메뉴 건너뛰기




Volumn 75, Issue , 2016, Pages 112-121

Esterase D enhances type I interferon signal transduction to suppress foot-and-mouth disease virus replication

Author keywords

Antiviral response; Esterase D; Foot and mouth disease virus; Interferon stimulated genes; IRF3

Indexed keywords

ANTIVIRUS AGENT; BETA INTERFERON; CARBOXYLESTERASE; INTERFERON; INTERFERON REGULATORY FACTOR 3; MESSENGER RNA; S-FORMYLGLUTATHIONE HYDROLASE; THIOL ESTER HYDROLASE;

EID: 84979300806     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2016.05.016     Document Type: Article
Times cited : (15)

References (39)
  • 1
    • 65649083024 scopus 로고    scopus 로고
    • Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2
    • Bamming, D., Horvath, C.M., Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2. J. Biol. Chem. 284 (2009), 9700–9712.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9700-9712
    • Bamming, D.1    Horvath, C.M.2
  • 2
    • 0033988512 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
    • Belsham, G.J., McInerney, G.M., Ross-Smith, N., Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells. J. Virol. 74 (2000), 272–280.
    • (2000) J. Virol. , vol.74 , pp. 272-280
    • Belsham, G.J.1    McInerney, G.M.2    Ross-Smith, N.3
  • 4
    • 32444446676 scopus 로고    scopus 로고
    • The leader proteinase of foot-and-mouth disease virus inhibits the induction of beta interferon mRNA and blocks the host innate immune response
    • de Los Santos, T., de Avila Botton, S., Weiblen, R., Grubman, M.J., The leader proteinase of foot-and-mouth disease virus inhibits the induction of beta interferon mRNA and blocks the host innate immune response. J. Virol. 80 (2006), 1906–1914.
    • (2006) J. Virol. , vol.80 , pp. 1906-1914
    • de Los Santos, T.1    de Avila Botton, S.2    Weiblen, R.3    Grubman, M.J.4
  • 5
    • 79951815029 scopus 로고    scopus 로고
    • Porcine type I interferon rapidly protects swine against challenge with multiple serotypes of foot-and-mouth disease virus
    • Dias, C.C., Moraes, M.P., Segundo, F.D., de los Santos, T., Grubman, M.J., Porcine type I interferon rapidly protects swine against challenge with multiple serotypes of foot-and-mouth disease virus. J. Interferon Cytokine Res. 31 (2011), 227–236.
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 227-236
    • Dias, C.C.1    Moraes, M.P.2    Segundo, F.D.3    de los Santos, T.4    Grubman, M.J.5
  • 6
    • 84955244450 scopus 로고    scopus 로고
    • Swine TRIM21 restricts FMDV infection via an intracellular neutralization mechanism
    • Fan, W., Zhang, D., Qian, P., Qian, S., Wu, M., Chen, H., Li, X., Swine TRIM21 restricts FMDV infection via an intracellular neutralization mechanism. Antiviral Res. 127 (2016), 32–40.
    • (2016) Antiviral Res. , vol.127 , pp. 32-40
    • Fan, W.1    Zhang, D.2    Qian, P.3    Qian, S.4    Wu, M.5    Chen, H.6    Li, X.7
  • 8
    • 0342656954 scopus 로고    scopus 로고
    • Regulation of RANTES chemokine gene expression requires cooperativity between NF-kappa B and IFN-regulatory factor transcription factors
    • Genin, P., Algarte, M., Roof, P., Lin, R.T., Hiscott, J., Regulation of RANTES chemokine gene expression requires cooperativity between NF-kappa B and IFN-regulatory factor transcription factors. J. Immunol. 164 (2000), 5352–5361.
