메뉴 건너뛰기




Volumn 9, Issue 11, 2014, Pages

A TIR domain protein from e. faecalis attenuates myD88-Mediated signaling and nf-kb activation

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1 RECEPTOR; LIPOTEICHOIC ACID; MYELOID DIFFERENTIATION FACTOR 88; BACTERIAL PROTEIN; LIPOPOLYSACCHARIDE; MYD88 PROTEIN, MOUSE; TEICHOIC ACID;

EID: 84943316852     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0112010     Document Type: Article
Times cited : (24)

References (51)
  • 1
    • 67650744795 scopus 로고    scopus 로고
    • The ecology, Epidemiology and virulence of enterococcus
    • Fisher K, Phillips C (2009) The ecology, epidemiology and virulence of Enterococcus. Microbiology 155: 1749-1757.
    • (2009) Microbiology , vol.155 , pp. 1749-1757
    • Fisher, K.1    Phillips, C.2
  • 2
    • 54949148412 scopus 로고    scopus 로고
    • Nhsn annual update: Antimicrobial-resistant pathogens associated with healthcareassociated infections: Annual summary of data reported to the national healthcare safety network at the centers for disease control and prevention, 2006-2007
    • Hidron AI, Edwards JR, Patel J, Horan TC, Sievert DM, et al. (2008) NHSN annual update: Antimicrobial-resistant pathogens associated with healthcareassociated infections: Annual summary of data reported to the National Healthcare Safety Network at the Centers for Disease Control and Prevention, 2006-2007. Infect Control Hosp Epidemiol 29: 996-1011.
    • (2008) Infect Control Hosp Epidemiol , vol.29 , pp. 996-1011
    • Hidron, A.I.1    Edwards, J.R.2    Patel, J.3    Horan, T.C.4    Sievert, D.M.5
  • 3
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S, Uematsu S, Takeuchi O (2006) Pathogen recognition and innate immunity. Cell 124: 783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 4
    • 33748090945 scopus 로고    scopus 로고
    • Toll-like receptors as molecular switches
    • Gay NJ, Gangloff M, Weber AN (2006) Toll-like receptors as molecular switches. Nat Rev Immunol 6: 693-698.
    • (2006) Nat Rev Immunol , vol.6 , pp. 693-698
    • Gay, N.J.1    Gangloff, M.2    Weber, A.N.3
  • 5
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR-domain-containing adaptors in toll-like receptor signalling
    • O'Neill LA, Bowie AG (2007) The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. Nat Rev Immunol 7: 353-364.
    • (2007) Nat Rev Immunol , vol.7 , pp. 353-364
    • O'Neill, L.A.1    Bowie, A.G.2
  • 6
    • 5444262511 scopus 로고    scopus 로고
    • Toll-like receptor control of the adaptive immune responses
    • Iwasaki A, Medzhitov R (2004) Toll-like receptor control of the adaptive immune responses. Nat Immunol 5: 987-995.
    • (2004) Nat Immunol , vol.5 , pp. 987-995
    • Iwasaki, A.1    Medzhitov, R.2
  • 7
    • 61849170035 scopus 로고    scopus 로고
    • TLRS and innate immunity
    • Beutler BA (2009) TLRs and innate immunity. Blood 113: 1399-1407.
    • (2009) Blood , vol.113 , pp. 1399-1407
    • Beutler, B.A.1
  • 8
    • 5444234216 scopus 로고    scopus 로고
    • The interface between innate and adaptive immunity
    • Hoebe K, Janssen E, Beutler B (2004) The interface between innate and adaptive immunity. Nat Immunol 5: 971-974.
    • (2004) Nat Immunol , vol.5 , pp. 971-974
    • Hoebe, K.1    Janssen, E.2    Beutler, B.3
  • 9
    • 0036851306 scopus 로고    scopus 로고
    • Bacterial strategies for overcoming host innate and adaptive immune responses
    • Hornef MW, Wick MJ, Rhen M, Normark S (2002) Bacterial strategies for overcoming host innate and adaptive immune responses. Nat Immunol 3: 1033-1040.
