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Volumn 14, Issue 6, 2016, Pages 360-373

Viral evasion of intracellular DNA and RNA sensing

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CYCLIC AMP; CYCLIC GMP; GAMMA INTERFERON; GAMMA INTERFERON INDUCIBLE PROTEIN 16; NUCLEIC ACID; PATTERN RECOGNITION RECEPTOR; PROTEIN; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS RNA; IFI16 PROTEIN, HUMAN; INFLAMMASOME; INTERFERON INDUCING AGENT; NUCLEAR PROTEIN; PHOSPHOPROTEIN; RETINOIC ACID INDUCIBLE PROTEIN I;

EID: 84967215091     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro.2016.45     Document Type: Review
Times cited : (350)

References (164)
  • 1
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi, O. & Akira, S. Pattern recognition receptors and inflammation. Cell 140, 805-820 (2010).
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 2
    • 84920896754 scopus 로고    scopus 로고
    • C-type lectins in immunity: Recent developments
    • Dambuza, I. M. & Brown, G. D. C-type lectins in immunity: recent developments. Curr. Opin. Immunol. 32, 21-27 (2015).
    • (2015) Curr. Opin. Immunol. , vol.32 , pp. 21-27
    • Dambuza, I.M.1    Brown, G.D.2
  • 4
    • 84896987305 scopus 로고    scopus 로고
    • Interferon-stimulated genes: A complex web of host defenses
    • Schneider, W. M., Chevillotte, M. D. & Rice, C. M. Interferon-stimulated genes: a complex web of host defenses. Annu. Rev. Immunol. 32, 513-545 (2014).
    • (2014) Annu. Rev. Immunol. , vol.32 , pp. 513-545
    • Schneider, W.M.1    Chevillotte, M.D.2    Rice, C.M.3
  • 5
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • Yoneyama, M. et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat. Immunol. 5, 730-737 (2004).
    • (2004) Nat. Immunol. , vol.5 , pp. 730-737
    • Yoneyama, M.1
  • 6
    • 10344259136 scopus 로고    scopus 로고
    • The v proteins of paramyxoviruses bind the IFN-inducible RNA helicase, MDA5, and inhibit its activation of the IFN-β promoter
    • Andrejeva, J. et al. The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, MDA5, and inhibit its activation of the IFN-β promoter. Proc. Natl Acad. Sci. USA 101, 17264-17269 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 17264-17269
    • Andrejeva, J.1
  • 7
    • 84949725975 scopus 로고    scopus 로고
    • LGP2 synergy with MDA5 in RLR-mediated RNA recognition and antiviral signaling
    • Bruns, A. M. & Horvath, C. M. LGP2 synergy with MDA5 in RLR-mediated RNA recognition and antiviral signaling. Cytokine 74, 198-206 (2015).
    • (2015) Cytokine , vol.74 , pp. 198-206
    • Bruns, A.M.1    Horvath, C.M.2
  • 8
    • 33646342149 scopus 로고    scopus 로고
    • Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
    • Kato, H. et al. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature 441, 101-105 (2006).
    • (2006) Nature , vol.441 , pp. 101-105
    • Kato, H.1
  • 9
    • 37349052379 scopus 로고    scopus 로고
    • Distinct RIG-I and MDA5 signaling by RNA viruses in innate immunity
    • Loo, Y. M. et al. Distinct RIG-I and MDA5 signaling by RNA viruses in innate immunity. J. Virol. 82, 335-345 (2008).
    • (2008) J. Virol. , vol.82 , pp. 335-345
    • Loo, Y.M.1
  • 10
    • 84884157315 scopus 로고    scopus 로고
    • Master sensors of pathogenic RNA-RIG-I like receptors
    • Schlee, M. Master sensors of pathogenic RNA-RIG-I like receptors. Immunobiology 218, 1322-1335 (2013).
    • (2013) Immunobiology , vol.218 , pp. 1322-1335
    • Schlee, M.1
  • 11
    • 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
    • Rasmussen, S. B. 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, 74-78 (2009).
    • (2009) J. Gen. Virol. , vol.90 , pp. 74-78
    • Rasmussen, S.B.1
  • 12
    • 84899106416 scopus 로고    scopus 로고
    • An important role for mitochondrial antiviral signaling protein in the Kaposi's sarcoma-associated herpesvirus life cycle
    • West, J. A. et al. An important role for mitochondrial antiviral signaling protein in the Kaposi's sarcoma-associated herpesvirus life cycle. J. Virol. 88, 5778-5787 (2014).
    • (2014) J. Virol. , vol.88 , pp. 5778-5787
    • West, J.A.1
  • 13
    • 84908330408 scopus 로고    scopus 로고
    • Regulation of RIG-I-like receptor signaling by host and viral proteins
    • Chiang, J. J., Davis, M. E. & Gack, M. U. Regulation of RIG-I-like receptor signaling by host and viral proteins. Cytokine Growth Factor Rev. 25, 491-505 (2014).
    • (2014) Cytokine Growth Factor Rev. , vol.25 , pp. 491-505
    • Chiang, J.J.1    Davis, M.E.2    Gack, M.U.3
  • 14
    • 77949422543 scopus 로고    scopus 로고
    • Phosphorylation-mediated negative regulation of RIG-I antiviral activity
    • Gack, M. U., Nistal-Villan, E., Inn, K. S., Garcia-Sastre, A. & Jung, J. U. Phosphorylation-mediated negative regulation of RIG-I antiviral activity. J. Virol. 84, 3220-3229 (2010).
    • (2010) J. Virol. , vol.84 , pp. 3220-3229
    • Gack, M.U.1    Nistal-Villan, E.2    Inn, K.S.3    Garcia-Sastre, A.4    Jung, J.U.5
  • 15
    • 84857073450 scopus 로고    scopus 로고
    • Conventional protein kinase C- A(PKC-a) and PKC-p negatively regulate RIG-I antiviral signal transduction
    • Maharaj, N. P., Wies, E., Stoll, A. & Gack, M. U. Conventional protein kinase C-a(PKC-a) and PKC-p negatively regulate RIG-I antiviral signal transduction. J. Virol. 86, 1358-1371 (2012).
    • (2012) J. Virol. , vol.86 , pp. 1358-1371
    • Maharaj, N.P.1    Wies, E.2    Stoll, A.3    Gack, M.U.4
  • 16
    • 84875542059 scopus 로고    scopus 로고
    • Dephosphorylation of the RNA sensors RIG-I and MDA5 by the phosphatase PP1 is essential for innate immune signaling
    • Wies, E. et al. Dephosphorylation of the RNA sensors RIG-I and MDA5 by the phosphatase PP1 is essential for innate immune signaling. Immunity 38, 437-449 (2013).
    • (2013) Immunity , vol.38 , pp. 437-449
    • Wies, E.1
  • 17
    • 78650665171 scopus 로고    scopus 로고
    • Phosphorylation of RIG-I by casein kinase II inhibits its antiviral response
    • Sun, Z., Ren, H., Liu, Y, Teeling, J. L. & Gu, J. Phosphorylation of RIG-I by casein kinase II inhibits its antiviral response. J. Virol. 85, 1036-1047 (2011).
    • (2011) J. Virol. , vol.85 , pp. 1036-1047
    • Sun, Z.1    Ren, H.2    Liu, Y.3    Teeling, J.L.4    Gu, J.5
  • 18
    • 84929273566 scopus 로고    scopus 로고
    • RIOK3-mediated phosphorylation of MDA5 interferes with its assembly and attenuates the innate immune response
    • Takashima, K., Oshiumi, H., Takaki, H., Matsumoto, M. & Seya, T. RIOK3-mediated phosphorylation of MDA5 interferes with its assembly and attenuates the innate immune response. Cell Rep. 11, 192-200 (2015).
    • (2015) Cell Rep. , vol.11 , pp. 192-200
    • Takashima, K.1    Oshiumi, H.2    Takaki, H.3    Matsumoto, M.4    Seya, T.5
  • 19
    • 84869845792 scopus 로고    scopus 로고
    • A structure-based model of RIG-I activation
    • Kolakofsky, D., Kowalinski, E. & Cusack, S. A structure-based model of RIG-I activation. RNA 18, 2118-2127 (2012).
    • (2012) RNA , vol.18 , pp. 2118-2127
    • Kolakofsky, D.1    Kowalinski, E.2    Cusack, S.3
  • 20
    • 80054703126 scopus 로고    scopus 로고
    • Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA
    • Kowalinski, E. et al. Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. Cell 147, 423-435 (2011).
