메뉴 건너뛰기




Volumn 194, Issue 8, 2015, Pages 3756-3767

Mycobacterium tuberculosis Mce3E suppresses host innate immune responses by targeting ERK1/2 signaling

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; INTERLEUKIN 6; MAMMALIAN CELL ENTRY PROTEIN 3E; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; 1,3 BUTADIENE DERIVATIVE; 1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; IL6 PROTEIN, HUMAN; MAPK1 PROTEIN, HUMAN; NITRILE; TNF PROTEIN, HUMAN; TUMOR NECROSIS FACTOR ALPHA;

EID: 84927646643     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1402679     Document Type: Article
Times cited : (54)

References (51)
  • 1
    • 84878560475 scopus 로고    scopus 로고
    • Geneva, Switzerland: WHO. Accessed: February 25, 2015
    • World Health Organization. 2013. Global tuberculosis report 2013. Geneva, Switzerland: WHO. Available at: http://apps.who.int/iris/bitstream/10665/91355/1/9789241564656-eng.pdf. Accessed: February 25, 2015.
    • (2013) Global Tuberculosis Report 2013
    • World Health Organization1
  • 3
    • 84856688022 scopus 로고    scopus 로고
    • Host-pathogen coevolution in human tuberculosis
    • Gagneux, S. 2012. Host-pathogen coevolution in human tuberculosis. Philos. Trans. R. Soc. Lond. B Biol. Sci. 367:850-859.
    • (2012) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.367 , pp. 850-859
    • Gagneux, S.1
  • 4
    • 0034651738 scopus 로고    scopus 로고
    • Virulent Mycobacterium tuberculosis strains evade apoptosis of infected alveolar macrophages
    • Keane, J., H. G. Remold, and H. Kornfeld. 2000. Virulent Mycobacterium tuberculosis strains evade apoptosis of infected alveolar macrophages. J. Immunol. 164:2016-2020.
    • (2000) J. Immunol. , vol.164 , pp. 2016-2020
    • Keane, J.1    Remold, H.G.2    Kornfeld, H.3
  • 5
    • 84859884162 scopus 로고    scopus 로고
    • Coronin-1a inhibits autophagosome formation around Mycobacterium tuberculosis-containing phagosomes and assists mycobacterial survival in macrophages
    • Seto, S., K. Tsujimura, and Y. Koide. 2012. Coronin-1a inhibits autophagosome formation around Mycobacterium tuberculosis-containing phagosomes and assists mycobacterial survival in macrophages. Cell. Microbiol. 14:710-727.
    • (2012) Cell. Microbiol. , vol.14 , pp. 710-727
    • Seto, S.1    Tsujimura, K.2    Koide, Y.3
  • 6
    • 80052050200 scopus 로고    scopus 로고
    • Importance of phagosomal functionality for growth restriction of Mycobacterium tuberculosis in primary human macrophages
    • Welin, A., J. Raffetseder, D. Eklund, O. Stendahl, and M. Lerm. 2011. Importance of phagosomal functionality for growth restriction of Mycobacterium tuberculosis in primary human macrophages. J. Innate Immun. 3:508-518.
    • (2011) J. Innate Immun. , vol.3 , pp. 508-518
    • Welin, A.1    Raffetseder, J.2    Eklund, D.3    Stendahl, O.4    Lerm, M.5
  • 7
    • 33746493349 scopus 로고    scopus 로고
    • Tuberculosis chemotherapy: The influence of bacillary stress and damage response pathways on drug efficacy
    • Warner, D. F., and V. Mizrahi. 2006. Tuberculosis chemotherapy: the influence of bacillary stress and damage response pathways on drug efficacy. Clin. Microbiol. Rev. 19:558-570.
    • (2006) Clin. Microbiol. Rev. , vol.19 , pp. 558-570
    • Warner, D.F.1    Mizrahi, V.2
  • 9
    • 33644976705 scopus 로고    scopus 로고
    • MAP kinases in immune responses
    • Zhang, Y. L., and C. Dong. 2005. MAP kinases in immune responses. Cell. Mol. Immunol. 2:20-27.
    • (2005) Cell. Mol. Immunol. , vol.2 , pp. 20-27
    • Zhang, Y.L.1    Dong, C.2
  • 10
    • 84867619205 scopus 로고    scopus 로고
    • Innate immune gene polymorphisms in tuberculosis
    • Azad, A. K., W. Sadee, and L. S. Schlesinger. 2012. Innate immune gene polymorphisms in tuberculosis. Infect. Immun. 80:3343-3359.
