Cited by 3,888interferon and immune responsesImmune Response and InflammationRNA regulation and disease

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Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses

Kato, Hiroki, Takeuchi, Osamu, Sato, Shintaro, Yoneyama, Mitsutoshi, Yamamoto, Masahiro, Matsui, Kosuke, Uematsu, Satoshi, Jung, Andreas, Kawai, Taro, Ishii, Ken J., Yamaguchi, Osamu, Otsu, Kinya, Tsujimura, Tohru, Koh, Chang-Sung, Reis e Sousa, Caetano, Matsuura, Yoshiharu, Fujita, Takashi, Akira, Shizuo·2006·Nature

DOI 10.1038/nature04734

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Abstract

The innate immune system senses viral infection by recognizing a variety of viral components (including double-stranded (ds)RNA) and triggers antiviral responses. The cytoplasmic helicase proteins RIG-I (retinoic-acid-inducible protein I, also known as Ddx58) and MDA5 (melanoma-differentiation-associated gene 5, also known as Ifih1 or Helicard) have been implicated in viral dsRNA recognition. In vitro studies suggest that both RIG-I and MDA5 detect RNA viruses and polyinosine-polycytidylic acid (poly(I:C)), a synthetic dsRNA analogue. Although a critical role for RIG-I in the recognition of several RNA viruses has been clarified, the functional role of MDA5 and the relationship between these dsRNA detectors in vivo are yet to be determined. Here we use mice deficient in MDA5 (MDA5-/-) to show that MDA5 and RIG-I recognize different types of dsRNAs: MDA5 recognizes poly(I:C), and RIG-I detects in vitro transcribed dsRNAs. RNA viruses are also differentially recognized by RIG-I and MDA5. We find that RIG-I is essential for the production of interferons in response to RNA viruses including paramyxoviruses, influenza virus and Japanese encephalitis virus, whereas MDA5 is critical for picornavirus detection. Furthermore, RIG-I-/- and MDA5-/- mice are highly susceptible to infection with these respective RNA viruses compared to control mice. Together, our data show that RIG-I and MDA5 distinguish different RNA viruses and are critical for host antiviral responses.

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Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3
Alexopoulou, L., Holt, A. C., Medzhitov, R., & Flavell, R. A. (2001) · Nature · doi:10.1038/35099560 · Cited by 6,129
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Iwasaki, A., & Medzhitov, R. M. (2004) · Nature Immunology · doi:10.1038/ni1112 · Cited by 4,166
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Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA
Diebold, S. S., Kaisho, T., Hemmi, H., Akira, S., & Reis e Sousa, C. (2004) · Science · doi:10.1126/science.1093616 · Cited by 3,444
Identification and Characterization of MAVS, a Mitochondrial Antiviral Signaling Protein that Activates NF-κB and IRF3
Seth, R. B., Sun, L., Ea, C.-K., & Chen, Z. J. (2005) · Cell · doi:10.1016/j.cell.2005.08.012 · Cited by 3,329
Role of Adaptor TRIF in the MyD88-Independent Toll-Like Receptor Signaling Pathway
Yamamoto, M., Sato, S., Hemmi, H., Hoshino, K., Kaisho, T., Sanjo, H., Takeuchi, O., Sugiyama, M., Okabe, M., Takeda, K., et al. (2003) · Science · doi:10.1126/science.1087262 · Cited by 3,286
IKKε and TBK1 are essential components of the IRF3 signaling pathway
Fitzgerald, K. A., McWhirter, S. M., Faia, K. L., Rowe, D. C., Latz, E., Golenbock, D. T., Coyle, A. J., Liao, S.-M., & Maniatis, T. (2003) · Nature Immunology · doi:10.1038/ni921 · Cited by 2,680
IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
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Dephosphorylation of the RNA Sensors RIG-I and MDA5 by the Phosphatase PP1 Is Essential for Innate Immune Signaling
