nucleic Acids Res (2009) 37:2014-25. doi:10.1093/nar/gkp059
    • (2009) Nucleic Acids Res , vol.37 , pp. 2014-2025
    • Pippig, D.A.1    Hellmuth, J.C.2    Cui, S.3    Kirchhofer, A.4    Lammens, K.5    Lammens, A.6
  • 65
    • 76549109497 scopus 로고    scopus 로고
    • LGP2 is a positive regulator of RIG-I-and MDA5-mediated antiviral responses
    • doi:10.1073/pnas.0912986107
    • Satoh T, Kato H, Kumagai Y, Yoneyama M, Sato S, Matsushita K, et al. LGP2 is a positive regulator of RIG-I-and MDA5-mediated antiviral responses. Proc Natl Acad Sci U S A (2010) 107:1512-7. doi:10.1073/pnas.0912986107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1512-1517
    • Satoh, T.1    Kato, H.2    Kumagai, Y.3    Yoneyama, M.4    Sato, S.5    Matsushita, K.6
  • 66
    • 84872348735 scopus 로고    scopus 로고
    • ATP hydrolysis enhances RNA recognition and antiviral signal transduction by the innate immune sensor, laboratory of genetics and physiology 2 (LGP2)
    • doi:10.1074/jbc.M112.424416
    • Bruns AM, Pollpeter D, Hadizadeh N, Myong S, Marko JF, Horvath CM. ATP hydrolysis enhances RNA recognition and antiviral signal transduction by the innate immune sensor, laboratory of genetics and physiology 2 (LGP2). J Biol Chem (2013) 288:938-46. doi:10.1074/jbc.M112.424416
    • (2013) J Biol Chem , vol.288 , pp. 938-946
    • Bruns, A.M.1    Pollpeter, D.2    Hadizadeh, N.3    Myong, S.4    Marko, J.F.5    Horvath, C.M.6
  • 67
    • 84877326407 scopus 로고    scopus 로고
    • LGP2 plays a critical role in sensitizing mda-5 to activation by double-stranded RNA
    • doi:10.1371/journal.pone.0064202
    • Childs KS, Randall RE, Goodbourn S. LGP2 plays a critical role in sensitizing mda-5 to activation by double-stranded RNA. PLoS One (2013) 8:e64202. doi:10.1371/journal.pone.0064202
    • (2013) PLoS One , vol.8
    • Childs, K.S.1    Randall, R.E.2    Goodbourn, S.3
  • 68
    • 79960724199 scopus 로고    scopus 로고
    • From unwinding to clamping-the DEAD box RNA helicase family
    • doi:10.1038/nrm3154
    • Linder P, Jankowsky E. From unwinding to clamping-the DEAD box RNA helicase family. Nat Rev Mol Cell Biol (2011) 12:505-16. doi:10.1038/nrm3154
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 505-516
    • Linder, P.1    Jankowsky, E.2
  • 69
    • 84878108881 scopus 로고    scopus 로고
    • DExD/H-box RNA helicases as mediators of anti-viral innate immunity and essential host factors for viral replication
    • doi:10.1016/j.bbagrm.2013.03.012
    • Fullam A, Schroder M. DExD/H-box RNA helicases as mediators of anti-viral innate immunity and essential host factors for viral replication. Biochim Biophys Acta (2013) 1829:854-65. doi:10.1016/j.bbagrm.2013.03.012
    • (2013) Biochim Biophys Acta , vol.1829 , pp. 854-865
    • Fullam, A.1    Schroder, M.2
  • 70
    • 77951044335 scopus 로고    scopus 로고
    • DEAD/H BOX 3 (DDX3) helicase binds the RIG-I adaptor IPS-1 to up-regulate IFN-beta-inducing potential
    • doi:10.1002/eji.200940203
    • Oshiumi H, Sakai K, Matsumoto M, Seya T. DEAD/H BOX 3 (DDX3) helicase binds the RIG-I adaptor IPS-1 to up-regulate IFN-beta-inducing potential. Eur J Immunol (2010) 40:940-8. doi:10.1002/eji.200940203
    • (2010) Eur J Immunol , vol.40 , pp. 940-948
    • Oshiumi, H.1    Sakai, K.2    Matsumoto, M.3    Seya, T.4
  • 71
    • 49149113373 scopus 로고    scopus 로고
    • Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKKepsilon-mediated IRF activation
    • doi:10.1038/emboj.2008.143
    • Schroder M, Baran M, Bowie AG. Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKKepsilon-mediated IRF activation. EMBO J (2008) 27:2147-57. doi:10.1038/emboj.2008.143
    • (2008) EMBO J , vol.27 , pp. 2147-2157