    • (2002) Nat Immunol , vol.3 , pp. 1033-1040
    • Hornef, M.W.1    Wick, M.J.2    Rhen, M.3    Normark, S.4
  • 10
    • 0035432063 scopus 로고    scopus 로고
    • Pathogenic trickery: Deception of host cell processes
    • Knodler LA, Celli J, Finlay BB (2001) Pathogenic trickery: deception of host cell processes. Nat Rev Mol Cell Biol 2: 578-588.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 578-588
    • Knodler, L.A.1    Celli, J.2    Finlay, B.B.3
  • 11
    • 0038557053 scopus 로고    scopus 로고
    • Phagocyte sabotage: Disruption of macrophage signalling by bacterial pathogens
    • Rosenberger CM, Finlay BB (2003) Phagocyte sabotage: disruption of macrophage signalling by bacterial pathogens. Nat Rev Mol Cell Biol 4: 385-396.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 385-396
    • Rosenberger, C.M.1    Finlay, B.B.2
  • 12
    • 0035899360 scopus 로고    scopus 로고
    • Structural mimicry in bacterial virulence
    • Stebbins CE, Galan JE (2001) Structural mimicry in bacterial virulence. Nature 412: 701-705.
    • (2001) Nature , vol.412 , pp. 701-705
    • Stebbins, C.E.1    Galan, J.E.2
  • 13
    • 0036081269 scopus 로고    scopus 로고
    • Host-pathogen interactions: Subversion and utilization of the NF-kappa b pathway during infection
    • Tato CM, Hunter CA (2002) Host-pathogen interactions: subversion and utilization of the NF-kappa B pathway during infection. Infect Immun 70: 3311- 3317.
    • (2002) Infect Immun , vol.70 , pp. 3311-3317
    • Tato, C.M.1    Hunter, C.A.2
  • 14
    • 29644438009 scopus 로고    scopus 로고
    • Identification and characterization of a novel bacterial virulence factor that shares homology with mammalian toll/interleukin-1 receptor family proteins
    • Newman RM, Salunkhe P, Godzik A, Reed JC (2006) Identification and characterization of a novel bacterial virulence factor that shares homology with mammalian Toll/interleukin-1 receptor family proteins. Infect Immun 74: 594- 601.
    • (2006) Infect Immun , vol.74 , pp. 594-601
    • Newman, R.M.1    Salunkhe, P.2    Godzik, A.3    Reed, J.C.4
  • 15
    • 41849102701 scopus 로고    scopus 로고
    • Subversion of toll-like receptor signaling by a unique family of bacterial toll/interleukin-1 receptor domain-containing proteins
    • Cirl C, Wieser A, Yadav M, Duerr S, Schubert S, et al. (2008) Subversion of Toll-like receptor signaling by a unique family of bacterial Toll/interleukin-1 receptor domain-containing proteins. Nat Med 14: 399-406.
    • (2008) Nat Med , vol.14 , pp. 399-406
    • Cirl, C.1    Wieser, A.2    Yadav, M.3    Duerr, S.4    Schubert, S.5
  • 16
    • 40349103656 scopus 로고    scopus 로고
    • Brucella control of dendritic cell maturation is dependent on the TIR-containing protein BTP1
    • Salcedo SP, Marchesini MI, Lelouard H, Fugier E, Jolly G, et al. (2008) Brucella control of dendritic cell maturation is dependent on the TIR-containing protein BTP1. Plos Pathog 4: e21.
    • (2008) Plos Pathog , vol.4 , pp. e21
    • Salcedo, S.P.1    Marchesini, M.I.2    Lelouard, H.3    Fugier, E.4    Jolly, G.5
  • 17
    • 33947356714 scopus 로고    scopus 로고
    • Characterization of a TIR-like protein from paracoccus denitrificans
    • Low LY, Mukasa T, Reed JC, Pascual J (2007) Characterization of a TIR-like protein from Paracoccus denitrificans. Biochem Biophys Res Commun 356: 481-486.
    • (2007) Biochem Biophys Res Commun , vol.356 , pp. 481-486
    • Low, L.Y.1    Mukasa, T.2    Reed, J.C.3    Pascual, J.4
  • 18
    • 84902821133 scopus 로고    scopus 로고
    • A staphylococcus aureus TIR domain protein virulence factor blocks TLR2- mediated NF-kappab signaling
    • Askarian F, van Sorge NM, Sangvik M, Beasley FC, Henriksen JR, et al. (2014) A Staphylococcus aureus TIR domain protein virulence factor blocks TLR2- mediated NF-kappaB signaling. J Innate Immun 6: 485-498.