Wies, E., Wang, M. K., Maharaj, N. P., Chen, K., Zhou, S., Finberg, R. W., & Gack, M. U. (2013) · Immunity · doi:10.1016/j.immuni.2012.11.018 · Cited by 316
Toll-Like Receptor Agonists in Cancer Therapy
Adams, S. (2009) · Immunotherapy · doi:10.2217/imt.09.70 · Cited by 311
Differential Role of TLR- and RLR-Signaling in the Immune Responses to Influenza A Virus Infection and Vaccination
Koyama, S., Ishii, K. J., Kumar, H., Tanimoto, T., Coban, C., Uematsu, S., Kawai, T., & Akira, S. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.7.4711 · Cited by 315
Anti–Melanoma Differentiation–Associated Protein 5–Associated Dermatomyositis: Expanding the Clinical Spectrum
Hall, J. C., Casciola-Rosen, L. A., Samedy-Bates, L.-A., Werner, J. L., Owoyemi, K., Danoff, S. K., & Christopher‐Stine, L. (2013) · Arthritis Care & Research · doi:10.1002/acr.21992 · Cited by 306
The Coxsackievirus B 3Cpro Protease Cleaves MAVS and TRIF to Attenuate Host Type I Interferon and Apoptotic Signaling
Mukherjee, A., Morosky, S. A., Delorme‐Axford, E., Dybdahl-Sissoko, N., Oberste, M. S., Wang, T., & Coyne, C. B. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1001311 · Cited by 316
TRADD Protein Is an Essential Component of the RIG-like Helicase Antiviral Pathway
Michallet, M., Meylan, E., Ermolaeva, M., Vázquez, J., Rebsamen, M., Curran, J. A., Poeck, H., Bscheider, M., Hartmann, G., König, M. F., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.03.013 · Cited by 304
An evolutionary NS1 mutation enhances Zika virus evasion of host interferon induction
Xia, H., Luo, H., Shan, C., Muruato, A. E., Nunes, B. T. D., Medeiros, D. B. D. A., Zou, J., Xie, X., Giraldo, M. I., Vasconcelos, P. F. D. C., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02816-2 · Cited by 316
DDX60, a DEXD/H Box Helicase, Is a Novel Antiviral Factor Promoting RIG-I-Like Receptor-Mediated Signaling
Miyashita, M., Oshiumi, H., Matsumoto, M., & Seya, T. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01368-10 · Cited by 297
Recognition of viral nucleic acids in innate immunity
Yoneyama, M., & Fujita, T. (2009) · Reviews in Medical Virology · doi:10.1002/rmv.633 · Cited by 313
Regulation of immunity and oncogenesis by the IRF transcription factor family
Savitsky, D., Tamura, T., Yanai, H., & Taniguchi, T. (2010) · Cancer Immunology, Immunotherapy · doi:10.1007/s00262-009-0804-6 · Cited by 298
IFN Regulatory Factor Family Members Differentially Regulate the Expression of Type III IFN (IFN-λ) Genes
Österlund, P., Pietilä, T. E., Veckman, V., Kotenko, S. V., & Julkunen, I. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.6.3434 · Cited by 301
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Childs, K., Stock, N., Ross, C., Andrejeva, J., Hilton, L. S., Skinner, M. A., Randall, R. E., & Goodbourn, S. (2006) · Virology · doi:10.1016/j.virol.2006.09.023 · Cited by 299
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Targeting the DNA damage response in immuno-oncology: developments and opportunities
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Foxman, E. F., Storer, J. A., Fitzgerald, M. E., Wasik, B. R., Hou, L., Zhao, H., Turner, P. E., Pyle, A. M., & Iwasaki, A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411030112 · Cited by 302
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McWhirter, S. M., Barbalat, R., Monroe, K. M., Fontana, M. F., Hyodo, M., Joncker, N. T., Ishii, K. J., Akira, S., Colonna, M., Chen, Z. J., et al. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20082874 · Cited by 301