    • (2000) J. Immunol. , vol.164 , pp. 5352-5361
    • Genin, P.1    Algarte, M.2    Roof, P.3    Lin, R.T.4    Hiscott, J.5
  • 9
    • 33744938480 scopus 로고    scopus 로고
    • Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG
    • Gonzalez, C.F., Proudfoot, M., Brown, G., Korniyenko, Y., Mori, H., Savchenko, A.V., Yakunin, A.F., Molecular basis of formaldehyde detoxification. Characterization of two S-formylglutathione hydrolases from Escherichia coli, FrmB and YeiG. J. Biol. Chem. 281 (2006), 14514–14522.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14514-14522
    • Gonzalez, C.F.1    Proudfoot, M.2    Brown, G.3    Korniyenko, Y.4    Mori, H.5    Savchenko, A.V.6    Yakunin, A.F.7
  • 10
    • 0029967019 scopus 로고    scopus 로고
    • S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification?
    • Harms, N., Ras, J., Reijnders, W.N., van Spanning, R.J., Stouthamer, A.H., S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification?. J. Bacteriol. 178 (1996), 6296–6299.
    • (1996) J. Bacteriol. , vol.178 , pp. 6296-6299
    • Harms, N.1    Ras, J.2    Reijnders, W.N.3    van Spanning, R.J.4    Stouthamer, A.H.5
  • 11
    • 4344701248 scopus 로고    scopus 로고
    • The UK foot-and-mouth disease outbreak – the aftermath
    • Haydon, D.T., Kao, R.R., Kitching, R.P., The UK foot-and-mouth disease outbreak – the aftermath. Nat. Rev. Microbiol. 2 (2004), 675–681.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 675-681
    • Haydon, D.T.1    Kao, R.R.2    Kitching, R.P.3
  • 12
    • 49649125136 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Ro52 negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3
    • Higgs, R., Gabhann, J.N., Ben Larbi, N., Breen, E.P., Fitzgerald, K.A., Jefferies, C.A., The E3 ubiquitin ligase Ro52 negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. J. Immunol. 181 (2008), 1780–1786.
    • (2008) J. Immunol. , vol.181 , pp. 1780-1786
    • Higgs, R.1    Gabhann, J.N.2    Ben Larbi, N.3    Breen, E.P.4    Fitzgerald, K.A.5    Jefferies, C.A.6
  • 13
    • 79957604087 scopus 로고    scopus 로고
    • Identification of the role of RIG-I, MDA-5 and TLR3 in sensing RNA viruses in porcine epithelial cells using lentivirus-driven RNA interference
    • Husser, L., Alves, M.P., Ruggli, N., Summerfield, A., Identification of the role of RIG-I, MDA-5 and TLR3 in sensing RNA viruses in porcine epithelial cells using lentivirus-driven RNA interference. Virus Res. 159 (2011), 9–16.
    • (2011) Virus Res. , vol.159 , pp. 9-16
    • Husser, L.1    Alves, M.P.2    Ruggli, N.3    Summerfield, A.4
  • 15
    • 84886792476 scopus 로고    scopus 로고
    • The economic impacts of foot and mouth disease – what are they, how big are they and where do they occur?
    • Knight-Jones, T.J., Rushton, J., The economic impacts of foot and mouth disease – what are they, how big are they and where do they occur?. Prev. Vet. Med. 112 (2013), 161–173.
    • (2013) Prev. Vet. Med. , vol.112 , pp. 161-173
    • Knight-Jones, T.J.1    Rushton, J.2
  • 16
    • 65649141586 scopus 로고    scopus 로고
    • Pathogen recognition in the innate immune response
    • Kumar, H., Kawai, T., Akira, S., Pathogen recognition in the innate immune response. Biochem. J. 420 (2009), 1–16.
    • (2009) Biochem. J. , vol.420 , pp. 1-16
    • Kumar, H.1    Kawai, T.2    Akira, S.3
  • 18
    • 84958999529 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus non-structural protein 3A inhibits the interferon-β signaling pathway
    • Li, D., Lei, C., Xu, Z., Yang, F., Liu, H., Zhu, Z., Li, S., Liu, X., Shu, H., Zheng, H., Foot-and-mouth disease virus non-structural protein 3A inhibits the interferon-β signaling pathway. Sci. Rep., 6, 2016, 21888.