    • Schroder, M.1    Baran, M.2    Bowie, A.G.3
  • 72
    • 78650127763 scopus 로고    scopus 로고
    • Hepatitis C virus core protein abrogates the DDX3 function that enhances IPS-1-mediated IFN-beta induction
    • doi:10.1371/journal.pone.0014258
    • Oshiumi H, Ikeda M, Matsumoto M, Watanabe A, Takeuchi O, Akira S, et al. Hepatitis C virus core protein abrogates the DDX3 function that enhances IPS-1-mediated IFN-beta induction. PLoS One (2010) 5:e14258. doi:10.1371/journal.pone.0014258
    • (2010) PLoS One , vol.5
    • Oshiumi, H.1    Ikeda, M.2    Matsumoto, M.3    Watanabe, A.4    Takeuchi, O.5    Akira, S.6
  • 73
    • 80555133355 scopus 로고    scopus 로고
    • DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells
    • doi:10.4049/jimmunol.1101307
    • Zhang Z, Yuan B, Lu N, Facchinetti V, Liu YJ. DHX9 pairs with IPS-1 to sense double-stranded RNA in myeloid dendritic cells. J Immunol (2011) 187:4501-8. doi:10.4049/jimmunol.1101307
    • (2011) J Immunol , vol.187 , pp. 4501-4508
    • Zhang, Z.1    Yuan, B.2    Lu, N.3    Facchinetti, V.4    Liu, Y.J.5
  • 74
    • 79959344720 scopus 로고    scopus 로고
    • DDX1, DDX21, and DHX36 helicases form a complex with the adaptor molecule TRIF to sense dsRNA in dendritic cells
    • doi:10.1016/j.immuni.2011.03.027
    • Zhang Z, Kim T, Bao M, Facchinetti V, Jung SY, Ghaffari AA, et al. DDX1, DDX21, and DHX36 helicases form a complex with the adaptor molecule TRIF to sense dsRNA in dendritic cells. Immunity (2011) 34:866-78. doi:10.1016/j.immuni.2011.03.027
    • (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
  • 75
    • 77957009390 scopus 로고    scopus 로고
    • Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A helicases sense microbial DNA in human plasmacytoid dendritic cells
    • doi:10.1073/pnas.1006539107
    • Kim T, Pazhoor S, Bao M, Zhang Z, Hanabuchi S, Facchinetti V, 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 U S A (2010) 107:15181-6. doi:10.1073/pnas.1006539107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 15181-15186
    • Kim, T.1    Pazhoor, S.2    Bao, M.3    Zhang, Z.4    Hanabuchi, S.5    Facchinetti, V.6
  • 76
    • 84880745984 scopus 로고    scopus 로고
    • The DHX33 RNA helicase senses cytosolic RNA and activates the NLRP3 inflammasome
    • doi:10.1016/j.immuni.2013.07.001
    • Mitoma H, Hanabuchi S, Kim T, Bao M, Zhang Z, Sugimoto N, et al. The DHX33 RNA helicase senses cytosolic RNA and activates the NLRP3 inflammasome. Immunity (2013) 39:123-35. doi:10.1016/j.immuni.2013.07.001
    • (2013) Immunity , vol.39 , pp. 123-135
    • Mitoma, H.1    Hanabuchi, S.2    Kim, T.3    Bao, M.4    Zhang, Z.5    Sugimoto, N.6
  • 77
    • 84891802708 scopus 로고    scopus 로고
    • The interaction between the helicase DHX33 and IPS-1 as a novel pathway to sense double-stranded RNA and RNA viruses in myeloid dendritic cells
    • doi: 10.1038/cmi.2013.40
    • Liu Y, Lu N, Yuan B, Weng L, Wang F, Liu YJ, et al. The interaction between the helicase DHX33 and IPS-1 as a novel pathway to sense double-stranded RNA and RNA viruses in myeloid dendritic cells. Cell Mol Immunol (2013). doi:10.1038/cmi.2013.40
    • (2013) Cell Mol Immunol
    • Liu, Y.1    Lu, N.2    Yuan, B.3    Weng, L.4    Wang, F.5    Liu, Y.J.6
  • 78
    • 80052603804 scopus 로고    scopus 로고
    • DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-like receptor-mediated signaling
    • doi:10.1128/MCB.01368-10
    • Miyashita M, Oshiumi H, Matsumoto M, Seya T. DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-like receptor-mediated signaling. Mol Cell Biol (2011) 31:3802-19. doi:10.1128/MCB.01368-10
    • (2011) Mol Cell Biol , vol.31 , pp. 3802-3819