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Lei, Y. L., Wen, H., Yu, Y., Taxman, D. J., Zhang, L., Widman, D. G., Swanson, K. V., Wen, K. W., Damania, B., Moore, C., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.03.025 · Cited by 297
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Zhou, X., Xie, F., Wang, L., Zhang, L., Zhang, S., Fang, M., & Zhou, F. (2020) · Cellular & Molecular Immunology · doi:10.1038/s41423-020-0391-1 · Cited by 294
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Hu, Y., Li, W., Gao, T., Cui, Y., Jin, Y., Li, P., Ma, Q., Liu, X. E., & Cao, C. (2017) · Journal of Virology · doi:10.1128/jvi.02143-16 · Cited by 294
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Coronavirus endoribonuclease targets viral polyuridine sequences to evade activating host sensors
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Ye, X., Zhou, S., & Zhang, H. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02334 · Cited by 299
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Adjuvants: Classification, Modus Operandi , and Licensing
Apostólico, J. D. S., Lunardelli, V. A. S., Coirada, F. C., Boscardin, S. B., & Rosa, D. S. (2016) · Journal of Immunology Research · doi:10.1155/2016/1459394 · Cited by 303
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Judge, A. D., & MacLachlan, I. (2008) · Human Gene Therapy · doi:10.1089/hum.2007.179 · Cited by 281
IFN? induction by influenza A virus is mediated by RIG-I which is regulated by the viral NS1 protein
Opitz, B., Rejaibi, A., Dauber, B., Eckhard, J., Vinzing, M., Schmeck, B., Hippenstiel, S., Suttorp, N., & Wolff, T. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00841.x · Cited by 281
The Control of Adaptive Immune Responses by the Innate Immune System
Schenten, D., & Medzhitov, R. M. (2011) · Advances in immunology · doi:10.1016/b978-0-12-387664-5.00003-0 · Cited by 290
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Casadio, M., Ciancanelli, M. J., Ou, Y.-H., Lorenzo, L., Klaudel‐Dreszler, M., Pauwels, E., Sancho‐Shimizu, V., de Diego, R. P., Abhyankar, A., Israelsson, E., et al. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20111316 · Cited by 292
Viral apoptosis is induced by IRF‐3‐mediated activation of Bax
Chattopadhyay, S., Marques, J. T., Yamashita, M., Peters, K. L., Smith, K., Desai, A., Williams, B. R. G., & Sen, G. C. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.50 · Cited by 281
Dual recognition of herpes simplex viruses by TLR2 and TLR9 in dendritic cells
Sato, A., Linehan, M. M., & Iwasaki, A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605102103 · Cited by 278
The IRF family, revisited
Paun, A., & Pitha, P. M. (2007) · Biochimie · doi:10.1016/j.biochi.2007.01.014 · Cited by 277
Innate Immune Recognition in Infectious and Noninfectious Diseases of the Lung
Opitz, B., van Laak, V., Eitel, J., & Suttorp, N. (2010) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200909-1427so · Cited by 287
Antiviral Activity of Human OASL Protein Is Mediated by Enhancing Signaling of the RIG-I RNA Sensor
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Phosphoinositide Interactions Position cGAS at the Plasma Membrane to Ensure Efficient Distinction between Self- and Viral DNA
Barnett, K. C., Coronas-Serna, J. M., Zhou, W., Ernandes, M. J., Cao, A., Kranzusch, P. J., & Kagan, J. C. (2019) · Cell · doi:10.1016/j.cell.2019.01.049 · Cited by 275
Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein 1β Modulates Host Innate Immune Response by Antagonizing IRF3 Activation
Beura, L. K., Sarkar, S. N., Kwon, B., Subramaniam, S., Jones, C., Pattnaik, A. K., & Osorio, F. A. (2009) · Journal of Virology · doi:10.1128/jvi.01326-09 · Cited by 271
The Innate Immune Sensor LGP2 Activates Antiviral Signaling by Regulating MDA5-RNA Interaction and Filament Assembly