    • (2016) Sci. Rep. , vol.6 , pp. 21888
    • Li, D.1    Lei, C.2    Xu, Z.3    Yang, F.4    Liu, H.5    Zhu, Z.6    Li, S.7    Liu, X.8    Shu, H.9    Zheng, H.10
  • 19
    • 84966393533 scopus 로고    scopus 로고
    • The VP3 structural protein of foot-and-mouth disease virus inhibits the IFN-β signaling pathway
    • fj.15-281410
    • Li, D., Yang, W., Yang, F., Liu, H., Zhu, Z., Lian, K., Lei, C., Li, S., Liu, X., Zheng, H., The VP3 structural protein of foot-and-mouth disease virus inhibits the IFN-β signaling pathway. FASEB J., 1, 2016 fj.15-281410.
    • (2016) FASEB J. , vol.1
    • Li, D.1    Yang, W.2    Yang, F.3    Liu, H.4    Zhu, Z.5    Lian, K.6    Lei, C.7    Li, S.8    Liu, X.9    Zheng, H.10
  • 20
    • 58149401211 scopus 로고    scopus 로고
    • CaMKII promotes TLR-triggered proinflammatory cytokine and type I interferon production by directly binding and activating TAK1 and IRF3 in macrophages
    • Liu, X., Yao, M., Li, N., Wang, C., Zheng, Y., Cao, X., CaMKII promotes TLR-triggered proinflammatory cytokine and type I interferon production by directly binding and activating TAK1 and IRF3 in macrophages. Blood 112 (2008), 4961–4970.
    • (2008) Blood , vol.112 , pp. 4961-4970
    • Liu, X.1    Yao, M.2    Li, N.3    Wang, C.4    Zheng, Y.5    Cao, X.6
  • 21
    • 0037232731 scopus 로고    scopus 로고
    • Molecular basis of pathogenesis of FMDV
    • Mason, P.W., Grubman, M.J., Baxt, B., Molecular basis of pathogenesis of FMDV. Virus Res. 91 (2003), 9–32.
    • (2003) Virus Res. , vol.91 , pp. 9-32
    • Mason, P.W.1    Grubman, M.J.2    Baxt, B.3
  • 22
    • 78650048628 scopus 로고    scopus 로고
    • Function and regulation of retinoic acid-inducible gene-I
    • Matsumiya, T., Stafforini, D.M., Function and regulation of retinoic acid-inducible gene-I. Crit. Rev. Immunol. 30 (2010), 489–513.
    • (2010) Crit. Rev. Immunol. , vol.30 , pp. 489-513
    • Matsumiya, T.1    Stafforini, D.M.2
  • 23
    • 0028919610 scopus 로고
    • Stimulation of interferon and cytokine gene expression by imiquimod and stimulation by Sendai virus utilize similar signal transduction pathways
    • Megyeri, K., Au, W.-C., Rosztoczy, I., Raj, N., Miller, R.L., Tomai, M.A., Pitha, P.M., Stimulation of interferon and cytokine gene expression by imiquimod and stimulation by Sendai virus utilize similar signal transduction pathways. Mol. Cell. Biol. 15 (1995), 2207–2218.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2207-2218
    • Megyeri, K.1    Au, W.-C.2    Rosztoczy, I.3    Raj, N.4    Miller, R.L.5    Tomai, M.A.6    Pitha, P.M.7
  • 24
    • 34250840521 scopus 로고    scopus 로고
    • Enhanced antiviral activity against foot-and-mouth disease virus by a combination of type I and II porcine interferons
    • Moraes, M.P., de Los Santos, T., Koster, M., Turecek, T., Wang, H., Andreyev, V.G., Grubman, M.J., Enhanced antiviral activity against foot-and-mouth disease virus by a combination of type I and II porcine interferons. J. Virol. 81 (2007), 7124–7135.
    • (2007) J. Virol. , vol.81 , pp. 7124-7135
    • Moraes, M.P.1    de Los Santos, T.2    Koster, M.3    Turecek, T.4    Wang, H.5    Andreyev, V.G.6    Grubman, M.J.7
  • 25
    • 45449109432 scopus 로고    scopus 로고
    • Proteomic surveillance of retinal autoantigens in endogenous uveitis: implication of esterase D and brain-type creatine kinase as novel autoantigens
    • Okunuki, Y., Usui, Y., Kezuka, T., Hattori, T., Masuko, K., Nakamura, H., Yudoh, K., Goto, H., Usui, M., Nishioka, K., Kato, T., Takeuchi, M., Proteomic surveillance of retinal autoantigens in endogenous uveitis: implication of esterase D and brain-type creatine kinase as novel autoantigens. Mol. Vis. 14 (2008), 1094–1104.