    • (2012) Infect. Immun. , vol.80 , pp. 3343-3359
    • Azad, A.K.1    Sadee, W.2    Schlesinger, L.S.3
  • 11
    • 77955906264 scopus 로고    scopus 로고
    • The nuclear factor NF-kappaB pathway in inflammation
    • Lawrence, T. 2009. The nuclear factor NF-kappaB pathway in inflammation. Cold Spring Harb. Perspect. Biol. 1:a001651.
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1 , pp. a001651
    • Lawrence, T.1
  • 12
    • 35648987280 scopus 로고    scopus 로고
    • Pathogen subversion of cell-intrinsic innate immunity
    • Roy, C. R., and E. S. Mocarski. 2007. Pathogen subversion of cell-intrinsic innate immunity. Nat. Immunol. 8:1179-1187.
    • (2007) Nat. Immunol. , vol.8 , pp. 1179-1187
    • Roy, C.R.1    Mocarski, E.S.2
  • 13
    • 0030904244 scopus 로고    scopus 로고
    • Yersinia enterocolitica promotes deactivation of macrophage mitogen-activated protein kinases extracellular signal-regulated kinase-1/2, p38, and c-Jun. NH2-terminal kinase: Correlation with its inhibitory effect on tumor necrosis factor-alpha production
    • Ruckdeschel, K., J. Machold, A. Roggenkamp, S. Schubert, J. Pierre, R. Zumbihl, J. P. Liautard, J. Heesemann, and B. Rouot. 1997. Yersinia enterocolitica promotes deactivation of macrophage mitogen-activated protein kinases extracellular signal-regulated kinase-1/2, p38, and c-Jun. NH2-terminal kinase: correlation with its inhibitory effect on tumor necrosis factor-alpha production. J. Biol. Chem. 272:15920-15927.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15920-15927
    • Ruckdeschel, K.1    Machold, J.2    Roggenkamp, A.3    Schubert, S.4    Pierre, J.5    Zumbihl, R.6    Liautard, J.P.7    Heesemann, J.8    Rouot, B.9
  • 14
    • 0036263080 scopus 로고    scopus 로고
    • Differential regulation of the mitogenactivated protein kinases by pathogenic and nonpathogenic mycobacteria
    • Roach, S. K., and J. S. Schorey. 2002. Differential regulation of the mitogenactivated protein kinases by pathogenic and nonpathogenic mycobacteria. Infect. Immun. 70:3040-3052.
    • (2002) Infect. Immun. , vol.70 , pp. 3040-3052
    • Roach, S.K.1    Schorey, J.S.2
  • 15
    • 0037406537 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinase pathways in the production of tumor necrosis factor-alpha, interleukin-10, and monocyte chemotactic protein-1 by Mycobacterium tuberculosis H37Rv-infected human monocytes
    • Song, C. H., J. S. Lee, S. H. Lee, K. Lim, H. J. Kim, J. K. Park, T. H. Paik, and E. K. Jo. 2003. Role of mitogen-activated protein kinase pathways in the production of tumor necrosis factor-alpha, interleukin-10, and monocyte chemotactic protein-1 by Mycobacterium tuberculosis H37Rv-infected human monocytes. J. Clin. Immunol. 23:194-201.
    • (2003) J. Clin. Immunol. , vol.23 , pp. 194-201
    • Song, C.H.1    Lee, J.S.2    Lee, S.H.3    Lim, K.4    Kim, H.J.5    Park, J.K.6    Paik, T.H.7    Jo, E.K.8
  • 16
    • 22644435472 scopus 로고    scopus 로고
    • The six mammalian cell entry proteins (Mce3A-F) encoded by the mce3 operon are expressed during in vitro growth of Mycobacterium tuberculosis
    • Ahmad, S., S. El-Shazly, A. S. Mustafa, and R. Al-Attiyah. 2005. The six mammalian cell entry proteins (Mce3A-F) encoded by the mce3 operon are expressed during in vitro growth of Mycobacterium tuberculosis. Scand. J. Immunol. 62:16-24.
    • (2005) Scand. J. Immunol. , vol.62 , pp. 16-24
    • Ahmad, S.1    El-Shazly, S.2    Mustafa, A.S.3    Al-Attiyah, R.4
  • 17
    • 33847775356 scopus 로고    scopus 로고
    • A phylogenomic analysis of the Actinomycetales mce operons
    • Casali, N., and L. W. Riley. 2007. A phylogenomic analysis of the Actinomycetales mce operons. BMC Genomics 8:60.