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Innate immune evasion strategies of DNA and RNA viruses
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Yoneyama, M., & Fujita, T. (2008) · Immunity · doi:10.1016/j.immuni.2008.07.009 · Cited by 266
The response of mammalian cells to double-stranded RNA
Gantier, M. P., & Williams, B. R. G. (2007) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2007.06.016 · Cited by 273
Type I interferons: crucial participants in disease amplification in autoimmunity
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Autoimmune Disorders Associated with Gain of Function of the Intracellular Sensor MDA5
Funabiki, M., Kato, H., Miyachi, Y., Toki, H., Motegi, H., Inoue, M., Minowa, O., Yoshida, A., Deguchi, K., Satō, H., et al. (2014) · Immunity · doi:10.1016/j.immuni.2013.12.014 · Cited by 262
The Ubiquitin Ligase Riplet Is Essential for RIG-I-Dependent Innate Immune Responses to RNA Virus Infection
Oshiumi, H., Miyashita, M., Inoue, N., Okabe, M., Matsumoto, M., & Seya, T. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.11.008 · Cited by 264
SARS-CoV-2 ORF9b inhibits RIG-I-MAVS antiviral signaling by interrupting K63-linked ubiquitination of NEMO
Wu, J., Shi, Y., Pan, X., Wu, S., Hou, R., Zhang, Y., Zhong, T., Tang, H., Du, W., Wang, L., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108761 · Cited by 278
Aspects of Genetic Susceptibility to Human Infectious Diseases
Hill, A. V. S. (2006) · Annual Review of Genetics · doi:10.1146/annurev.genet.40.110405.090546 · Cited by 267
Positive Regulation of Interferon Regulatory Factor 3 Activation by Herc5 via ISG15 Modification
Shi, H.-X., Yang, K. S., Liu, X., Liu, X.-Y., Wei, B., Shan, Y.-F., Zhu, L.-H., & Wang, C. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01466-09 · Cited by 265
Dermatomyositis With Anti-MDA5 Antibodies: Bioclinical Features, Pathogenesis and Emerging Therapies
Nombel, A., Fabien, N., & Coutant, F. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.773352 · Cited by 276
The IRF Family Transcription Factors at the Interface of Innate and Adaptive Immune ResponsesPreprint
Ikushima, H., Negishi, H., & Taniguchi, T. (2013) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2013.78.020321 · Cited by 273
Viral Myocarditis
Yajima, T., & Knowlton, K. U. (2009) · Circulation · doi:10.1161/circulationaha.108.766022 · Cited by 266
Anti-MDA5 and anti-TIF1-γ antibodies have clinical significance for patients with dermatomyositis
Hoshino, K., Muro, Y., Sugiura, K., Tomita, Y., Nakashima, R., & Mimori, T. (2010) · Lara D. Veeken · doi:10.1093/rheumatology/keq153 · Cited by 261
Regulation of NF‐κB by deubiquitinases
Harhaj, E. W., & Dixit, V. M. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01100.x · Cited by 266
Mitochondrial Membrane Potential Is Required for MAVS-Mediated Antiviral Signaling
Koshiba, T., Yasukawa, K., Yanagi, Y., & Kawabata, S.-I. (2011) · Science Signaling · doi:10.1126/scisignal.2001147 · Cited by 257
Mitochondrial Antiviral Signaling Protein Plays a Major Role in Induction of the Fish Innate Immune Response against RNA and DNA Viruses
Biacchesi, S., Berre, M. L., Lamoureux, A., Louise, Y., Lauret, É., Boudinot, P., & Brémont, M. (2009) · Journal of Virology · doi:10.1128/jvi.00404-09 · Cited by 258
Innate immunity, macrophage activation, and atherosclerosis
Yan, Z., & Hansson, G. K. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00554.x · Cited by 258
Peli1 facilitates TRIF-dependent Toll-like receptor signaling and proinflammatory cytokine production
Chang, M., Jin, W., & Sun, S. (2009) · Nature Immunology · doi:10.1038/ni.1777 · Cited by 259