    • (2008) Mol. Vis. , vol.14 , pp. 1094-1104
    • Okunuki, Y.1    Usui, Y.2    Kezuka, T.3    Hattori, T.4    Masuko, K.5    Nakamura, H.6    Yudoh, K.7    Goto, H.8    Usui, M.9    Nishioka, K.10    Kato, T.11    Takeuchi, M.12
  • 26
    • 34547930163 scopus 로고    scopus 로고
    • Interferon regulatory factor 3 is regulated by a dual phosphorylation-dependent switch
    • Panne, D., McWhirter, S.M., Maniatis, T., Harrison, S.C., Interferon regulatory factor 3 is regulated by a dual phosphorylation-dependent switch. J. Biol. Chem. 282 (2007), 22816–22822.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22816-22822
    • Panne, D.1    McWhirter, S.M.2    Maniatis, T.3    Harrison, S.C.4
  • 27
    • 18844457095 scopus 로고    scopus 로고
    • Mechanisms of type-I- and type-II-interferon-mediated signalling
    • Platanias, L.C., Mechanisms of type-I- and type-II-interferon-mediated signalling. Nat. Rev. Immunol. 5 (2005), 375–386.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 375-386
    • Platanias, L.C.1
  • 29
    • 82955187705 scopus 로고    scopus 로고
    • Interferon-stimulated genes and their antiviral effector functions
    • Schoggins, J.W., Rice, C.M., Interferon-stimulated genes and their antiviral effector functions. Curr. Opin. Virol. 1 (2011), 519–525.
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 519-525
    • Schoggins, J.W.1    Rice, C.M.2
  • 30
    • 75749090852 scopus 로고    scopus 로고
    • SnapShot: pathways of antiviral innate immunity
    • 436-436 e432
    • Sun, L., Liu, S., Chen, Z.J., SnapShot: pathways of antiviral innate immunity. Cell, 140, 2010 436-436 e432.
    • (2010) Cell , vol.140
    • Sun, L.1    Liu, S.2    Chen, Z.J.3
  • 31
    • 77955479087 scopus 로고    scopus 로고
    • Perturbation of 60 S ribosomal biogenesis results in ribosomal protein L5- and L11-dependent p53 activation
    • Sun, X.X., Wang, Y.G., Xirodimas, D.P., Dai, M.S., Perturbation of 60 S ribosomal biogenesis results in ribosomal protein L5- and L11-dependent p53 activation. J. Biol. Chem. 285 (2010), 25812–25821.
    • (2010) J. Biol. Chem. , vol.285 , pp. 25812-25821
    • Sun, X.X.1    Wang, Y.G.2    Xirodimas, D.P.3    Dai, M.S.4
  • 32
    • 77955565711 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus leader proteinase inhibits dsRNA-induced type I interferon transcription by decreasing interferon regulatory factor 3/7 in protein levels
    • Wang, D., Fang, L., Luo, R., Ye, R., Fang, Y., Xie, L., Chen, H., Xiao, S., Foot-and-mouth disease virus leader proteinase inhibits dsRNA-induced type I interferon transcription by decreasing interferon regulatory factor 3/7 in protein levels. Biochem. Biophys. Res. Commun. 399 (2010), 72–78.
    • (2010) Biochem. Biophys. Res. Commun. , vol.399 , pp. 72-78
    • Wang, D.1    Fang, L.2    Luo, R.3    Ye, R.4    Fang, Y.5    Xie, L.6    Chen, H.7    Xiao, S.8
  • 33
  • 34
    • 84904156702 scopus 로고    scopus 로고
    • Swine interferon-induced transmembrane protein, sIFITM3, inhibits foot-and-mouth disease virus infection in vitro and in vivo
    • Xu, J., Qian, P., Wu, Q., Liu, S., Fan, W., Zhang, K., Wang, R., Zhang, H., Chen, H., Li, X., Swine interferon-induced transmembrane protein, sIFITM3, inhibits foot-and-mouth disease virus infection in vitro and in vivo. Antiviral Res. 109 (2014), 22–29.