    • (2011) Cell , vol.147 , pp. 423-435
    • Kowalinski, E.1
  • 21
    • 79955075657 scopus 로고    scopus 로고
    • The double-stranded RNA-binding protein PACT functions as a cellular activator of RIG-I to facilitate innate antiviral response
    • Kok, K. H. et al. The double-stranded RNA-binding protein PACT functions as a cellular activator of RIG-I to facilitate innate antiviral response. Cell Host Microbe 9, 299-309 (2011).
    • (2011) Cell Host Microbe , vol.9 , pp. 299-309
    • Kok, K.H.1
  • 22
    • 34247341367 scopus 로고    scopus 로고
    • TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
    • Gack, M. U. et al. TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity. Nature 446, 916-920 (2007).
    • (2007) Nature , vol.446 , pp. 916-920
    • Gack, M.U.1
  • 23
    • 84883324602 scopus 로고    scopus 로고
    • A distinct role of Riplet-mediated K63-linked polyubiquitination of the RIG-I repressor domain in human antiviral innate immune responses
    • Oshiumi, H., Miyashita, M., Matsumoto, M. & Seya, T. A distinct role of Riplet-mediated K63-linked polyubiquitination of the RIG-I repressor domain in human antiviral innate immune responses. PLoS Pathog. 9, e1003533 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. e1003533
    • Oshiumi, H.1    Miyashita, M.2    Matsumoto, M.3    Seya, T.4
  • 24
    • 80052281413 scopus 로고    scopus 로고
    • Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus
    • Horner, S. M., Liu, H. M., Park, H. S., Briley, J. & Gale, M. Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus. Proc. Natl Acad. Sci. USA 108, 14590-14595 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 14590-14595
    • Horner, S.M.1    Liu, H.M.2    Park, H.S.3    Briley, J.4    Gale, M.5
  • 25
    • 77951708374 scopus 로고    scopus 로고
    • Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity
    • Zeng, W et al. Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 141, 315-330 (2010).
    • (2010) Cell , vol.141 , pp. 315-330
    • Zeng, W.1
  • 26
    • 84861181618 scopus 로고    scopus 로고
    • The mitochondrial targeting chaperone 14-3-3e regulates a RIG-I translocon that mediates membrane association and innate antiviral immunity
    • Liu, H. M. et al. The mitochondrial targeting chaperone 14-3-3e regulates a RIG-I translocon that mediates membrane association and innate antiviral immunity. Cell Host Microbe 11, 528-537 (2012).
    • (2012) Cell Host Microbe , vol.11 , pp. 528-537
    • Liu, H.M.1
  • 27
    • 84872604349 scopus 로고    scopus 로고
    • Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5
    • Wu, B. et al. Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5. Cell 152, 276-289 (2013).
    • (2013) Cell , vol.152 , pp. 276-289
    • Wu, B.1
  • 28
    • 77952503750 scopus 로고    scopus 로고
    • Peroxisomes are signaling platforms for antiviral innate immunity
    • Dixit, E. et al. Peroxisomes are signaling platforms for antiviral innate immunity. Cell 141, 668-681 (2010).
    • (2010) Cell , vol.141 , pp. 668-681
    • Dixit, E.1
  • 29
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • Hou, F et al. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 146, 448-461 (2011).
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1
  • 30
    • 84921280194 scopus 로고    scopus 로고
    • The RNA sensor RIG-I dually functions as an innate sensor and direct antiviral factor for hepatitis B virus
    • Sato, S. et al. The RNA sensor RIG-I dually functions as an innate sensor and direct antiviral factor for hepatitis B virus. Immunity 42, 123-132 (2015).
    • (2015) Immunity , vol.42 , pp. 123-132
    • Sato, S.1
  • 31
    • 84926139701 scopus 로고    scopus 로고
    • Influenza virus adaptation PB2-627K modulates nucleocapsid inhibition by the pathogen sensor RIG-I
    • Weber, M. et al. Influenza virus adaptation PB2-627K modulates nucleocapsid inhibition by the pathogen sensor RIG-I. Cell Host Microbe 17, 309-319 (2015).
    • (2015) Cell Host Microbe , vol.17 , pp. 309-319
    • Weber, M.1
  • 32
    • 84928928403 scopus 로고    scopus 로고
    • ATP-dependent effector-like functions of RIG-I-like receptors
    • Yao, H. et al. ATP-dependent effector-like functions of RIG-I-like receptors. Mol. Cell 58, 541-548 (2015).
    • (2015) Mol. Cell , vol.58 , pp. 541-548
    • Yao, H.1
  • 33
    • 84937763934 scopus 로고    scopus 로고
    • Innate immune recognition of DNA: A recent history
    • Dempsey, A. & Bowie, A. G. Innate immune recognition of DNA: a recent history. Virology 479-480, 146-152 (2015).
    • (2015) Virology , vol.479-480 , pp. 146-152
    • Dempsey, A.1    Bowie, A.G.2
  • 34
    • 53349168904 scopus 로고    scopus 로고
    • The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation
    • Zhong, B. et al. The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity 29, 538-550 (2008).
    • (2008) Immunity , vol.29 , pp. 538-550
    • Zhong, B.1
  • 35
    • 70349943834 scopus 로고    scopus 로고
    • STING regulates intracellular DNA-mediated, type i interferon-dependent innate immunity
    • Ishikawa, H., Ma, Z. & Barber, G. N. STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity. Nature 461, 788-792 (2009).
    • (2009) Nature , vol.461 , pp. 788-792
    • Ishikawa, H.1    Ma, Z.2    Barber, G.N.3
  • 36
    • 66649109939 scopus 로고    scopus 로고
    • ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization
    • Sun, W. et al. ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization. Proc. Natl Acad. Sci. USA 106, 8653-8658 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 8653-8658
    • Sun, W.1
  • 37
    • 84873711885 scopus 로고    scopus 로고
    • Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type i interferon pathway
    • Sun, L., Wu, J., Du, F., Chen, X. & Chen, Z. J. Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway. Science 339, 786-791 (2013).
    • (2013) Science , vol.339 , pp. 786-791
    • Sun, L.1    Wu, J.2    Du, F.3    Chen, X.4    Chen, Z.J.5
  • 38
    • 84882896267 scopus 로고    scopus 로고
    • Cyclic GMP-AMP synthase is an innate immune sensor of HIV and other retroviruses
    • Gao, D. et al. Cyclic GMP-AMP synthase is an innate immune sensor of HIV and other retroviruses. Science 341, 903-906 (2013).
    • (2013) Science , vol.341 , pp. 903-906
    • Gao, D.1
  • 39
    • 84884675857 scopus 로고    scopus 로고
    • Pivotal roles of cGAS-cGAMP signaling in antiviral defense and immune adjuvant effects
    • Li, X. D. et al. Pivotal roles of cGAS-cGAMP signaling in antiviral defense and immune adjuvant effects. Science 341, 1390-1394 (2013).
    • (2013) Science , vol.341 , pp. 1390-1394
    • Li, X.D.1
  • 40
    • 84895904323 scopus 로고    scopus 로고
    • Pan-viral specificity of IFN-induced genes reveals new roles for cGAS in innate immunity
    • Schoggins, J. W. et al. Pan-viral specificity of IFN-induced genes reveals new roles for cGAS in innate immunity. Nature 505, 691-695 (2014).
    • (2014) Nature , vol.505 , pp. 691-695
    • Schoggins, J.W.1
  • 41
    • 84873724533 scopus 로고    scopus 로고
    • Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA
    • Wu, J. et al. Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA. Science 339, 826-830 (2013).
    • (2013) Science , vol.339 , pp. 826-830
    • Wu, J.1
  • 42
    • 84878309796 scopus 로고    scopus 로고
    • Cyclic [G(2′, 5′)pA(3′, 5′)p] is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase
    • Gao, P. et al. Cyclic [G(2′, 5′)pA(3′, 5′)p] is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase. Cell 153, 1094-1107 (2013).
    • (2013) Cell , vol.153 , pp. 1094-1107
    • Gao, P.1
  • 43
    • 84879385334 scopus 로고    scopus 로고
    • CGAS produces a 2′-5′-linked cyclic dinucleotide second messenger that activates STING
    • Ablasser, A. et al. cGAS produces a 2′-5′-linked cyclic dinucleotide second messenger that activates STING. Nature 498, 380-384 (2013).
    • (2013) Nature , vol.498 , pp. 380-384
    • Ablasser, A.1
  • 44
    • 84888637695 scopus 로고    scopus 로고
    • Cell intrinsic immunity spreads to bystander cells via the intercellular transfer of cGAMP
    • Ablasser, A. et al. Cell intrinsic immunity spreads to bystander cells via the intercellular transfer of cGAMP. Nature 503, 530-534 (2013).