Mitofusin 2 Inhibits Mitochondrial Antiviral Signaling
Yasukawa, K., Oshiumi, H., Takeda, M., Ishihara, N., Yanagi, Y., Seya, T., Kawabata, S.-I., & Koshiba, T. (2009) · Science Signaling · doi:10.1126/scisignal.2000287 · Cited by 255
Origin and evolution of the RIG-I like RNA helicase gene family
Zou, J., Chang, M., Nie, P., & Secombes, C. J. (2009) · BMC Evolutionary Biology · doi:10.1186/1471-2148-9-85 · Cited by 257
Immunity to Respiratory Viruses
Kohlmeier, J. E., & Woodland, D. L. (2008) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132625 · Cited by 262
MDA5 Detects the Double-Stranded RNA Replicative Form in Picornavirus-Infected Cells
Feng, Q., Hato, S. V., Langereis, M. A., Zoll, J., Virgen‐Slane, R., Peisley, A., Hur, S., Semler, B. L., van Rij, R. P., & van Kuppeveld, F. J. M. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.10.005 · Cited by 254
Overcoming Barriers for siRNA Therapeutics: From Bench to Bedside
Sajid, M. I., Moazzam, M., Kato, S., Cho, K. Y., & Tiwari, R. K. (2020) · Pharmaceuticals · doi:10.3390/ph13100294 · Cited by 262
Toll‐like receptors, RIG‐I‐like RNA helicases and the antiviral innate immune response
Thompson, A. J. V., & LOCARNINI, S. A. (2007) · Immunology and Cell Biology · doi:10.1038/sj.icb.7100100 · Cited by 260
Phosphatase SHP-1 promotes TLR- and RIG-I-activated production of type I interferon by inhibiting the kinase IRAK1
An, H., Hou, J., Zhou, J., Zhao, W., Xu, H., Zheng, Y., Yu, Y., Liu, S., & Cao, X. (2008) · Nature Immunology · doi:10.1038/ni.1604 · Cited by 250
Peste Des Petits Ruminants Virus Infection of Small Ruminants: A Comprehensive Review
Kumar, N., Maherchandani, S., Kashyap, S. K., Singh, S. V., Sharma, S., Chaubey, K. K., & Ly, H. (2014) · Viruses · doi:10.3390/v6062287 · Cited by 249
Constitutive aryl hydrocarbon receptor signaling constrains type I interferon-mediated antiviral innate defense
Yamada, T., Horimoto, H., Kameyama, T., Hayakawa, S., Yamato, H., Dazai, M., Takada, A., Kida, H., Bott, D., Zhou, A. C., et al. (2016) · Nature Immunology · doi:10.1038/ni.3422 · Cited by 251
Particulate formulations for the delivery of poly(I:C) as vaccine adjuvant
Hafner, A. M., Corthésy, B., & Merkle, H. P. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2013.05.013 · Cited by 254
Manipulation of the nuclear factor-κB pathway and the innate immune response by viruses
Hiscott, J. B., Nguyen, T.-L. A., Argüello, M., Nakhaei, P., & Paz, S. (2006) · Oncogene · doi:10.1038/sj.onc.1209941 · Cited by 251
RIP kinases: key decision makers in cell death and innate immunity
Humphries, F., Yang, S., Wang, B., & Moynagh, P. N. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.126 · Cited by 249
The Influenza Virus Protein PB1-F2 Inhibits the Induction of Type I Interferon at the Level of the MAVS Adaptor Protein
Varga, Z. T., Ramos, I., Hai, R., Schmolke, M., García‐Sastre, A., Fernández-Sesma, A., & Palese, P. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002067 · Cited by 246
The molecular mechanism of RIG‐I activation and signaling
Thoresen, D., Wang, W., Galls, D., Guo, R., Xu, L., & Pyle, A. M. (2021) · Immunological Reviews · doi:10.1111/imr.13022 · Cited by 243
Cytoplasmic DNA innate immune pathways
Barber, G. N. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01051.x · Cited by 254
Whatever turns you on: accessory-cell-dependent activation of NK cells by pathogens
Newman, K. C., & Riley, E. M. (2007) · Nature reviews. Immunology · doi:10.1038/nri2057 · Cited by 245
The E3 ubiquitin ligase TRIM21 negatively regulates the innate immune response to intracellular double-stranded DNA