    • (2014) J Innate Immun , vol.6 , pp. 485-498
    • Askarian, F.1    Van Sorge, N.M.2    Sangvik, M.3    Beasley, F.C.4    Henriksen, J.R.5
  • 19
    • 65649148280 scopus 로고    scopus 로고
    • Brucella TIR domain-containing protein mimics properties of the toll-like receptor adaptor protein TIRsAP
    • Radhakrishnan GK, Yu Q, Harms JS, Splitter GA (2009) Brucella TIR Domain-containing Protein Mimics Properties of the Toll-like Receptor Adaptor Protein TIRAP. J Biol Chem 284: 9892-9898.
    • (2009) J Biol Chem , vol.284 , pp. 9892-9898
    • Radhakrishnan, G.K.1    Yu, Q.2    Harms, J.S.3    Splitter, G.A.4
  • 20
    • 0034623005 scopus 로고    scopus 로고
    • T-coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J (2000) T-Coffee: A novel method for fast and accurate multiple sequence alignment. J Mol Biol 302: 205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 21
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • Bates PA, Kelley LA, MacCallum RM, Sternberg MJ (2001) Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins Suppl5: 39-46.
    • (2001) Proteins , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.4
  • 23
    • 77953622695 scopus 로고    scopus 로고
    • Biochemical and functional analysis of TIR domain containing protein from brucella melitensis
    • Radhakrishnan GK, Splitter GA (2010) Biochemical and functional analysis of TIR domain containing protein from Brucella melitensis. Biochem Biophys Res Commun 397: 59-63.
    • (2010) Biochem Biophys Res Commun , vol.397 , pp. 59-63
    • Radhakrishnan, G.K.1    Splitter, G.A.2
  • 24
    • 70350434311 scopus 로고    scopus 로고
    • Capsular polysaccharide production in enterococcus faecalis and contribution of CPSF to capsule serospecificity
    • Thurlow LR, Thomas VC, Hancock LE (2009) Capsular polysaccharide production in Enterococcus faecalis and contribution of CPSF to capsule serospecificity. J Bacteriol 191: 6203-6210.
    • (2009) J Bacteriol , vol.191 , pp. 6203-6210
    • Thurlow, L.R.1    Thomas, V.C.2    Hancock, L.E.3
  • 25
    • 84862702935 scopus 로고    scopus 로고
    • Biofilm and planktonic enterococcus faecalis elicit different responses from host phagocytes in vitro
    • Daw K, Baghdayan AS, Awasthi S, Shankar N (2012) Biofilm and planktonic Enterococcus faecalis elicit different responses from host phagocytes in vitro. FEMS Immunol Med Microbiol 65: 270-282.
    • (2012) FEMS Immunol Med Microbiol , vol.65 , pp. 270-282
    • Daw, K.1    Baghdayan, A.S.2    Awasthi, S.3    Shankar, N.4
  • 26
    • 57349112300 scopus 로고    scopus 로고
    • An arac-type transcriptional regulator encoded on the enterococcus faecalis pathogenicity island contributes to pathogenesis and intracellular macrophage survival
    • Coburn PS, Baghdayan AS, Dolan GT, Shankar N (2008) An Arac-type transcriptional regulator encoded on the Enterococcus faecalis pathogenicity island contributes to pathogenesis and intracellular macrophage survival. Infect Immun 76: 5668-5676.
    • (2008) Infect Immun , vol.76 , pp. 5668-5676
    • Coburn, P.S.1    Baghdayan, A.S.2    Dolan, G.T.3    Shankar, N.4
  • 27
    • 0033849733 scopus 로고    scopus 로고
    • Aggregation substance promotes adherence, phagocytosis, and intracellular survival of enterococcus faecalis within human macrophages and suppresses respiratory burst
    • Sussmuth SD, Muscholl-Silberhorn A, Wirth R, Susa M, Marre R, et al. (2000) Aggregation substance promotes adherence, phagocytosis, and intracellular survival of Enterococcus faecalis within human macrophages and suppresses respiratory burst. Infect Immun 68: 4900-4906.
    • (2000) Infect Immun , vol.68 , pp. 4900-4906
    • Sussmuth, S.D.1    Muscholl-Silberhorn, A.2    Wirth, R.3    Susa, M.4    Marre, R.5
  • 28
    • 84864822573 scopus 로고    scopus 로고
    • The spx regulator modulates stress responses and virulence in enterococcus faecalis
    • Kajfasz JK, Mendoza JE, Gaca AO, Miller JH, Koselny KA, et al. (2012) The Spx regulator modulates stress responses and virulence in Enterococcus faecalis. Infect Immun 80: 2265-2275.