    • (2013) Nature , vol.503 , pp. 530-534
    • Ablasser, A.1
  • 45
    • 78650214109 scopus 로고    scopus 로고
    • The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA
    • Tsuchida, T. et al. The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA. Immunity 33, 765-776 (2010).
    • (2010) Immunity , vol.33 , pp. 765-776
    • Tsuchida, T.1
  • 46
    • 84865270570 scopus 로고    scopus 로고
    • TRIM32 protein modulates type i interferon induction and cellular antiviral response by targeting MITA/STING protein for K63-linked ubiquitination
    • Zhang, J., Hu, M. M., Wang, Y. Y. & Shu, H. B. TRIM32 protein modulates type I interferon induction and cellular antiviral response by targeting MITA/STING protein for K63-linked ubiquitination. J. Biol. Chem. 287, 28646-28655 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 28646-28655
    • Zhang, J.1    Hu, M.M.2    Wang, Y.Y.3    Shu, H.B.4
  • 47
    • 84924778328 scopus 로고    scopus 로고
    • Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation
    • Liu, S. et al. Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation. Science 347, aaa2630 (2015).
    • (2015) Science , vol.347 , pp. aaa2630
    • Liu, S.1
  • 48
    • 84857937262 scopus 로고    scopus 로고
    • STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway
    • Tanaka, Y. & Chen, Z. J. STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway. Sci. Signal. 5, ra20 (2012).
    • (2012) Sci. Signal. , vol.5 , pp. ra20
    • Tanaka, Y.1    Chen, Z.J.2
  • 49
    • 77958140656 scopus 로고    scopus 로고
    • IFI16 is an innate immune sensor for intracellular DNA
    • Unterholzner, L. et al. IFI16 is an innate immune sensor for intracellular DNA. Nat. Immunol. 11, 997-1004 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 997-1004
    • Unterholzner, L.1
  • 50
    • 84859986329 scopus 로고    scopus 로고
    • Structures of the HIN domain: DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor
    • Jin, T. et al. Structures of the HIN domain: DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor. Immunity 36, 561-571 (2012).
    • (2012) Immunity , vol.36 , pp. 561-571
    • Jin, T.1
  • 51
    • 56749133272 scopus 로고    scopus 로고
    • Viral evasion and subversion of pattern-recognition receptor signalling
    • Bowie, A. G. & Unterholzner, L. Viral evasion and subversion of pattern-recognition receptor signalling. Nat. Rev. Immunol. 8, 911-922 (2008).
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 911-922
    • Bowie, A.G.1    Unterholzner, L.2
  • 52
    • 84873304007 scopus 로고    scopus 로고
    • Recent advances in understanding viral evasion of type i interferon
    • Taylor, K. E. & Mossman, K. L. Recent advances in understanding viral evasion of type I interferon. Immunology 138, 190-197 (2013).
    • (2013) Immunology , vol.138 , pp. 190-197
    • Taylor, K.E.1    Mossman, K.L.2
  • 53
    • 84925719276 scopus 로고    scopus 로고
    • The dengue virus conceals double-stranded RNA in the intracellular membrane to escape from an interferon response
    • Uchida, L. et al. The dengue virus conceals double-stranded RNA in the intracellular membrane to escape from an interferon response. Sci. Rep. 4, 7395 (2014).
    • (2014) Sci. Rep. , vol.4 , pp. 7395
    • Uchida, L.1
  • 54
    • 33646748294 scopus 로고    scopus 로고
    • Ebola virus VP35 protein binds double-stranded RNA and inhibits a/p-interferon production induced by RIG-I signaling
    • Cardenas, W. B. et al. Ebola virus VP35 protein binds double-stranded RNA and inhibits a/p-interferon production induced by RIG-I signaling. J. Virol. 80, 5168-5178 (2006).
    • (2006) J. Virol. , vol.80 , pp. 5168-5178
    • Cardenas, W.B.1
  • 55
    • 84874423425 scopus 로고    scopus 로고
    • Structural basis for Marburg virus VP35-mediated immune evasion mechanisms
    • Ramanan, P. et al. Structural basis for Marburg virus VP35-mediated immune evasion mechanisms. Proc. Natl Acad. Sci. USA 109, 20661-20666 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 20661-20666
    • Ramanan, P.1
  • 56
    • 0027102716 scopus 로고
    • Binding of influenza A virus NS1 protein to dsRNA in vitro
    • Hatada, E. & Fukuda, R. Binding of influenza A virus NS1 protein to dsRNA in vitro. J. Gen. Virol. 73, 3325-3329 (1992).
    • (1992) J. Gen. Virol. , vol.73 , pp. 3325-3329
    • Hatada, E.1    Fukuda, R.2
  • 57
    • 0029400032 scopus 로고
    • An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure
    • Qian, X. Y, Chien, C. Y, Lu, Y, Montelione, G. T & Krug, R. M. An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure. RNA 1, 948-956 (1995).
    • (1995) RNA , vol.1 , pp. 948-956
    • Qian, X.Y.1    Chien, C.Y.2    Lu, Y.3    Montelione, G.T.4    Krug, R.M.5
  • 58
    • 0345167006 scopus 로고    scopus 로고
    • A recombinant influenza A virus expressing an RNA-binding-defective NS1 protein induces high levels of (interferon and is attenuated in mice
    • Donelan, N. R., Basler, C. F. & Garcia-Sastre, A. A recombinant influenza A virus expressing an RNA-binding-defective NS1 protein induces high levels of (interferon and is attenuated in mice. J. Virol. 77, 13257-13266 (2003).
    • (2003) J. Virol. , vol.77 , pp. 13257-13266
    • Donelan, N.R.1    Basler, C.F.2    Garcia-Sastre, A.3
  • 59
    • 77956275377 scopus 로고    scopus 로고
    • Inhibition of the RNA polymerase III-mediated dsDNA-sensing pathway of innate immunity by vaccinia virus protein E3
    • Valentine, R. & Smith, G. L. Inhibition of the RNA polymerase III-mediated dsDNA-sensing pathway of innate immunity by vaccinia virus protein E3. J. Gen. Virol. 91, 2221-2229 (2010).
    • (2010) J. Gen. Virol. , vol.91 , pp. 2221-2229
    • Valentine, R.1    Smith, G.L.2
  • 60
    • 49149128081 scopus 로고    scopus 로고
    • Cellular la protein shields nonsegmented negative-strand RNA viral leader RNA from RIG-I and enhances virus growth by diverse mechanisms
    • Bitko, V, Musiyenko, A., Bayfield, M. A., Maraia, R. J. & Barik, S. Cellular La protein shields nonsegmented negative-strand RNA viral leader RNA from RIG-I and enhances virus growth by diverse mechanisms. J. Virol. 82, 7977-7987 (2008).
    • (2008) J. Virol. , vol.82 , pp. 7977-7987
    • Bitko, V.1    Musiyenko, A.2    Bayfield, M.A.3    Maraia, R.J.4    Barik, S.5
  • 61
    • 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
    • Boonyaratanakornkit, J. 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. 85, 1495-1506 (2011).
    • (2011) J. Virol. , vol.85 , pp. 1495-1506
    • Boonyaratanakornkit, J.1
  • 62
    • 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
    • Habjan, M. et al. Processing of genome 5'termini as a strategy of negative-strand RNA viruses to avoid RIG-I-dependent interferon induction. PLoS ONE 3, e2032 (2008).
    • (2008) PLoS ONE , vol.3 , pp. e2032
    • Habjan, M.1
  • 63
    • 79955605785 scopus 로고    scopus 로고
    • Old World hantaviruses do not produce detectable amounts of dsRNA in infected cells and the 5' termini of their genomic RNAs are monophosphorylated
    • Wang, H., Vaheri, A., Weber, F & Plyusnin, A. Old World hantaviruses do not produce detectable amounts of dsRNA in infected cells and the 5' termini of their genomic RNAs are monophosphorylated. J. Gen. Virol. 92, 1199-1204 (2011).
    • (2011) J. Gen. Virol. , vol.92 , pp. 1199-1204
    • Wang, H.1    Vaheri, A.2    Weber, F.3    Plyusnin, A.4
  • 64
    • 77953308262 scopus 로고    scopus 로고
    • Unpaired 5'-ppp-nucleotides, as found in arenavirus double-stranded RNA panhandles, are not recognized by RIG-I
    • Marq, J. B., Kolakofsky, D. & Garcin, D. Unpaired 5'-ppp-nucleotides, as found in arenavirus double-stranded RNA panhandles, are not recognized by RIG-I. J. Biol. Chem. 285, 18208-18216 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 18208-18216
    • Marq, J.B.1    Kolakofsky, D.2    Garcin, D.3
  • 65
    • 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
    • Marq, J. B., 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. 286, 6108-6116 (2011).