    • Miyashita, M.1    Oshiumi, H.2    Matsumoto, M.3    Seya, T.4
  • 79
    • 84878173821 scopus 로고    scopus 로고
    • Cytosolic sensing of viruses
    • doi:10.1016/j.immuni.2013.05.007
    • Goubau D, Deddouche S, Reis ES. Cytosolic sensing of viruses. Immunity (2013) 38:855-69. doi:10.1016/j.immuni.2013.05.007
    • (2013) Immunity , vol.38 , pp. 855-869
    • Goubau, D.1    Deddouche, S.2    Reis, E.S.3
  • 80
    • 46249115827 scopus 로고    scopus 로고
    • Interferon-inducible antiviral effectors
    • doi:10.1038/nri2314
    • Sadler AJ, Williams BR. Interferon-inducible antiviral effectors. Nat Rev Immunol (2008) 8:559-68. doi:10.1038/nri2314
    • (2008) Nat Rev Immunol , vol.8 , pp. 559-568
    • Sadler, A.J.1    Williams, B.R.2
  • 81
    • 36749086446 scopus 로고    scopus 로고
    • 5'-Triphosphate-dependent activation of PKR by RNAs with short stem-loops
    • doi:10.1126/science.1147347
    • Nallagatla SR, Hwang J, Toroney R, Zheng X, Cameron CE, Bevilacqua PC. 5'-Triphosphate-dependent activation of PKR by RNAs with short stem-loops. Science (2007) 318:1455-8. doi:10.1126/science.1147347
    • (2007) Science , vol.318 , pp. 1455-1458
    • Nallagatla, S.R.1    Hwang, J.2    Toroney, R.3    Zheng, X.4    Cameron, C.E.5    Bevilacqua, P.C.6
  • 83
    • 84874671928 scopus 로고    scopus 로고
    • Structural basis for viral 5'-PPP-RNA recognition by human IFIT proteins
    • doi:10.1038/nature11783
    • Abbas YM, Pichlmair A, Gorna MW, Superti-Furga G, Nagar B. Structural basis for viral 5'-PPP-RNA recognition by human IFIT proteins. Nature (2013) 494:60-4. doi:10.1038/nature11783
    • (2013) Nature , vol.494 , pp. 60-64
    • Abbas, Y.M.1    Pichlmair, A.2    Gorna, M.W.3    Superti-Furga, G.4    Nagar, B.5
  • 84
    • 84883310180 scopus 로고    scopus 로고
    • Ifit1 inhibits Japanese encephalitis virus replication through binding to 5' capped 2'-O unmethylated RNA
    • doi:10.1128/JVI.00883-13
    • Kimura T, Katoh H, Kayama H, Saiga H, Okuyama M, Okamoto T, et al. Ifit1 inhibits Japanese encephalitis virus replication through binding to 5' capped 2'-O unmethylated RNA. J Virol (2013) 87:9997-10003. doi:10.1128/JVI.00883-13
    • (2013) J Virol , vol.87 , pp. 9997-10003
    • Kimura, T.1    Katoh, H.2    Kayama, H.3    Saiga, H.4    Okuyama, M.5    Okamoto, T.6
  • 85
    • 78549284909 scopus 로고    scopus 로고
    • 2'-O methylation of the viral mRNA cap evades host restriction by IFIT family members
    • doi:10.1038/nature09489
    • Daffis S, Szretter KJ, Schriewer J, Li J, Youn S, Errett J, et al. 2'-O methylation of the viral mRNA cap evades host restriction by IFIT family members. Nature (2010) 468:452-6. doi:10.1038/nature09489
    • (2010) Nature , vol.468 , pp. 452-456
    • Daffis, S.1    Szretter, K.J.2    Schriewer, J.3    Li, J.4    Youn, S.5    Errett, J.6
  • 86
    • 84863711523 scopus 로고    scopus 로고
    • 2'-O methylation of the viral mRNA cap by West Nile virus evades ifit1-dependent and-independent mechanisms of host restriction in vivo
    • doi:10.1371/journal.ppat.1002698
    • Szretter KJ, Daniels BP, Cho H, Gainey MD, Yokoyama WM, Gale M Jr, et al. 2'-O methylation of the viral mRNA cap by West Nile virus evades ifit1-dependent and-independent mechanisms of host restriction in vivo. PLoS Pathog (2012) 8:e1002698. doi:10.1371/journal.ppat.1002698
    • (2012) PLoS Pathog , vol.8
    • Szretter, K.J.1    Daniels, B.P.2    Cho, H.3    Gainey, M.D.4    Yokoyama, W.M.5    Gale Jr., M.6
  • 87
    • 84865802844 scopus 로고    scopus 로고
    • Crystal structure of ISG54 reveals a novel RNA binding structure and potential functional mechanisms
    • doi:10.1038/cr.2012.111