    • (2007) BMC Genomics , vol.8 , pp. 60
    • Casali, N.1    Riley, L.W.2
  • 19
    • 34748850660 scopus 로고    scopus 로고
    • Internalization by HeLa cells of latex beads coated with mammalian cell entry (Mce) proteins encoded by the mce3 operon of Mycobacterium tuberculosis
    • El-Shazly, S., S. Ahmad, A. S. Mustafa, R. Al-Attiyah, and D. Krajci. 2007. Internalization by HeLa cells of latex beads coated with mammalian cell entry (Mce) proteins encoded by the mce3 operon of Mycobacterium tuberculosis. J. Med. Microbiol. 56:1145-1151.
    • (2007) J. Med. Microbiol. , vol.56 , pp. 1145-1151
    • El-Shazly, S.1    Ahmad, S.2    Mustafa, A.S.3    Al-Attiyah, R.4    Krajci, D.5
  • 23
    • 4944261797 scopus 로고    scopus 로고
    • Mammalian cellentry proteins encoded by the mce3 operon of Mycobacterium tuberculosis are expressed during natural infection in humans
    • Ahmad, S., S. El-Shazly, A. S. Mustafa, and R. Al-Attiyah. 2004. Mammalian cellentry proteins encoded by the mce3 operon of Mycobacterium tuberculosis are expressed during natural infection in humans. Scand. J. Immunol. 60:382-391.
    • (2004) Scand. J. Immunol. , vol.60 , pp. 382-391
    • Ahmad, S.1    El-Shazly, S.2    Mustafa, A.S.3    Al-Attiyah, R.4
  • 24
    • 77953575196 scopus 로고    scopus 로고
    • Characterization of human cellular immune responses to Mycobacterium tuberculosis proteins encoded by genes predicted in RD15 genomic region that is absent in Mycobacterium bovis BCG
    • Al-Attiyah, R., and A. S. Mustafa. 2010. Characterization of human cellular immune responses to Mycobacterium tuberculosis proteins encoded by genes predicted in RD15 genomic region that is absent in Mycobacterium bovis BCG. FEMS Immunol. Med. Microbiol. 59:177-187.
    • (2010) FEMS Immunol. Med. Microbiol. , vol.59 , pp. 177-187
    • Al-Attiyah, R.1    Mustafa, A.S.2
  • 25
    • 33847154642 scopus 로고    scopus 로고
    • The phosphothreonine lyase activity of a bacterial type III effector family
    • Li, H., H. Xu, Y. Zhou, J. Zhang, C. Long, S. Li, S. Chen, J. M. Zhou, and F. Shao. 2007. The phosphothreonine lyase activity of a bacterial type III effector family. Science 315:1000-1003.
    • (2007) Science , vol.315 , pp. 1000-1003
    • Li, H.1    Xu, H.2    Zhou, Y.3    Zhang, J.4    Long, C.5    Li, S.6    Chen, S.7    Zhou, J.M.8    Shao, F.9
  • 26
    • 0036218194 scopus 로고    scopus 로고
    • Expression and localization of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA
    • Cowley, S. C., R. Babakaiff, and Y. Av-Gay. 2002. Expression and localization of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA. Res. Microbiol. 153:233-241.
    • (2002) Res. Microbiol. , vol.153 , pp. 233-241
    • Cowley, S.C.1    Babakaiff, R.2    Av-Gay, Y.3
  • 27
    • 0033578923 scopus 로고    scopus 로고
    • Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector
    • Orth, K., L. E. Palmer, Z. Q. Bao, S. Stewart, A. E. Rudolph, J. B. Bliska, and J. E. Dixon. 1999. Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector. Science 285:1920-1923.
    • (1999) Science , vol.285 , pp. 1920-1923
    • Orth, K.1    Palmer, L.E.2    Bao, Z.Q.3    Stewart, S.4    Rudolph, A.E.5    Bliska, J.B.6    Dixon, J.E.7
  • 29
    • 84871403015 scopus 로고    scopus 로고
    • C-Jun. N-terminal kinase (JNK) and p38 mitogen-activated protein kinase (p38 MAPK) are involved in Mycobacterium tuberculosis-induced expression of Leukotactin-1
    • Cho, J. E., S. Park, S. N. Cho, H. Lee, and Y. S. Kim. 2012. c-Jun. N-terminal kinase (JNK) and p38 mitogen-activated protein kinase (p38 MAPK) are involved in Mycobacterium tuberculosis-induced expression of Leukotactin-1. BMB Rep. 45:583-588.