Zhang, Z., Bao, M., Lu, N., Weng, L., Yuan, B., & Liu, Y. (2012) · Nature Immunology · doi:10.1038/ni.2492 · Cited by 249
How RIG-I like receptors activate MAVS
Wu, B., & Hur, S. (2015) · Current Opinion in Virology · doi:10.1016/j.coviro.2015.04.004 · Cited by 242
Expanding role of ubiquitination in NF-κB signaling
Liu, S., & Chen, Z. J. (2010) · Cell Research · doi:10.1038/cr.2010.170 · Cited by 243
Functional analysis via standardized whole-blood stimulation systems defines the boundaries of a healthy immune response to complex stimuli
Duffy, D., Rouilly, V., Libri, V., Hasan, M., Beitz, B., David, M., Urrutia, A., Bisiaux, A., LaBrie, S. T., Dubois, A., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.03.002 · Cited by 242
Evasion of Influenza A Viruses from Innate and Adaptive Immune Responses
van de Sandt, C. E., Kreijtz, J. H. C. M., & Rimmelzwaan, G. F. (2012) · Viruses · doi:10.3390/v4091438 · Cited by 267
Role of Double-Stranded RNA Pattern Recognition Receptors in Rhinovirus-Induced Airway Epithelial Cell Responses
Wang, Q. A., Nagarkar, D. R., Bowman, E., Schneider, D., Gosangi, B., Lei, J., Zhao, Y., McHenry, C. L., Burgens, R. V., Miller, D. J., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901386 · Cited by 244
Ebola Virus Protein VP35 Impairs the Function of Interferon Regulatory Factor-Activating Kinases IKKε and TBK-1
Prins, K. C., Cardenas, W. B., & Basler, C. F. (2009) · Journal of Virology · doi:10.1128/jvi.01875-08 · Cited by 238
Pathogen recognition by innate immunity and its signaling
AKIRA, S. (2009) · Proceedings of the Japan Academy, Series B · doi:10.2183/pjab.85.143 · Cited by 240
Self-citation
Adenovirus vector induced innate immune responses: impact upon efficacy and toxicity in gene therapy and vaccine applications.
Hartman, Z. C., Appledorn, D. M., & Amalfitano, A. (2008) · Virus Research · doi:10.1016/j.virusres.2007.10.005 · Cited by 239
Convergence of the NF-κB and IRF pathways in the regulation of the innate antiviral response
Hiscott, J. B. (2007) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2007.06.002 · Cited by 239
Apoptosis and Necroptosis as Host Defense Strategies to Prevent Viral Infection
Orzalli, M. H., & Kagan, J. C. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.05.007 · Cited by 241
Sweeten PAMPs: Role of sugar complexed PAMPs in innate immunity and vaccine biology
Mahla, R. S. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00248 · Cited by 239
Negative Feedback Regulation of RIG-I-Mediated Antiviral Signaling by Interferon-Induced ISG15 Conjugation
Kim, M.-J., Hwang, S., Imaizumi, T., & Yoo, J.-Y. (2007) · Journal of Virology · doi:10.1128/jvi.01650-07 · Cited by 239
The role of airway epithelial cells and innate immune cells in chronic respiratory disease
Holtzman, M. J., Byers, D. E., Alexander‐Brett, J. M., & Wang, X. (2014) · Nature reviews. Immunology · doi:10.1038/nri3739 · Cited by 246
Pathogen recognition by innate receptors
Kumagai, Y., Takeuchi, O., & Akira, S. (2008) · Journal of Infection and Chemotherapy · doi:10.1007/s10156-008-0596-1 · Cited by 241
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Saitoh, T., Satoh, T., Yamamoto, N., Uematsu, S., Takeuchi, O., Kawai, T., & Akira, S. (2011) · Immunity · doi:10.1016/j.immuni.2011.03.010 · Cited by 237
SARS-CoV nucleocapsid protein antagonizes IFN-β response by targeting initial step of IFN-β induction pathway, and its C-terminal region is critical for the antagonism
Lu, X., Pan, J., Tao, J., & Guo, D. (2010) · Virus Genes · doi:10.1007/s11262-010-0544-x · Cited by 235
Induction and evasion of type I interferon responses by influenza viruses
García‐Sastre, A. (2011) · Virus Research · doi:10.1016/j.virusres.2011.10.017 · Cited by 235