    • (2012) Infect Immun , vol.80 , pp. 2265-2275
    • Kajfasz, J.K.1    Mendoza, J.E.2    Gaca, A.O.3    Miller, J.H.4    Koselny, K.A.5
  • 29
    • 79956344015 scopus 로고    scopus 로고
    • Study of histopathological and molecular changes of rat kidney under simulated weightlessness and resistance training protective effect
    • Ding Y, Zou J, Li Z, Tian J, Abdelalim S, et al. (2011) Study of histopathological and molecular changes of rat kidney under simulated weightlessness and resistance training protective effect. PLoS One 6: e20008.
    • (2011) PLoS One , vol.6 , pp. e20008
    • Ding, Y.1    Zou, J.2    Li, Z.3    Tian, J.4    Abdelalim, S.5
  • 30
    • 0037470983 scopus 로고    scopus 로고
    • Role of mobile DNA in the evolution of vancomycin-resistant enterococcus faecalis
    • Paulsen IT, Banerjei L, Myers GS, Nelson KE, Seshadri R, et al. (2003) Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science 299: 2071-2074.
    • (2003) Science , vol.299 , pp. 2071-2074
    • Paulsen, I.T.1    Banerjei, L.2    Myers, G.S.3    Nelson, K.E.4    Seshadri, R.5
  • 32
    • 34548459895 scopus 로고    scopus 로고
    • Structure, function and regulation of the TOLL/IL-1 receptor adaptor proteins
    • Watters TM, Kenny EF, O'Neill LA (2007) Structure, function and regulation of the Toll/IL-1 receptor adaptor proteins. Immunol Cell Biol 85: 411-419.
    • (2007) Immunol Cell Biol , vol.85 , pp. 411-419
    • Watters, T.M.1    Kenny, E.F.2    O'Neill, L.A.3
  • 33
    • 84876578144 scopus 로고    scopus 로고
    • New functional families (funfams) in cath to improve the mapping of conserved functional sites to 3d structures
    • Sillitoe I, Cuff AL, Dessailly BH, Dawson NL, Furnham N, et al. (2013) New functional families (FunFams) in CATH to improve the mapping of conserved functional sites to 3D structures. Nucleic Acids Res 41: D490-D498.
    • (2013) Nucleic Acids Res , vol.41 , pp. D490-D498
    • Sillitoe, I.1    Cuff, A.L.2    Dessailly, B.H.3    Dawson, N.L.4    Furnham, N.5
  • 36
    • 33749574498 scopus 로고    scopus 로고
    • Structural and functional evidence for the role of the TLR2 DD loop in TLR1/TLR2 heterodimerization and signaling
    • Gautam JK, Ashish, Comeau LD, Krueger JK, Smith MF Jr (2006) Structural and functional evidence for the role of the TLR2 DD loop in TLR1/TLR2 heterodimerization and signaling. J Biol Chem 281: 30132-30142.
    • (2006) J Biol Chem , vol.281 , pp. 30132-30142
    • Gautam, J.K.1    Ashish2    Comeau, L.D.3    Krueger, J.K.4    Smith, M.F.5
  • 37
    • 84861899161 scopus 로고    scopus 로고
    • A toll/interleukin (il)-1 receptor domain protein from yersinia pestis interacts with mammalian il-1/toll-like receptor pathways but does not play a central role in the virulence of y. Pestis in a mouse model of bubonic plague
    • Spear AM, Rana RR, Jenner DC, Flick-Smith HC, Oyston PC, et al. (2012) A Toll/interleukin (IL)-1 receptor domain protein from Yersinia pestis interacts with mammalian IL-1/Toll-like receptor pathways but does not play a central role in the virulence of Y. pestis in a mouse model of bubonic plague. Microbiology 158: 1593-1606.
    • (2012) Microbiology , vol.158 , pp. 1593-1606
    • Spear, A.M.1    Rana, R.R.2    Jenner, D.C.3    Flick-Smith, H.C.4    Oyston, P.C.5
  • 38
    • 0347567036 scopus 로고    scopus 로고
    • Soluble expression of a functionally active plasmodium falciparum falcipain-2 fused to maltose-binding protein in Escherichia coli
    • Goh LL, Loke P, Singh M, Sim TS (2003) Soluble expression of a functionally active Plasmodium falciparum falcipain-2 fused to maltose-binding protein in Escherichia coli. Protein Expr Purif 32: 194-201.