    • (2012) BMB Rep. , vol.45 , pp. 583-588
    • Cho, J.E.1    Park, S.2    Cho, S.N.3    Lee, H.4    Kim, Y.S.5
  • 30
    • 79952773453 scopus 로고    scopus 로고
    • Modulation of NF-κB signalling by microbial pathogens
    • Rahman, M. M., and G. McFadden. 2011. Modulation of NF-κB signalling by microbial pathogens. Nat. Rev. Microbiol. 9:291-306.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 291-306
    • Rahman, M.M.1    McFadden, G.2
  • 31
    • 11144329901 scopus 로고    scopus 로고
    • Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain
    • Gu, S., J. Chen, K. M. Dobos, E. M. Bradbury, J. T. Belisle, and X. Chen. 2003. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Mol. Cell. Proteomics 2:1284-1296.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1284-1296
    • Gu, S.1    Chen, J.2    Dobos, K.M.3    Bradbury, E.M.4    Belisle, J.T.5    Chen, X.6
  • 32
    • 79955776183 scopus 로고    scopus 로고
    • A Yersinia effector with enhanced inhibitory activity on the NF-κB pathway activates the NLRP3/ASC/caspase-1 inflammasome in macrophages
    • Zheng, Y., S. Lilo, I. E. Brodsky, Y. Zhang, R. Medzhitov, K. B. Marcu, and J. B. Bliska. 2011. A Yersinia effector with enhanced inhibitory activity on the NF-κB pathway activates the NLRP3/ASC/caspase-1 inflammasome in macrophages. PLoS Pathog. 7:e1002026.
    • (2011) PLoS Pathog. , vol.7 , pp. e1002026
    • Zheng, Y.1    Lilo, S.2    Brodsky, I.E.3    Zhang, Y.4    Medzhitov, R.5    Marcu, K.B.6    Bliska, J.B.7
  • 33
    • 84864271151 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and bacterial virulence
    • Whitmore, S. E., and R. J. Lamont. 2012. Tyrosine phosphorylation and bacterial virulence. Int. J. Oral Sci. 4:1-6.
    • (2012) Int. J. Oral Sci. , vol.4 , pp. 1-6
    • Whitmore, S.E.1    Lamont, R.J.2
  • 34
    • 84898618028 scopus 로고    scopus 로고
    • Contribution of eukaryotic-type serine/threonine kinase to stress response and virulence of Streptococcus suis
    • Zhu, H., J. Zhou, Y. Ni, Z. Yu, A. Mao, Y. Hu, W. Wang, X. Zhang, L. Wen, B. Li, et al. 2014. Contribution of eukaryotic-type serine/threonine kinase to stress response and virulence of Streptococcus suis. PLoS One 9:e91971.
    • (2014) PLoS One , vol.9 , pp. e91971
    • Zhu, H.1    Zhou, J.2    Ni, Y.3    Yu, Z.4    Mao, A.5    Hu, Y.6    Wang, W.7    Zhang, X.8    Wen, L.9    Li, B.10
  • 35
    • 79955585865 scopus 로고    scopus 로고
    • Protein kinase LegK2 is a type IV secretion system effector involved in endoplasmic reticulum recruitment and intracellular replication of Legionella pneumophila
    • Hervet, E., X. Charpentier, A. Vianney, J. C. Lazzaroni, C. Gilbert, D. Atlan, and P. Doublet. 2011. Protein kinase LegK2 is a type IV secretion system effector involved in endoplasmic reticulum recruitment and intracellular replication of Legionella pneumophila. Infect. Immun. 79:1936-1950.
    • (2011) Infect. Immun. , vol.79 , pp. 1936-1950
    • Hervet, E.1    Charpentier, X.2    Vianney, A.3    Lazzaroni, J.C.4    Gilbert, C.5    Atlan, D.6    Doublet, P.7
  • 36
    • 50349093357 scopus 로고    scopus 로고
    • Substrate discrimination among mitogen-activated protein kinases through distinct docking sequence motifs
    • Sheridan, D. L., Y. Kong, S. A. Parker, K. N. Dalby, and B. E. Turk. 2008. Substrate discrimination among mitogen-activated protein kinases through distinct docking sequence motifs. J. Biol. Chem. 283:19511-19520.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19511-19520
    • Sheridan, D.L.1    Kong, Y.2    Parker, S.A.3    Dalby, K.N.4    Turk, B.E.5
  • 37
    • 0035847076 scopus 로고    scopus 로고
    • Selective targeting of MAPKs to the ETS domain transcription factor SAP-1
    • Galanis, A., S. H. Yang, and A. D. Sharrocks. 2001. Selective targeting of MAPKs to the ETS domain transcription factor SAP-1. J. Biol. Chem. 276:965-973.