    • (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
  • 66
    • 79952303123 scopus 로고    scopus 로고
    • Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3'-to-5' exonuclease activity essential for immune suppression
    • Hastie, K. M., Kimberlin, C. R., Zandonatti, M. A., MacRae, I. J. & Saphire, E. O. Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3'-to-5' exonuclease activity essential for immune suppression. Proc. Natl Acad. Sci. USA 108, 2396-2401 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , 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
  • 67
    • 84911386623 scopus 로고    scopus 로고
    • Exonuclease domain of the Lassa virus nucleoprotein is critical to avoid RIG-I signaling and to inhibit the innate immune response
    • Reynard, S., Russier, M., Fizet, A., Carnec, X. & Baize, S. Exonuclease domain of the Lassa virus nucleoprotein is critical to avoid RIG-I signaling and to inhibit the innate immune response. J. Virol. 88, 13923-13927 (2014).
    • (2014) J. Virol. , vol.88 , pp. 13923-13927
    • Reynard, S.1    Russier, M.2    Fizet, A.3    Carnec, X.4    Baize, S.5
  • 68
    • 65549164536 scopus 로고    scopus 로고
    • Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I
    • Gack, M. U. et al. Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I. Cell Host Microbe 5, 439-449 (2009).
    • (2009) Cell Host Microbe , vol.5 , pp. 439-449
    • Gack, M.U.1
  • 69
    • 84870820660 scopus 로고    scopus 로고
    • Species-specific inhibition of RIG-I ubiquitination and IFN induction by the influenza A virus NS1 protein
    • Rajsbaum, R. et al. Species-specific inhibition of RIG-I ubiquitination and IFN induction by the influenza A virus NS1 protein. PLoS Pathog. 8, e1003059 (2012).
    • (2012) PLoS Pathog. , vol.8 , pp. e1003059
    • Rajsbaum, R.1
  • 70
    • 80055007460 scopus 로고    scopus 로고
    • Inhibition of RIG-I-mediated signaling by Kaposi's sarcoma-associated herpesvirus-encoded deubiquitinase ORF64
    • Inn, K. S. et al. Inhibition of RIG-I-mediated signaling by Kaposi's sarcoma-associated herpesvirus-encoded deubiquitinase ORF64. J. Virol. 85, 10899-10904 (2011).
    • (2011) J. Virol. , vol.85 , pp. 10899-10904
    • Inn, K.S.1
  • 71
    • 77950806384 scopus 로고    scopus 로고
    • Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases
    • Clementz, M. A. et al. Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases. J. Virol. 84, 4619-4629 (2010).
    • (2010) J. Virol. , vol.84 , pp. 4619-4629
    • Clementz, M.A.1
  • 72
    • 79952837091 scopus 로고    scopus 로고
    • The leader proteinase of foot-and-mouth disease virus negatively regulates the type i interferon pathway by acting as a viral deubiquitinase
    • Wang, D. et al. The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase. J. Virol. 85, 3758-3766 (2011).
    • (2011) J. Virol. , vol.85 , pp. 3758-3766
    • Wang, D.1
  • 73
    • 84874504652 scopus 로고    scopus 로고
    • Deubiquitinase function of arterivirus papain-like protease 2 suppresses the innate immune response in infected host cells
    • van Kasteren, P. B. et al. Deubiquitinase function of arterivirus papain-like protease 2 suppresses the innate immune response in infected host cells. Proc. Natl Acad. Sci. USA 110, E838-E847 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E838-E847
    • Van Kasteren, P.B.1
  • 74
    • 84906983279 scopus 로고    scopus 로고
    • Downregulation of microRNA miR-526a by enterovirus inhibits RIG-I-dependent innate immune response
    • Xu, C. et al. Downregulation of microRNA miR-526a by enterovirus inhibits RIG-I-dependent innate immune response. J. Virol. 88, 11356-11368 (2014).
    • (2014) J. Virol. , vol.88 , pp. 11356-11368
    • Xu, C.1
  • 75
    • 84943577112 scopus 로고    scopus 로고
    • Dengue subgenomic RNA binds TRIM25 to inhibit interferon expression for epidemiological fitness
    • Manokaran, G. et al. Dengue subgenomic RNA binds TRIM25 to inhibit interferon expression for epidemiological fitness. Science 350, 217-221 (2015).
    • (2015) Science , vol.350 , pp. 217-221
    • Manokaran, G.1
  • 76
    • 84892428607 scopus 로고    scopus 로고
    • The ubiquitin-specific protease USP15 promotes RIG-I-mediated antiviral signaling by deubiquitylating TRIM25
    • Pauli, E. K. et al. The ubiquitin-specific protease USP15 promotes RIG-I-mediated antiviral signaling by deubiquitylating TRIM25. Sci. Signal. 7, ra3 (2014).
    • (2014) Sci. Signal. , vol.7 , pp. ra3
    • Pauli, E.K.1
  • 77
    • 84904213086 scopus 로고    scopus 로고
    • Antagonism of the phosphatase PP1 by the measles virus v protein is required for innate immune escape of MDA5
    • Davis, M. E. et al. Antagonism of the phosphatase PP1 by the measles virus V protein is required for innate immune escape of MDA5. Cell Host Microbe 16, 19-30 (2014).
    • (2014) Cell Host Microbe , vol.16 , pp. 19-30
    • Davis, M.E.1
  • 78
    • 84904182245 scopus 로고    scopus 로고
    • Measles virus suppresses RIG-I-like receptor activation in dendritic cells via DC-SIGN-mediated inhibition of PP1 phosphatases
    • Mesman, A. W. et al. Measles virus suppresses RIG-I-like receptor activation in dendritic cells via DC-SIGN-mediated inhibition of PP1 phosphatases. Cell Host Microbe 16, 31-42 (2014).
    • (2014) Cell Host Microbe , vol.16 , pp. 31-42
    • Mesman, A.W.1
  • 79
  • 80
    • 84894522449 scopus 로고    scopus 로고
    • pro targets MDA5 and MAVS in infected cells
    • pro targets MDA5 and MAVS in infected cells. J. Virol. 88, 3369-3378 (2014).
    • (2014) J. Virol. , vol.88 , pp. 3369-3378
    • Feng, Q.1
  • 81
    • 79953279338 scopus 로고    scopus 로고
    • The coxsackievirus B 3C protease cleaves MAVS and TRIF to attenuate host type i interferon and apoptotic signaling
    • Mukherjee, A. et al. The coxsackievirus B 3C protease cleaves MAVS and TRIF to attenuate host type I interferon and apoptotic signaling. PLoS Pathog. 7, e1001311 (2011).
    • (2011) PLoS Pathog. , vol.7 , pp. e1001311
    • Mukherjee, A.1
  • 82
    • 29144462494 scopus 로고    scopus 로고
    • Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity
    • Li, X. D., Sun, L., Seth, R. B., Pineda, G. & Chen, Z. J. Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity. Proc. Natl Acad. Sci. USA 102, 17717-17722 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 17717-17722
    • Li, X.D.1    Sun, L.2    Seth, R.B.3    Pineda, G.4    Chen, Z.J.5
  • 83
    • 34249855382 scopus 로고    scopus 로고
    • Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor
    • Yang, Y. et al. Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor. Proc. Natl Acad. Sci. USA 104, 7253-7258 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 7253-7258
    • Yang, Y.1
  • 84
    • 33846106820 scopus 로고    scopus 로고
    • GB virus B disrupts RIG-I signaling by NS3/4A-mediated cleavage of the adaptor protein MAVS
    • Chen, Z. et al. GB virus B disrupts RIG-I signaling by NS3/4A-mediated cleavage of the adaptor protein MAVS. J. Virol. 81, 964-976 (2007).
    • (2007) J. Virol. , vol.81 , pp. 964-976
    • Chen, Z.1
  • 85
    • 70350625078 scopus 로고    scopus 로고
    • Cleavage of IPS-1 in cells infected with human rhinovirus
    • Drahos, J. & Racaniello, V. R. Cleavage of IPS-1 in cells infected with human rhinovirus. J. Virol. 83, 11581-11587 (2009).