    • Yang Z, Liang H, Zhou Q, Li Y, Chen H, Ye W, et al. Crystal structure of ISG54 reveals a novel RNA binding structure and potential functional mechanisms. Cell Res (2012) 22:1328-38. doi:10.1038/cr.2012.111
    • (2012) Cell Res , vol.22 , pp. 1328-1338
    • Yang, Z.1    Liang, H.2    Zhou, Q.3    Li, Y.4    Chen, H.5    Ye, W.6
  • 89
    • 33846014297 scopus 로고    scopus 로고
    • Critical role for cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double-stranded RNA
    • doi:10.1074/jbc.M607594200
    • Kanneganti TD, Body-Malapel M, Amer A, Park JH, Whitfield J, Franchi L, et al. Critical role for cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double-stranded RNA. J Biol Chem (2006) 281:36560-8. doi:10.1074/jbc.M607594200
    • (2006) J Biol Chem , vol.281 , pp. 36560-36568
    • Kanneganti, T.D.1    Body-Malapel, M.2    Amer, A.3    Park, J.H.4    Whitfield, J.5    Franchi, L.6
  • 90
    • 64049111768 scopus 로고    scopus 로고
    • The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA
    • doi:10.1016/j.immuni.2009.02.005
    • Allen IC, Scull MA, Moore CB, Holl EK, McElvania-Tekippe E, Taxman DJ, et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity (2009) 30:556-65. doi:10.1016/j.immuni.2009.02.005
    • (2009) Immunity , vol.30 , pp. 556-565
    • Allen, I.C.1    Scull, M.A.2    Moore, C.B.3    Holl, E.K.4    McElvania-Tekippe, E.5    Taxman, D.J.6
  • 91
    • 77952566304 scopus 로고    scopus 로고
    • The cytosolic nucleic acid sensor LRRFIP1 mediates the production of type I interferon via a beta-catenin-dependent pathway
    • doi:10.1038/ni.1876
    • Yang P, An H, Liu X, Wen M, Zheng Y, Rui Y, et al. The cytosolic nucleic acid sensor LRRFIP1 mediates the production of type I interferon via a beta-catenin-dependent pathway. Nat Immunol (2010) 11:487-94. doi:10.1038/ni.1876
    • (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
  • 93
    • 67650169079 scopus 로고    scopus 로고
    • Patterns of oligonucleotide sequences in viral and host cell RNA identify mediators of the host innate immune system
    • doi:10.1371/journal.pone.0005969
    • Greenbaum BD, Rabadan R, Levine AJ. Patterns of oligonucleotide sequences in viral and host cell RNA identify mediators of the host innate immune system. PLoS One (2009) 4:e5969. doi:10.1371/journal.pone.0005969
    • (2009) PLoS One , vol.4
    • Greenbaum, B.D.1    Rabadan, R.2    Levine, A.J.3
  • 94
    • 79952858062 scopus 로고    scopus 로고
    • Oligonucleotide motifs that disappear during the evolution of influenza virus in humans increase alpha interferon secretion by plasmacytoid dendritic cells
    • doi:10.1128/JVI.01908-10
    • Jimenez-Baranda S, Greenbaum B, Manches O, Handler J, Rabadan R, Levine A, et al. Oligonucleotide motifs that disappear during the evolution of influenza virus in humans increase alpha interferon secretion by plasmacytoid dendritic cells. J Virol (2011) 85:3893-904. doi:10.1128/JVI.01908-10
    • (2011) J Virol , vol.85 , pp. 3893-3904
    • Jimenez-Baranda, S.1    Greenbaum, B.2    Manches, O.3    Handler, J.4    Rabadan, R.5    Levine, A.6
  • 95
    • 84859991845 scopus 로고    scopus 로고
    • The biased nucleotide composition of HIV-1 triggers type I interferon response and correlates with subtype D increased pathogenicity
    • doi:10.1371/journal.pone.0033502
    • Vabret N, Bailly-Bechet M, Najburg V, Muller-Trutwin M, Verrier B, Tangy F. The biased nucleotide composition of HIV-1 triggers type I interferon response and correlates with subtype D increased pathogenicity. PLoS One (2012) 7:e33502. doi:10.1371/journal.pone.0033502
    • (2012) PLoS One , vol.7