    • (2001) J. Biol. Chem. , vol.276 , pp. 965-973
    • Galanis, A.1    Yang, S.H.2    Sharrocks, A.D.3
  • 38
    • 71849119627 scopus 로고    scopus 로고
    • The subcellular localization of MEK and ERK-a novel nuclear translocation signal (NTS) paves a way to the nucleus
    • Zehorai, E., Z. Yao, A. Plotnikov, and R. Seger. 2010. The subcellular localization of MEK and ERK-a novel nuclear translocation signal (NTS) paves a way to the nucleus. Mol. Cell. Endocrinol. 314:213-220.
    • (2010) Mol. Cell. Endocrinol. , vol.314 , pp. 213-220
    • Zehorai, E.1    Yao, Z.2    Plotnikov, A.3    Seger, R.4
  • 39
    • 70449106252 scopus 로고    scopus 로고
    • Thioredoxin regulates cell cycle via the ERK1/2-cyclin D1 pathway
    • Mochizuki, M., Y. W. Kwon, J. Yodoi, and H. Masutani. 2009. Thioredoxin regulates cell cycle via the ERK1/2-cyclin D1 pathway. Antioxid. Redox Signal. 11:2957-2971.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2957-2971
    • Mochizuki, M.1    Kwon, Y.W.2    Yodoi, J.3    Masutani, H.4
  • 40
    • 84883623114 scopus 로고    scopus 로고
    • Abrogated thioredoxin system causes increased sensitivity to TNF-a-induced apoptosis via enrichment of p-ERK 1/2 in the nucleus
    • Yoo, M. H., B. A. Carlson, V. N. Gladyshev, and D. L. Hatfield. 2013. Abrogated thioredoxin system causes increased sensitivity to TNF-a-induced apoptosis via enrichment of p-ERK 1/2 in the nucleus. PLoS One 8:e71427.
    • (2013) PLoS One , vol.8 , pp. e71427
    • Yoo, M.H.1    Carlson, B.A.2    Gladyshev, V.N.3    Hatfield, D.L.4
  • 41
    • 84886743358 scopus 로고    scopus 로고
    • Serine phosphorylation of cortactin is required for maximal host cell invasion by Campylobacter jejuni
    • Samuelson, D. R., and M. E. Konkel. 2013. Serine phosphorylation of cortactin is required for maximal host cell invasion by Campylobacter jejuni. Cell Commun. Signal. 11:82.
    • (2013) Cell Commun. Signal. , vol.11 , pp. 82
    • Samuelson, D.R.1    Konkel, M.E.2
  • 43
    • 25444461419 scopus 로고    scopus 로고
    • The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes
    • Kim, D. W., G. Lenzen, A. L. Page, P. Legrain, P. J. Sansonetti, and C. Parsot. 2005. The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes. Proc. Natl. Acad. Sci. USA 102:14046-14051.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14046-14051
    • Kim, D.W.1    Lenzen, G.2    Page, A.L.3    Legrain, P.4    Sansonetti, P.J.5    Parsot, C.6
  • 44
    • 18844364205 scopus 로고    scopus 로고
    • Subcellular localization determines MAP kinase signal output
    • Harding, A., T. Tian, E. Westbury, E. Frische, and J. F. Hancock. 2005. Subcellular localization determines MAP kinase signal output. Curr. Biol. 15:869-873.
    • (2005) Curr. Biol. , vol.15 , pp. 869-873
    • Harding, A.1    Tian, T.2    Westbury, E.3    Frische, E.4    Hancock, J.F.5
  • 45
    • 33644864788 scopus 로고    scopus 로고
    • Compartmentalized Ras/MAPK signaling
    • Mor, A., and M. R. Philips. 2006. Compartmentalized Ras/MAPK signaling. Annu. Rev. Immunol. 24:771-800.
    • (2006) Annu. Rev. Immunol. , vol.24 , pp. 771-800
    • Mor, A.1    Philips, M.R.2
  • 48
    • 84872321691 scopus 로고    scopus 로고
    • Cellular regulation by protein phosphorylation
    • Fischer, E. H. 2013. Cellular regulation by protein phosphorylation. Biochem. Biophys. Res. Commun. 430:865-867.
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 865-867
    • Fischer, E.H.1
  • 49
    • 43049181499 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation of human vacuolar protein sorting 33B
    • Bach, H., K. G. Papavinasasundaram, D. Wong, Z. Hmama, and Y. Av-Gay. 2008. Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation of human vacuolar protein sorting 33B. Cell Host Microbe 3:316-322.
    • (2008) Cell Host Microbe , vol.3 , pp. 316-322
    • Bach, H.1    Papavinasasundaram, K.G.2    Wong, D.3    Hmama, Z.4    Av-Gay, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.