    • (2009) J. Virol. , vol.83 , pp. 11581-11587
    • Drahos, J.1    Racaniello, V.R.2
  • 86
    • 84907319179 scopus 로고    scopus 로고
    • Influenza A virus protein PB1-F2 translocates into mitochondria via Tom40 channels and impairs innate immunity
    • Yoshizumi, T. et al. Influenza A virus protein PB1-F2 translocates into mitochondria via Tom40 channels and impairs innate immunity. Nat. Commun. 5, 4713 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 4713
    • Yoshizumi, T.1
  • 87
    • 84865095316 scopus 로고    scopus 로고
    • Influenza virus protein PB1-F2 inhibits the induction of type i interferon by binding to MAVS and decreasing mitochondrial membrane potential
    • Varga, Z. T., Grant, A., Manicassamy, B. & Palese, P. Influenza virus protein PB1-F2 inhibits the induction of type I interferon by binding to MAVS and decreasing mitochondrial membrane potential. J. Virol. 86, 8359-8366 (2012).
    • (2012) J. Virol. , vol.86 , pp. 8359-8366
    • Varga, Z.T.1    Grant, A.2    Manicassamy, B.3    Palese, P.4
  • 88
    • 77955496554 scopus 로고    scopus 로고
    • The hepatitis B virus X protein disrupts innate immunity by downregulating mitochondrial antiviral signaling protein
    • Wei, C. et al. The hepatitis B virus X protein disrupts innate immunity by downregulating mitochondrial antiviral signaling protein. J. Immunol. 185, 1158-1168 (2010).
    • (2010) J. Immunol. , vol.185 , pp. 1158-1168
    • Wei, C.1
  • 89
    • 34247127075 scopus 로고    scopus 로고
    • MDA-5 is cleaved in poliovirus-infected cells
    • Barral, P. M. et al. MDA-5 is cleaved in poliovirus-infected cells. J. Virol. 81, 3677-3684 (2007).
    • (2007) J. Virol. , vol.81 , pp. 3677-3684
    • Barral, P.M.1
  • 90
    • 84897487697 scopus 로고    scopus 로고
    • Mitophagy enhances oncolytic measles virus replication by mitigating DDX58/RIG-I-like receptor signaling
    • Xia, M. et al. Mitophagy enhances oncolytic measles virus replication by mitigating DDX58/RIG-I-like receptor signaling. J. Virol. 88, 5152-5164 (2014).
    • (2014) J. Virol. , vol.88 , pp. 5152-5164
    • Xia, M.1
  • 91
    • 84921664520 scopus 로고    scopus 로고
    • SARS-coronavirus open reading frame-9b suppresses innate immunity by targeting mitochondria and the MAVS/TRAF3/TRAF6 signalosome
    • Shi, C. S. et al. SARS-coronavirus open reading frame-9b suppresses innate immunity by targeting mitochondria and the MAVS/TRAF3/TRAF6 signalosome. J. Immunol. 193, 3080-3089 (2014).
    • (2014) J. Immunol. , vol.193 , pp. 3080-3089
    • Shi, C.S.1
  • 92
    • 84881188408 scopus 로고    scopus 로고
    • Viral degradasome hijacks mitochondria to suppress innate immunity
    • Goswami, R. et al. Viral degradasome hijacks mitochondria to suppress innate immunity. Cell Res. 23, 1025-1042 (2013).
    • (2013) Cell Res. , vol.23 , pp. 1025-1042
    • Goswami, R.1
  • 93
    • 84949844295 scopus 로고    scopus 로고
    • Flavivirus infection impairs peroxisome biogenesis and early antiviral signaling
    • You, J. et al. Flavivirus infection impairs peroxisome biogenesis and early antiviral signaling. J. Virol. 89, 12349-12361 (2015).
    • (2015) J. Virol. , vol.89 , pp. 12349-12361
    • You, J.1
  • 94
    • 84874675342 scopus 로고    scopus 로고
    • Amino acid requirements for MDA5 and LGP2 recognition by paramyxovirus v proteins: A single arginine distinguishes MDA5 from RIG-I
    • Rodriguez, K. R. & Horvath, C. M. Amino acid requirements for MDA5 and LGP2 recognition by paramyxovirus V proteins: a single arginine distinguishes MDA5 from RIG-I. J. Virol. 87, 2974-2978 (2013).
    • (2013) J. Virol. , vol.87 , pp. 2974-2978
    • Rodriguez, K.R.1    Horvath, C.M.2
  • 95
    • 84873523444 scopus 로고    scopus 로고
    • Paramyxovirus v proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling
    • Motz, C. et al. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science 339, 690-693 (2013).
    • (2013) Science , vol.339 , pp. 690-693
    • Motz, C.1
  • 96
    • 59749095300 scopus 로고    scopus 로고
    • Mechanism of MDA5 inhibition by paramyxovirus v proteins
    • Childs, K. S., Andrejeva, J., Randall, R. E. & Goodbourn, S. Mechanism of MDA5 inhibition by paramyxovirus V proteins. J. Virol. 83, 1465-1473 (2009).
    • (2009) J. Virol. , vol.83 , pp. 1465-1473
    • Childs, K.S.1    Andrejeva, J.2    Randall, R.E.3    Goodbourn, S.4
  • 97
    • 84880445500 scopus 로고    scopus 로고
    • Mutual antagonism between the Ebola virus VP35 protein and the RIG-I activator PACT determines infection outcome
    • Luthra, P. et al. Mutual antagonism between the Ebola virus VP35 protein and the RIG-I activator PACT determines infection outcome. Cell Host Microbe 14, 74-84 (2013).
    • (2013) Cell Host Microbe , vol.14 , pp. 74-84
    • Luthra, P.1
  • 98
    • 84904876332 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of the influenza A virus nonstructural proteins NS1 and NS2 during natural cell infection identifies PACT as an NS1 target protein and antiviral host factor
    • Tawaratsumida, K. et al. Quantitative proteomic analysis of the influenza A virus nonstructural proteins NS1 and NS2 during natural cell infection identifies PACT as an NS1 target protein and antiviral host factor. J. Virol. 88, 9038-9048 (2014).
    • (2014) J. Virol. , vol.88 , pp. 9038-9048
    • Tawaratsumida, K.1
  • 99
    • 84895534920 scopus 로고    scopus 로고
    • Middle east respiratory syndrome coronavirus 4a protein is a double-stranded RNA-binding protein that suppresses PACT-induced activation of RIG-I and MDA5 in the innate antiviral response
    • Siu, K. L. et al. Middle east respiratory syndrome coronavirus 4a protein is a double-stranded RNA-binding protein that suppresses PACT-induced activation of RIG-I and MDA5 in the innate antiviral response. J. Virol. 88, 4866-4876 (2014).
    • (2014) J. Virol. , vol.88 , pp. 4866-4876
    • Siu, K.L.1
  • 100
    • 67650230347 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus M protein inhibits type i interferon production by impeding the formation of TRAF3-TANK-TBK1/IKKϵ complex
    • Siu, K. L. et al. Severe acute respiratory syndrome coronavirus M protein inhibits type I interferon production by impeding the formation of TRAF3-TANK-TBK1/IKKϵ complex. J. Biol. Chem. 284, 16202-16209 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 16202-16209
    • Siu, K.L.1
  • 101
    • 75449114628 scopus 로고    scopus 로고
    • Z proteins of New World arenaviruses bind RIG-I and interfere with type i interferon induction
    • Fan, L., Briese, T. & Lipkin, W. I. Z proteins of New World arenaviruses bind RIG-I and interfere with type I interferon induction. J. Virol. 84, 1785-1791 (2010).
    • (2010) J. Virol. , vol.84 , pp. 1785-1791
    • Fan, L.1    Briese, T.2    Lipkin, W.I.3
  • 102
    • 84923008601 scopus 로고    scopus 로고
    • The Z proteins of pathogenic but not nonpathogenic arenaviruses inhibit RIG-I-like receptor-dependent interferon production
    • Xing, J., Ly, H. & Liang, Y. The Z proteins of pathogenic but not nonpathogenic arenaviruses inhibit RIG-I-like receptor-dependent interferon production. J. Virol. 89, 2944-2955 (2015).
    • (2015) J. Virol. , vol.89 , pp. 2944-2955
    • Xing, J.1    Ly, H.2    Liang, Y.3
  • 103
    • 44949111358 scopus 로고    scopus 로고
    • Human metapneumovirus glycoprotein G inhibits innate immune responses
    • Bao, X. et al. Human metapneumovirus glycoprotein G inhibits innate immune responses. PLoS Pathog. 4, e1000077 (2008).
    • (2008) PLoS Pathog. , vol.4 , pp. e1000077
    • Bao, X.1
  • 104
    • 84961392938 scopus 로고    scopus 로고
    • A phosphomimetic-based mechanism of dengue virus to antagonize innate immunity
    • Chan, Y. K. & Gack, M. U. A phosphomimetic-based mechanism of dengue virus to antagonize innate immunity. Nat. Immunol. 17, 523-530 (2016).