    • (2003) Protein Expr Purif , vol.32 , pp. 194-201
    • Goh, L.L.1    Loke, P.2    Singh, M.3    Sim, T.S.4
  • 40
    • 0034597766 scopus 로고    scopus 로고
    • Structural basis for signal transduction by the toll/interleukin-1 receptor domains
    • Xu Y, Tao X, Shen B, Horng T, Medzhitov R, et al. (2000) Structural basis for signal transduction by the Toll/interleukin-1 receptor domains. Nature 408: 111-115.
    • (2000) Nature , vol.408 , pp. 111-115
    • Xu, Y.1    Tao, X.2    Shen, B.3    Horng, T.4    Medzhitov, R.5
  • 41
    • 79951943072 scopus 로고    scopus 로고
    • TIR domain-containing adaptor SARM is a late addition to the ongoing microbe-host dialog
    • Zhang Q, Zmasek CM, Cai X, Godzik A (2011) TIR domain-containing adaptor SARM is a late addition to the ongoing microbe-host dialog. Dev Comp Immunol 35: 461-468.
    • (2011) Dev Comp Immunol , vol.35 , pp. 461-468
    • Zhang, Q.1    Zmasek, C.M.2    Cai, X.3    Godzik, A.4
  • 42
    • 68849085894 scopus 로고    scopus 로고
    • A cell biological view of toll-like receptor function: Regulation through compartmentalization
    • Barton GM, Kagan JC (2009) A cell biological view of Toll-like receptor function: regulation through compartmentalization. Nat Rev Immunol 9: 535-542.
    • (2009) Nat Rev Immunol , vol.9 , pp. 535-542
    • Barton, G.M.1    Kagan, J.C.2
  • 43
    • 33646908228 scopus 로고    scopus 로고
    • Phosphoinositide-mediated adaptor recruitment controls toll-like receptor signaling
    • Kagan JC, Medzhitov R (2006) Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling. Cell 125: 943-955.
    • (2006) Cell , vol.125 , pp. 943-955
    • Kagan, J.C.1    Medzhitov, R.2
  • 45
    • 0035019794 scopus 로고    scopus 로고
    • Oxygen-dependent anti-salmonella activity of macrophages
    • Vazquez-Torres A, Fang FC (2001) Oxygen-dependent anti-Salmonella activity of macrophages. Trends Microbiol 9: 29-33.
    • (2001) Trends Microbiol , vol.9 , pp. 29-33
    • Vazquez-Torres, A.1    Fang, F.C.2
  • 46
    • 0035057454 scopus 로고    scopus 로고
    • Diverse virulence traits underlying different clinical outcomes of salmonella infection
    • Fierer J, Guiney DG (2001) Diverse virulence traits underlying different clinical outcomes of Salmonella infection. J Clin Invest 107: 775-780.
    • (2001) J Clin Invest , vol.107 , pp. 775-780
    • Fierer, J.1    Guiney, D.G.2
  • 47
    • 0025334517 scopus 로고
    • A pair of mobilizable shuttle vectors conferring resistance to spectinomycin for molecular cloning in Escherichia coli and in gram-positive bacteria
    • Trieu-Cuot P, Carlier C, Poyart-Salmeron C, Courvalin P (1990) A pair of mobilizable shuttle vectors conferring resistance to spectinomycin for molecular cloning in Escherichia coli and in gram-positive bacteria. Nucleic Acids Res 18: 4296.
    • (1990) Nucleic Acids Res , vol.18 , pp. 4296
    • Trieu-Cuot, P.1    Carlier, C.2    Poyart-Salmeron, C.3    Courvalin, P.4
  • 49
    • 0024215242 scopus 로고
    • An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein
    • Maina CV, Riggs PD, Grandea AG, Slatko BE, Moran LS, et al. (1988) An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from Maltose-Binding Protein. Gene 74: 365-373.
    • (1988) Gene , vol.74 , pp. 365-373
    • Maina, C.V.1    Riggs, P.D.2    Grandea, A.G.3    Slatko, B.E.4    Moran, L.S.5
  • 50
    • 0037725380 scopus 로고    scopus 로고
    • Construction of the mobilizable plasmid PMV158GFP, a derivative of pmv158 that carries the gene encoding the green fluorescent protein
    • Nieto C, Espinosa M (2003) Construction of the mobilizable plasmid PMV158GFP, a derivative of pMV158 that carries the gene encoding the green fluorescent protein. Plasmid 49: 281-285.
    • (2003) Plasmid , vol.49 , pp. 281-285
    • Nieto, C.1    Espinosa, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.