    • Vabret, N.1    Bailly-Bechet, M.2    Najburg, V.3    Muller-Trutwin, M.4    Verrier, B.5    Tangy, F.6
  • 96
    • 44149112583 scopus 로고    scopus 로고
    • Nucleoside modifications modulate activation of the protein kinase PKR in an RNA structure-specific manner
    • doi:10.1261/rna.1007408
    • Nallagatla SR, Bevilacqua PC. Nucleoside modifications modulate activation of the protein kinase PKR in an RNA structure-specific manner. RNA (2008) 14:1201-13. doi:10.1261/rna.1007408
    • (2008) RNA , vol.14 , pp. 1201-1213
    • Nallagatla, S.R.1    Bevilacqua, P.C.2
  • 97
    • 84874612971 scopus 로고    scopus 로고
    • Native tertiary structure and nucleoside modifications suppress tRNA's intrinsic ability to activate the innate immune sensor PKR
    • doi:10.1371/journal.pone.0057905
    • Nallagatla SR, Jones CN, Ghosh SK, Sharma SD, Cameron CE, Spremulli LL, et al. Native tertiary structure and nucleoside modifications suppress tRNA's intrinsic ability to activate the innate immune sensor PKR. PLoS One (2013) 8:e57905. doi:10.1371/journal.pone.0057905
    • (2013) PLoS One , vol.8
    • Nallagatla, S.R.1    Jones, C.N.2    Ghosh, S.K.3    Sharma, S.D.4    Cameron, C.E.5    Spremulli, L.L.6
  • 98
    • 80054732966 scopus 로고    scopus 로고
    • Inosine-containing RNA is a novel innate immune recognition element and reduces RSV infection
    • doi:10.1371/journal.pone.0026463
    • Liao JY, Thakur SA, Zalinger ZB, Gerrish KE, Imani F. Inosine-containing RNA is a novel innate immune recognition element and reduces RSV infection. PLoS One (2011) 6:e26463. doi:10.1371/journal.pone.0026463
    • (2011) PLoS One , vol.6
    • Liao, J.Y.1    Thakur, S.A.2    Zalinger, Z.B.3    Gerrish, K.E.4    Imani, F.5
  • 99
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • doi:10.1038/nrm2838
    • Jackson RJ, Hellen CU, Pestova TV. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol (2010) 11:113-27. doi:10.1038/nrm2838
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 100
    • 65449115788 scopus 로고    scopus 로고
    • Targeting of immune signalling networks by bacterial pathogens
    • doi:10.1038/ncb0509-521
    • Brodsky IE, Medzhitov R. Targeting of immune signalling networks by bacterial pathogens. Nat Cell Biol (2009) 11:521-6. doi:10.1038/ncb0509-521
    • (2009) Nat Cell Biol , vol.11 , pp. 521-526
    • Brodsky, I.E.1    Medzhitov, R.2
  • 101
    • 44349143815 scopus 로고    scopus 로고
    • Processing of genome 5' termini as a strategy of negative-strand RNA viruses to avoid RIG-I-dependent interferon induction
    • doi:10.1371/journal.pone.0002032
    • Habjan M, Andersson I, Klingstrom J, Schumann M, Martin A, Zimmermann P, et al. Processing of genome 5' termini as a strategy of negative-strand RNA viruses to avoid RIG-I-dependent interferon induction. PLoS One (2008) 3:e2032. doi:10.1371/journal.pone.0002032
    • (2008) PLoS One , vol.3
    • Habjan, M.1    Andersson, I.2    Klingstrom, J.3    Schumann, M.4    Martin, A.5    Zimmermann, P.6
  • 102
    • 79953166075 scopus 로고    scopus 로고
    • Short double-stranded RNAs with an overhanging 5' ppp-nucleotide, as found in arenavirus genomes, act as RIG-I decoys
    • doi:10.1074/jbc.M110.186262
    • Marq JB, Hausmann S, Veillard N, Kolakofsky D, Garcin D. Short double-stranded RNAs with an overhanging 5' ppp-nucleotide, as found in arenavirus genomes, act as RIG-I decoys. J Biol Chem (2011) 286:6108-16. doi:10.1074/jbc.M110.186262
    • (2011) J Biol Chem , vol.286 , pp. 6108-6116
    • Marq, J.B.1    Hausmann, S.2    Veillard, N.3    Kolakofsky, D.4    Garcin, D.5
  • 103
    • 0002027029 scopus 로고
    • A new evolutionary law
    • Van Valen L. A new evolutionary law. Evol Theory (1973) 1:1-30.