    • (2016) Nat. Immunol. , vol.17 , pp. 523-530
    • Chan, Y.K.1    Gack, M.U.2
  • 105
    • 84864391552 scopus 로고    scopus 로고
    • Human respiratory syncytial virus nucleoprotein and inclusion bodies antagonize the innate immune response mediated by MDA5 and MAVS
    • Lifland, A. W. et al. Human respiratory syncytial virus nucleoprotein and inclusion bodies antagonize the innate immune response mediated by MDA5 and MAVS. J. Virol. 86, 8245-8258 (2012).
    • (2012) J. Virol. , vol.86 , pp. 8245-8258
    • Lifland, A.W.1
  • 106
    • 84896930327 scopus 로고    scopus 로고
    • Hijacking of RIG-I signaling proteins into virus-induced cytoplasmic structures correlates with the inhibition of type i interferon responses
    • Santiago, F. W. et al. Hijacking of RIG-I signaling proteins into virus-induced cytoplasmic structures correlates with the inhibition of type I interferon responses. J. Virol. 88, 4572-4585 (2014).
    • (2014) J. Virol. , vol.88 , pp. 4572-4585
    • Santiago, F.W.1
  • 107
    • 84883271505 scopus 로고    scopus 로고
    • Encephalomyocarditis virus disrupts stress granules, the critical platform for triggering antiviral innate immune responses
    • Ng, C. S. et al. Encephalomyocarditis virus disrupts stress granules, the critical platform for triggering antiviral innate immune responses. J. Virol. 87, 9511-9522 (2013).
    • (2013) J. Virol. , vol.87 , pp. 9511-9522
    • Ng, C.S.1
  • 108
    • 35848929915 scopus 로고    scopus 로고
    • Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase
    • White, J. P., Cardenas, A. M., Marissen, W. E. & Lloyd, R. E. Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase. Cell Host Microbe 2, 295-305 (2007).
    • (2007) Cell Host Microbe , vol.2 , pp. 295-305
    • White, J.P.1    Cardenas, A.M.2    Marissen, W.E.3    Lloyd, R.E.4
  • 109
    • 77958114725 scopus 로고    scopus 로고
    • The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1
    • Yan, N., Regalado-Magdos, A. D., Stiggelbout, B., Lee-Kirsch, M. A. & Lieberman, J. The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1. Nat. Immunol. 11, 1005-1013 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 1005-1013
    • Yan, N.1    Regalado-Magdos, A.D.2    Stiggelbout, B.3    Lee-Kirsch, M.A.4    Lieberman, J.5
  • 110
    • 84888054227 scopus 로고    scopus 로고
    • HIV-1 evades innate immune recognition through specific cofactor recruitment
    • Rasaiyaah, J. et al. HIV-1 evades innate immune recognition through specific cofactor recruitment. Nature 503, 402-405 (2013).
    • (2013) Nature , vol.503 , pp. 402-405
    • Rasaiyaah, J.1
  • 111
    • 84890215093 scopus 로고    scopus 로고
    • The capsids of HIV-1 and HIV-2 determine immune detection of the viral cDNA by the innate sensor cGAS in dendritic cells
    • Lahaye, X. et al. The capsids of HIV-1 and HIV-2 determine immune detection of the viral cDNA by the innate sensor cGAS in dendritic cells. Immunity 39, 1132-1142 (2013).
    • (2013) Immunity , vol.39 , pp. 1132-1142
    • Lahaye, X.1
  • 112
    • 84921638462 scopus 로고    scopus 로고
    • Hepatitis B virus polymerase disrupts K63-linked ubiquitination of STING to block innate cytosolic DNA-sensing pathways
    • Liu, Y. et al. Hepatitis B virus polymerase disrupts K63-linked ubiquitination of STING to block innate cytosolic DNA-sensing pathways. J. Virol. 89, 2287-2300 (2015).
    • (2015) J. Virol. , vol.89 , pp. 2287-2300
    • Liu, Y.1
  • 113
    • 84899584959 scopus 로고    scopus 로고
    • SARS coronavirus papain-like protease inhibits the type i interferon signaling pathway through interaction with the STING-TRAF3-TBK1 complex
    • Chen, X. et al. SARS coronavirus papain-like protease inhibits the type I interferon signaling pathway through interaction with the STING-TRAF3-TBK1 complex. Protein Cell 5, 369-381 (2014).
    • (2014) Protein Cell , vol.5 , pp. 369-381
    • Chen, X.1
  • 114
    • 84856501373 scopus 로고    scopus 로고
    • Coronavirus papain-like proteases negatively regulate antiviral innate immune response through disruption of STING-mediated signaling
    • Sun, L. et al. Coronavirus papain-like proteases negatively regulate antiviral innate immune response through disruption of STING-mediated signaling. PLoS ONE 7, e30802 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e30802
    • Sun, L.1
  • 115
    • 84879142678 scopus 로고    scopus 로고
    • The papain-like protease of porcine epidemic diarrhea virus negatively regulates type i interferon pathway by acting as a viral deubiquitinase
    • Xing, Y. et al. The papain-like protease of porcine epidemic diarrhea virus negatively regulates type I interferon pathway by acting as a viral deubiquitinase. J. Gen. Virol. 94, 1554-1567 (2013).
    • (2013) J. Gen. Virol. , vol.94 , pp. 1554-1567
    • Xing, Y.1
  • 116
    • 84872163319 scopus 로고    scopus 로고
    • Hepatitis C virus NS4B protein targets STING and abrogates RIG-I-mediated type i interferon-dependent innate immunity
    • Nitta, S. et al. Hepatitis C virus NS4B protein targets STING and abrogates RIG-I-mediated type I interferon-dependent innate immunity. Hepatology 57, 46-58 (2013).
    • (2013) Hepatology , vol.57 , pp. 46-58
    • Nitta, S.1
  • 117
    • 84879173207 scopus 로고    scopus 로고
    • Hepatitis C virus NS4B blocks the interaction of STING and TBK1 to evade host innate immunity
    • Ding, Q. et al. Hepatitis C virus NS4B blocks the interaction of STING and TBK1 to evade host innate immunity. J. Hepatol 59, 52-58 (2013).
    • (2013) J. Hepatol , vol.59 , pp. 52-58
    • Ding, Q.1
  • 118
    • 84945353895 scopus 로고    scopus 로고
    • DNA tumor virus oncogenes antagonize the cGAS-STING DNA sensing pathway
    • Lau, L., Gray, E. E., Brunette, R. L. & Stetson, D. B. DNA tumor virus oncogenes antagonize the cGAS-STING DNA sensing pathway. Science 350, 568-571 (2015).
    • (2015) Science , vol.350 , pp. 568-571
    • Lau, L.1    Gray, E.E.2    Brunette, R.L.3    Stetson, D.B.4
  • 119
    • 84938793241 scopus 로고    scopus 로고
    • Modulation of the cGAS-STING DNA sensing pathway by gammaherpesviruses
    • Ma, Z. et al. Modulation of the cGAS-STING DNA sensing pathway by gammaherpesviruses. Proc. Natl Acad. Sci. USA 112, E4306-E4315 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. E4306-E4315
    • Ma, Z.1
  • 120
    • 84922513904 scopus 로고    scopus 로고
    • Evasion of innate cytosolic DNA sensing by a gammaherpesvirus facilitates establishment of latent infection
    • Sun, C. et al. Evasion of innate cytosolic DNA sensing by a gammaherpesvirus facilitates establishment of latent infection. J. Immunol. 194, 1819-1831 (2015).
    • (2015) J. Immunol. , vol.194 , pp. 1819-1831
    • Sun, C.1
  • 121
    • 84868095535 scopus 로고    scopus 로고
    • Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein
    • Orzalli, M. H., DeLuca, N. A. & Knipe, D. M. Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein. Proc. Natl Acad. Sci. USA 109, E3008-E3017 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. E3008-E3017
    • Orzalli, M.H.1    DeLuca, N.A.2    Knipe, D.M.3
  • 122
    • 84888049352 scopus 로고    scopus 로고
    • The viral ubiquitin ligase ICP0 is neither sufficient nor necessary for degradation of the cellular DNA sensor IFI16 during herpes simplex virus 1 infection
    • Cuchet-Lourenco, D., Anderson, G., Sloan, E., Orr, A. & Everett, R. D. The viral ubiquitin ligase ICP0 is neither sufficient nor necessary for degradation of the cellular DNA sensor IFI16 during herpes simplex virus 1 infection. J. Virol. 87, 13422-13432 (2013).