    • (2014) Antiviral Res. , vol.109 , pp. 22-29
    • Xu, J.1    Qian, P.2    Wu, Q.3    Liu, S.4    Fan, W.5    Zhang, K.6    Wang, R.7    Zhang, H.8    Chen, H.9    Li, X.10
  • 35
    • 78650130030 scopus 로고    scopus 로고
    • The ubiquitin E3 ligase RAUL negatively regulates type I interferon through ubiquitination of the transcription factors IRF7 and IRF3
    • Yu, Y.X., Hayward, G.S., The ubiquitin E3 ligase RAUL negatively regulates type I interferon through ubiquitination of the transcription factors IRF7 and IRF3. Immunity 33 (2010), 863–877.
    • (2010) Immunity , vol.33 , pp. 863-877
    • Yu, Y.X.1    Hayward, G.S.2
  • 36
    • 78651488457 scopus 로고    scopus 로고
    • Interferon-Stimulated gene 15 and the protein ISGylation system
    • Zhang, D.X., Zhang, D.E., Interferon-Stimulated gene 15 and the protein ISGylation system. J. Interf. Cytok. Res. 31 (2011), 119–130.
    • (2011) J. Interf. Cytok. Res. , vol.31 , pp. 119-130
    • Zhang, D.X.1    Zhang, D.E.2
  • 37
    • 84872836331 scopus 로고    scopus 로고
    • Engineering foot-and-mouth disease viruses with improved growth properties for vaccine development
    • Zheng, H., Guo, J., Jin, Y., Yang, F., He, J., Lv, L., Zhang, K., Wu, Q., Liu, X., Cai, X., Engineering foot-and-mouth disease viruses with improved growth properties for vaccine development. PLoS One, 8, 2013, e55228.
    • (2013) PLoS One , vol.8 , pp. e55228
    • Zheng, H.1    Guo, J.2    Jin, Y.3    Yang, F.4    He, J.5    Lv, L.6    Zhang, K.7    Wu, Q.8    Liu, X.9    Cai, X.10
  • 38
    • 84908070742 scopus 로고    scopus 로고
    • The ER-associated protein ZDHHC1 is a positive regulator of DNA virus-triggered, MITA/STING-dependent innate immune signaling
    • Zhou, Q., Lin, H., Wang, S., Wang, S., Ran, Y., Liu, Y., Ye, W., Xiong, X., Zhong, B., Shu, H.B., Wang, Y.Y., The ER-associated protein ZDHHC1 is a positive regulator of DNA virus-triggered, MITA/STING-dependent innate immune signaling. Cell Host Microbe 16 (2014), 450–461.
    • (2014) Cell Host Microbe , vol.16 , pp. 450-461
    • Zhou, Q.1    Lin, H.2    Wang, S.3    Wang, S.4    Ran, Y.5    Liu, Y.6    Ye, W.7    Xiong, X.8    Zhong, B.9    Shu, H.B.10    Wang, Y.Y.11
  • 39
    • 84910148691 scopus 로고    scopus 로고
    • Type I interferon-mediated immune response against influenza A virus is attenuated in the absence of p53
    • Zhu, Z., Yang, Y., Wei, J., Shao, D., Shi, Z., Li, B., Liu, K., Qiu, Y., Zheng, H., Ma, Z., Type I interferon-mediated immune response against influenza A virus is attenuated in the absence of p53. Biochem. Biophys. Res. Commun. 454 (2014), 189–195.
    • (2014) Biochem. Biophys. Res. Commun. , vol.454 , pp. 189-195
    • Zhu, Z.1    Yang, Y.2    Wei, J.3    Shao, D.4    Shi, Z.5    Li, B.6    Liu, K.7    Qiu, Y.8    Zheng, H.9    Ma, Z.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.