    • (1973) Evol Theory , vol.1 , pp. 1-30
    • Van Valen, L.1
  • 104
    • 84856853136 scopus 로고    scopus 로고
    • Identification of modifications in microbial, native tRNA that suppress immunostimulatory activity
    • doi:10.1084/jem.20111044
    • Gehrig S, Eberle ME, Botschen F, Rimbach K, Eberle F, Eigenbrod T, et al. Identification of modifications in microbial, native tRNA that suppress immunostimulatory activity. J Exp Med (2012) 209:225-33. doi:10.1084/jem.20111044
    • (2012) J Exp Med , vol.209 , pp. 225-233
    • Gehrig, S.1    Eberle, M.E.2    Botschen, F.3    Rimbach, K.4    Eberle, F.5    Eigenbrod, T.6
  • 105
    • 84863115824 scopus 로고    scopus 로고
    • The 2'-O-methylation status of a single guanosine controls transfer RNA-mediated toll-like receptor 7 activation or inhibition
    • doi:10.1084/jem.20111075
    • Jockel S, Nees G, Sommer R, Zhao Y, Cherkasov D, Hori H, et al. The 2'-O-methylation status of a single guanosine controls transfer RNA-mediated toll-like receptor 7 activation or inhibition. J Exp Med (2012) 209:235-41. doi:10.1084/jem.20111075
    • (2012) J Exp Med , vol.209 , pp. 235-241
    • Jockel, S.1    Nees, G.2    Sommer, R.3    Zhao, Y.4    Cherkasov, D.5    Hori, H.6
  • 106
    • 77953280422 scopus 로고    scopus 로고
    • Viral reorganization of the secretory pathway generates distinct organelles for RNA replication
    • doi:10.1016/j.cell.2010.03.050
    • Hsu NY, Ilnytska O, Belov G, Santiana M, Chen YH, Takvorian PM, et al. Viral reorganization of the secretory pathway generates distinct organelles for RNA replication. Cell (2010) 141:799-811. doi:10.1016/j.cell.2010.03.050
    • (2010) Cell , vol.141 , pp. 799-811
    • Hsu, N.Y.1    Ilnytska, O.2    Belov, G.3    Santiana, M.4    Chen, Y.H.5    Takvorian, P.M.6
  • 107
    • 77956622041 scopus 로고    scopus 로고
    • Tick-borne encephalitis virus delays interferon induction and hides its double-stranded RNA in intracellular membrane vesicles
    • doi:10.1128/JVI.00176-10
    • Overby AK, Popov VL, Niedrig M, Weber F. Tick-borne encephalitis virus delays interferon induction and hides its double-stranded RNA in intracellular membrane vesicles. J Virol (2010) 84:8470-83. doi:10.1128/JVI.00176-10
    • (2010) J Virol , vol.84 , pp. 8470-8483
    • Overby, A.K.1    Popov, V.L.2    Niedrig, M.3    Weber, F.4
  • 108
    • 80052058424 scopus 로고    scopus 로고
    • Delayed cytosolic exposure of Japanese encephalitis virus double-stranded RNA impedes interferon activation and enhances viral dissemination in porcine cells
    • doi:10.1128/JVI.00233-11
    • Espada-Murao LA, Morita K. Delayed cytosolic exposure of Japanese encephalitis virus double-stranded RNA impedes interferon activation and enhances viral dissemination in porcine cells. J Virol (2011) 85:6736-49. doi:10.1128/JVI.00233-11
    • (2011) J Virol , vol.85 , pp. 6736-6749
    • Espada-Murao, L.A.1    Morita, K.2
  • 109
    • 84856554180 scopus 로고    scopus 로고
    • Formation of membrane-defined compartments by tick-borne encephalitis virus contributes to the early delay in interferon signaling
    • doi:10.1016/j.virusres.2011.11.020