    • (2013) J. Virol. , vol.87 , pp. 13422-13432
    • Cuchet-Lourenco, D.1    Anderson, G.2    Sloan, E.3    Orr, A.4    Everett, R.D.5
  • 123
    • 84940542596 scopus 로고    scopus 로고
    • Interactions of the antiviral factor interferon γ-inducible protein 16 (IFI16) mediate immune signaling and herpes simplex virus-1 immunosuppression
    • Diner, B. A., Lum, K. K., Javitt, A. & Cristea, I. M. Interactions of the antiviral factor interferon γ-inducible protein 16 (IFI16) mediate immune signaling and herpes simplex virus-1 immunosuppression. Mol. Cell Proteomics 14, 2341-2356 (2015).
    • (2015) Mol. Cell Proteomics , vol.14 , pp. 2341-2356
    • Diner, B.A.1    Lum, K.K.2    Javitt, A.3    Cristea, I.M.4
  • 124
    • 84868102239 scopus 로고    scopus 로고
    • DENV inhibits type i IFN production in infected cells by cleaving human STING
    • Aguirre, S. et al. DENV inhibits type I IFN production in infected cells by cleaving human STING. PLoS Pathog. 8, e1002934 (2012).
    • (2012) PLoS Pathog. , vol.8 , pp. e1002934
    • Aguirre, S.1
  • 125
    • 84864036246 scopus 로고    scopus 로고
    • Dengue virus targets the adaptor protein MITA to subvert host innate immunity
    • Yu, C. Y. et al. Dengue virus targets the adaptor protein MITA to subvert host innate immunity. PLoS Pathog. 8, e1002780 (2012).
    • (2012) PLoS Pathog. , vol.8 , pp. e1002780
    • Yu, C.Y.1
  • 126
    • 84941271782 scopus 로고    scopus 로고
    • Inhibition of cGAS DNA sensing by a herpesvirus virion protein
    • Wu, J. J. et al. Inhibition of cGAS DNA sensing by a herpesvirus virion protein. Cell Host Microbe 18, 333-344 (2015).
    • (2015) Cell Host Microbe , vol.18 , pp. 333-344
    • Wu, J.J.1
  • 127
    • 84887929864 scopus 로고    scopus 로고
    • Human cytomegalovirus tegument protein pUL83 inhibits IFI16-mediated DNA sensing for immune evasion
    • Li, T., Chen, J. & Cristea, I. M. Human cytomegalovirus tegument protein pUL83 inhibits IFI16-mediated DNA sensing for immune evasion. Cell Host Microbe 14, 591-599 (2013).
    • (2013) Cell Host Microbe , vol.14 , pp. 591-599
    • Li, T.1    Chen, J.2    Cristea, I.M.3
  • 128
    • 4644312884 scopus 로고    scopus 로고
    • Identification of proteins in human cytomegalovirus (HCMV) particles: The HCMV proteome
    • Varnum, S. M. et al. Identification of proteins in human cytomegalovirus (HCMV) particles: the HCMV proteome. J. Virol. 78, 10960-10966 (2004).
    • (2004) J. Virol. , vol.78 , pp. 10960-10966
    • Varnum, S.M.1
  • 129
    • 84901355951 scopus 로고    scopus 로고
    • Innate nuclear sensor IFI16 translocates into the cytoplasm during the early stage of in vitro human cytomegalovirus infection and is entrapped in the egressing virions during the late stage
    • Dell'Oste, V. et al. Innate nuclear sensor IFI16 translocates into the cytoplasm during the early stage of in vitro human cytomegalovirus infection and is entrapped in the egressing virions during the late stage. J. Virol. 88, 6970-6982 (2014).
    • (2014) J. Virol. , vol.88 , pp. 6970-6982
    • Dell'Oste, V.1
  • 130
    • 84886797274 scopus 로고    scopus 로고
    • Autophagy in infection, inflammation and immunity
    • Deretic, V., Saitoh, T. & Akira, S. Autophagy in infection, inflammation and immunity. Nat. Rev. Immunol. 13, 722-737 (2013).
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 722-737
    • Deretic, V.1    Saitoh, T.2    Akira, S.3
  • 131
    • 84945945130 scopus 로고    scopus 로고
    • RIG-I-like receptors and autoimmune diseases
    • Kato, H. & Fujita, T. RIG-I-like receptors and autoimmune diseases. Curr. Opin. Immunol. 37, 40-45 (2015).
    • (2015) Curr. Opin. Immunol. , vol.37 , pp. 40-45
    • Kato, H.1    Fujita, T.2
  • 132
    • 84930179594 scopus 로고    scopus 로고
    • Integration of PKR-dependent translation inhibition with innate immunity is required for a coordinated anti-viral response
    • Dalet, A., Gatti, E. & Pierre, P. Integration of PKR-dependent translation inhibition with innate immunity is required for a coordinated anti-viral response. FEBS Lett. 589, 1539-1545 (2015).
    • (2015) FEBS Lett. , vol.589 , pp. 1539-1545
    • Dalet, A.1    Gatti, E.2    Pierre, P.3
  • 133
    • 84876453384 scopus 로고    scopus 로고
    • Regulation of stress granules and P-bodies during RNA virus infection
    • Lloyd, R. E. Regulation of stress granules and P-bodies during RNA virus infection. Wiley Interdiscip Rev. RNA 4, 317-331 (2013).
    • (2013) Wiley Interdiscip Rev. RNA , vol.4 , pp. 317-331
    • Lloyd, R.E.1
  • 134
    • 84905123345 scopus 로고    scopus 로고
    • OAS proteins and cGAS: Unifying concepts in sensing and responding to cytosolic nucleic acids
    • Hornung, V., Hartmann, R., Ablasser, A. & Hopfner, K. P. OAS proteins and cGAS: unifying concepts in sensing and responding to cytosolic nucleic acids. Nat. Rev. Immunol. 14, 521-528 (2014).
    • (2014) Nat. Rev. Immunol. , vol.14 , pp. 521-528
    • Hornung, V.1    Hartmann, R.2    Ablasser, A.3    Hopfner, K.P.4
  • 135
    • 34547960175 scopus 로고    scopus 로고
    • Small self-RNA generated by RNase L amplifies antiviral innate immunity
    • Malathi, K., Dong, B., Gale, M. & Silverman, R. H. Small self-RNA generated by RNase L amplifies antiviral innate immunity. Nature 448, 816-819 (2007).
    • (2007) Nature , vol.448 , pp. 816-819
    • Malathi, K.1    Dong, B.2    Gale, M.3    Silverman, R.H.4
  • 136
    • 84929960168 scopus 로고    scopus 로고
    • DDX60 is involved in RIG-I-dependent and independent antiviral responses, and its function is attenuated by virus-induced EGFR activation
    • Oshiumi, H. et al. DDX60 is involved in RIG-I-dependent and independent antiviral responses, and its function is attenuated by virus-induced EGFR activation. Cell Rep. 11, 1193-1207 (2015).
    • (2015) Cell Rep. , vol.11 , pp. 1193-1207
    • Oshiumi, H.1
  • 137
    • 63649133278 scopus 로고    scopus 로고
    • AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
    • Hornung, V. et al. AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC. Nature 458, 514-518 (2009).
    • (2009) Nature , vol.458 , pp. 514-518
    • Hornung, V.1
  • 138
    • 77951269392 scopus 로고    scopus 로고
    • The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
    • Rathinam, V. A. et al. The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses. Nat. Immunol. 11, 395-402 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 395-402
    • Rathinam, V.A.1
  • 139
    • 84884332722 scopus 로고    scopus 로고
    • Mechanisms of NOD-like receptor-associated inflammasome activation
    • Wen, H., Miao, E. A. & Ting, J. P. Mechanisms of NOD-like receptor-associated inflammasome activation. Immunity 39, 432-441 (2013).
    • (2013) Immunity , vol.39 , pp. 432-441
    • Wen, H.1    Miao, E.A.2    Ting, J.P.3
  • 140
    • 77957228318 scopus 로고    scopus 로고
    • Central roles of NLRs and inflammasomes in viral infection
    • Kanneganti, T. D. Central roles of NLRs and inflammasomes in viral infection. Nat. Rev. Immunol. 10, 688-698 (2010).
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 688-698
    • Kanneganti, T.D.1
  • 141
    • 70349459620 scopus 로고    scopus 로고
    • Activation of innate immune antiviral responses by NOD2
    • Sabbah, A. et al. Activation of innate immune antiviral responses by NOD2. Nat. Immunol. 10, 1073-1080 (2009).
    • (2009) Nat. Immunol. , vol.10 , pp. 1073-1080
    • Sabbah, A.1
  • 142
    • 64049111768 scopus 로고    scopus 로고
    • The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA
    • Allen, I. C. et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity 30, 556-565 (2009).