Ral GTPases and cancer: linchpin support of the tumorigenic platform
Bodemann, B. O., & White, M. A. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2296 · Cited by 231
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Lu, C. C., Xu, H., Ranjith-Kumar, C. T., Brooks, M. T., Hou, T. Y., Hu, F., Herr, A. B., Strong, R. K., Kao, C. C., & Li, P. (2010) · Structure · doi:10.1016/j.str.2010.05.007 · Cited by 233
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Holm, C. K., Rahbek, S. H., Gad, H. H., Bak, R. O., Jakobsen, M. R., Jiang, Z., Hansen, A. L., Jensen, S. K., Sun, C., Thomsen, M. K., et al. (2016) · Nature Communications · doi:10.1038/ncomms10680 · Cited by 241
Mitochondrial DNA-triggered innate immune response: mechanisms and diseases
Hu, M.-M., & Shu, H. (2023) · Cellular and Molecular Immunology · doi:10.1038/s41423-023-01086-x · Cited by 263
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Garmaroudi, F. S., Marchant, D., Hendry, R. G., Luo, H., Yang, D., Ye, X., Shi, J., & McManus, B. M. (2015) · Future Microbiology · doi:10.2217/fmb.15.5 · Cited by 232
Vaccine adjuvants as potential cancer immunotherapeutics
Temizoz, B., Kuroda, E., & Ishii, K. J. (2016) · International Immunology · doi:10.1093/intimm/dxw015 · Cited by 236
Epithelial cells and airway diseases
Proud, D., & Leigh, R. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01033.x · Cited by 237
MDA-5 Recognition of a Murine Norovirus
McCartney, S. A., Thackray, L. B., Gitlin, L., Gilfillan, S., Virgin, H. W., & Colonna, M. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000108 · Cited by 224
Murine Coronavirus Mouse Hepatitis Virus Is Recognized by MDA5 and Induces Type I Interferon in Brain Macrophages/Microglia
Roth-Cross, J. K., Bender, S. J., & Weiss, S. R. (2008) · Journal of Virology · doi:10.1128/jvi.01199-08 · Cited by 228

Authors: Kato, H., Takeuchi, O., Sato, S., Yoneyama, M., Yamamoto, M., Matsui, K., Uematsu, S., Jung, A., Kawai, T., Ishii, K. J., Yamaguchi, O., Otsu, K., Tsujimura, T., Koh, C.-S., Reis e Sousa, C., Matsuura, Y., Fujita, T., & Akira, S.
Affiliations: Research Institute for Microbial Diseases, The University of Osaka (JP)
Japan Science and Technology Agency (JP)
Kyoto University (JP)
The University of Osaka (JP)
Hyogo Medical University (JP)
Shinshu University (JP)
Corresponding author: Akira, Shizuo
ORCID: Kato, Hiroki
Takeuchi, Osamu
Sato, Shintaro
Yoneyama, Mitsutoshi
Yamamoto, Masahiro
Uematsu, Satoshi
Kawai, Taro
Ishii, Ken J.
Yamaguchi, Osamu
Otsu, Kinya
Tsujimura, Tohru
Matsuura, Yoshiharu
Fujita, Takashi
Akira, Shizuo
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2006-04-09
Volume: 441
Issue: 7089
Pages: 101-105
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature04734
OpenAlex: W2028575270
Cited by: 3,888
References: 28
Citations by year: 2026: 143 · 2025: 156 · 2024: 146 · 2023: 163 · 2022: 176 · 2021: 204 · 2020: 182 · 2019: 169 · 2018: 169 · 2017: 175 · 2016: 169 · 2015: 182 · 2014: 233 · 2013: 218 · 2012: 236
FWCI: 88.17
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
Keywords: MDA5, RIG-I, double-stranded RNA recognition, antiviral innate immunity, interferon production, poly(I:C), paramyxovirus, influenza virus, Japanese encephalitis virus, picornavirus, viral susceptibility
MeSH terms: DEAD Box Protein 58, Interferon-Induced Helicase, IFIH1, Animals, Encephalitis Virus, Japanese, Encephalomyocarditis virus, Immunity, Innate, RNA Viruses, RNA, Double-Stranded, RNA, Viral, RNA Helicases, Mice, DEAD-box RNA Helicases

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Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses

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