    • Miorin L, Albornoz A, Baba MM, D'Agaro P, Marcello A. Formation of membrane-defined compartments by tick-borne encephalitis virus contributes to the early delay in interferon signaling. Virus Res (2012) 163:660-6. doi:10.1016/j.virusres.2011.11.020
    • (2012) Virus Res , vol.163 , pp. 660-666
    • Miorin, L.1    Albornoz, A.2    Baba, M.M.3    D'Agaro, P.4    Marcello, A.5
  • 110
    • 57749169511 scopus 로고    scopus 로고
    • X-ray structure of NS1 from a highly pathogenic H5N1 influenza virus
    • doi:10.1038/nature07444
    • Bornholdt ZA, Prasad BV. X-ray structure of NS1 from a highly pathogenic H5N1 influenza virus. Nature (2008) 456:985-8. doi:10.1038/nature07444
    • (2008) Nature , vol.456 , pp. 985-988
    • Bornholdt, Z.A.1    Prasad, B.V.2
  • 111
    • 81755166311 scopus 로고    scopus 로고
    • The genome-linked protein VPg of vertebrate viruses-a multifaceted protein
    • doi:10.1016/j.coviro.2011.09.003
    • Goodfellow I. The genome-linked protein VPg of vertebrate viruses-a multifaceted protein. Curr Opin Virol (2011) 1:355-62. doi:10.1016/j.coviro.2011.09.003
    • (2011) Curr Opin Virol , vol.1 , pp. 355-362
    • Goodfellow, I.1
  • 113
    • 79952303123 scopus 로고    scopus 로고
    • Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3' to 5' exonuclease activity essential for immune suppression
    • doi:10.1073/pnas.1016404108
    • Hastie KM, Kimberlin CR, Zandonatti MA, Macrae IJ, Saphire EO. Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3' to 5' exonuclease activity essential for immune suppression. Proc Natl Acad Sci U S A (2011) 108:2396-401. doi:10.1073/pnas.1016404108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2396-2401
    • Hastie, K.M.1    Kimberlin, C.R.2    Zandonatti, M.A.3    Macrae, I.J.4    Saphire, E.O.5
  • 114
    • 84878760993 scopus 로고    scopus 로고
    • Structures of arenaviral nucleoproteins with triphosphate dsRNA reveal a unique mechanism of immune suppression
    • doi:10.1074/jbc.M112.420521
    • Jiang X, Huang Q, Wang W, Dong H, Ly H, Liang Y, et al. Structures of arenaviral nucleoproteins with triphosphate dsRNA reveal a unique mechanism of immune suppression. J Biol Chem (2013) 288:16949-59. doi:10.1074/jbc.M112.420521
    • (2013) J Biol Chem , vol.288 , pp. 16949-16959
    • Jiang, X.1    Huang, Q.2    Wang, W.3    Dong, H.4    Ly, H.5    Liang, Y.6
  • 115
    • 78951490665 scopus 로고    scopus 로고
    • The C proteins of human parainfluenza virus type 1 limit double-stranded RNA accumulation that would otherwise trigger activation of MDA5 and protein kinase R
    • doi:10.1128/JVI.01297-10
    • Boonyaratanakornkit J, Bartlett E, Schomacker H, Surman S, Akira S, Bae YS, et al. The C proteins of human parainfluenza virus type 1 limit double-stranded RNA accumulation that would otherwise trigger activation of MDA5 and protein kinase R. J Virol (2011) 85:1495-506. doi:10.1128/JVI.01297-10
    • (2011) J Virol , vol.85 , pp. 1495-1506
    • Boonyaratanakornkit, J.1    Bartlett, E.2    Schomacker, H.3    Surman, S.4    Akira, S.5    Bae, Y.S.6


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