    • (2009) Immunity , vol.30 , pp. 556-565
    • Allen, I.C.1
  • 143
    • 60549112774 scopus 로고    scopus 로고
    • Inflammasome recognition of influenza virus is essential for adaptive immune responses
    • Ichinohe, T., Lee, H. K., Ogura, Y., Flavell, R. & Iwasaki, A. Inflammasome recognition of influenza virus is essential for adaptive immune responses. J. Exp. Med. 206, 79-87 (2009).
    • (2009) J. Exp. Med. , vol.206 , pp. 79-87
    • Ichinohe, T.1    Lee, H.K.2    Ogura, Y.3    Flavell, R.4    Iwasaki, A.5
  • 144
    • 74049126045 scopus 로고    scopus 로고
    • Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1β production
    • Poeck, H. et al. Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1β production. Nat. Immunol. 11, 63-69 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 63-69
    • Poeck, H.1
  • 145
    • 33750976374 scopus 로고    scopus 로고
    • 5′-triphosphate RNA is the ligand for RIG-I
    • Hornung, V. et al. 5′-triphosphate RNA is the ligand for RIG-I. Science 314, 994-997 (2006).
    • (2006) Science , vol.314 , pp. 994-997
    • Hornung, V.1
  • 146
    • 33750984771 scopus 로고    scopus 로고
    • RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates
    • Pichlmair, A. et al. RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates. Science 314, 997-1001 (2006).
    • (2006) Science , vol.314 , pp. 997-1001
    • Pichlmair, A.1
  • 147
    • 84908192059 scopus 로고    scopus 로고
    • Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5′-diphosphates
    • Goubau, D. et al. Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5′-diphosphates. Nature 514, 372-375 (2014).
    • (2014) Nature , vol.514 , pp. 372-375
    • Goubau, D.1
  • 148
    • 47949092573 scopus 로고    scopus 로고
    • Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA
    • Saito, T., Owen, D. M., Jiang, F., Marcotrigiano, J. & Gale, M. Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA. Nature 454, 523-527 (2008).
    • (2008) Nature , vol.454 , pp. 523-527
    • Saito, T.1    Owen, D.M.2    Jiang, F.3    Marcotrigiano, J.4    Gale, M.5
  • 149
    • 66149114745 scopus 로고    scopus 로고
    • Nucleotide sequences and modifications that determine RIG-I/RNA binding and signaling activities
    • Uzri, D. & Gehrke, L. Nucleotide sequences and modifications that determine RIG-I/RNA binding and signaling activities. J. Virol. 83, 4174-4184 (2009).
    • (2009) J. Virol. , vol.83 , pp. 4174-4184
    • Uzri, D.1    Gehrke, L.2
  • 150
    • 77957997708 scopus 로고    scopus 로고
    • Preference of RIG-I for short viral RNA molecules in infected cells revealed by next-generation sequencing
    • 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. USA 107, 16303-16308 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 16303-16308
    • Baum, A.1    Sachidanandam, R.2    Garcia-Sastre, A.3
  • 151
    • 75749140581 scopus 로고    scopus 로고
    • RIG-I detects viral genomic RNA during negative-strand RNA virus infection
    • Rehwinkel, J. et al. RIG-I detects viral genomic RNA during negative-strand RNA virus infection. Cell 140, 397-408 (2010).
    • (2010) Cell , vol.140 , pp. 397-408
    • Rehwinkel, J.1
  • 152
    • 70349728538 scopus 로고    scopus 로고
    • Activation of MDA5 requires higher-order RNA structures generated during virus infection
    • Pichlmair, A. et al. Activation of MDA5 requires higher-order RNA structures generated during virus infection. J. Virol. 83, 10761-10769 (2009).
    • (2009) J. Virol. , vol.83 , pp. 10761-10769
    • Pichlmair, A.1
  • 153
    • 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
    • Zust, R. 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. 12, 137-143 (2011).
    • (2011) Nat. Immunol. , vol.12 , pp. 137-143
    • Zust, R.1
  • 154
    • 84941954118 scopus 로고    scopus 로고
    • Sequence-specific activation of the DNA sensor cGAS by Y-form DNA structures as found in primary HIV-1 cDNA
    • Herzner, A. M. et al. Sequence-specific activation of the DNA sensor cGAS by Y-form DNA structures as found in primary HIV-1 cDNA. Nat. Immunol. 16, 1025-1033 (2015).
    • (2015) Nat. Immunol. , vol.16 , pp. 1025-1033
    • Herzner, A.M.1
  • 155
    • 84907515304 scopus 로고    scopus 로고
    • Cellular sensing of viral DNA and viral evasion mechanisms
    • Orzalli, M. H. & Knipe, D. M. Cellular sensing of viral DNA and viral evasion mechanisms. Annu. Rev. Microbiol. 68, 477-492 (2014).
    • (2014) Annu. Rev. Microbiol. , vol.68 , pp. 477-492
    • Orzalli, M.H.1    Knipe, D.M.2
  • 156
    • 84928889567 scopus 로고    scopus 로고
    • CGAS-mediated stabilization of IFI16 promotes innate signaling during herpes simplex virus infection
    • Orzalli, M. H. et al. cGAS-mediated stabilization of IFI16 promotes innate signaling during herpes simplex virus infection. Proc. Natl Acad. Sci. USA 112, E1773-E1781 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. E1773-E1781
    • Orzalli, M.H.1
  • 157
    • 40449097257 scopus 로고    scopus 로고
    • The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response
    • Muruve, D. A. et al. The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response. Nature 452, 103-107 (2008).
    • (2008) Nature , vol.452 , pp. 103-107
    • Muruve, D.A.1
  • 158
    • 33846014297 scopus 로고    scopus 로고
    • Critical role for Cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double-stranded RNA
    • Kanneganti, T. D. et al. Critical role for Cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double-stranded RNA. J. Biol. Chem. 281, 36560-36568 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 36560-36568
    • Kanneganti, T.D.1
  • 159
    • 11444262203 scopus 로고    scopus 로고
    • Influenza A mutant viruses with altered NS1 protein function provoke caspase-1 activation in primary human macrophages resulting in fast apoptosis and release of high levels of interleukins 1β and 18
    • Stasakova, J. et al. Influenza A mutant viruses with altered NS1 protein function provoke caspase-1 activation in primary human macrophages, resulting in fast apoptosis and release of high levels of interleukins 1β and 18. J. Gen. Virol. 86, 185-195 (2005).
    • (2005) J. Gen. Virol. , vol.86 , pp. 185-195
    • Stasakova, J.1
  • 160
    • 84855830938 scopus 로고    scopus 로고
    • Measles virus v protein inhibits NLRP3 inflammasome-mediated interleukin-1β secretion
    • Komune, N., Ichinohe, T., Ito, M. & Yanagi, Y. Measles virus V protein inhibits NLRP3 inflammasome-mediated interleukin-1β secretion. J. Virol. 85, 13019-13026 (2011).
    • (2011) J. Virol. , vol.85 , pp. 13019-13026
    • Komune, N.1    Ichinohe, T.2    Ito, M.3    Yanagi, Y.4
  • 161
    • 28844466449 scopus 로고    scopus 로고
    • A poxvirus-encoded pyrin domain protein interacts with ASC-1 to inhibit host inflammatory and apoptotic responses to infection
    • Johnston, J. B. et al. A poxvirus-encoded pyrin domain protein interacts with ASC-1 to inhibit host inflammatory and apoptotic responses to infection. Immunity 23, 587-598 (2005).
    • (2005) Immunity , vol.23 , pp. 587-598
    • Johnston, J.B.1
  • 162
    • 35548929476 scopus 로고    scopus 로고
    • A Shope fibroma virus PYRIN-only protein modulates the host immune response
    • Dorfleutner, A. et al. A Shope fibroma virus PYRIN-only protein modulates the host immune response. Virus Genes 35, 685-694 (2007).
    • (2007) Virus Genes , vol.35 , pp. 685-694
    • Dorfleutner, A.1
  • 163
    • 84877339331 scopus 로고    scopus 로고
    • Vaccinia virus F1L protein promotes virulence by inhibiting inflammasome activation
    • Gerlic, M. et al. Vaccinia virus F1L protein promotes virulence by inhibiting inflammasome activation. Proc. Natl Acad. Sci. USA 110, 7808-7813 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 7808-7813
    • Gerlic, M.1
  • 164
    • 78751680633 scopus 로고    scopus 로고
    • Discovery of a viral NLR homolog that inhibits the inflammasome
    • Gregory, S. M. et al. Discovery of a viral NLR homolog that inhibits the inflammasome. Science 331, 330-334 (2011).
    • (2011) Science , vol.331 , pp. 330-334
    • Gregory, S.M.1


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