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Volumn 289, Issue 2, 2014, Pages 654-668

Mechanism of bacterial interference with TLR4 signaling by brucella toll/interleukin-1 receptor domain-containing protein TcpB

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DIMERS;

EID: 84891946034     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.523274     Document Type: Article
Times cited : (64)

References (62)
  • 1
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity. Update on Toll-like receptors
    • Kawai, T., and Akira, S. (2010) The role of pattern-recognition receptors in innate immunity. Update on Toll-like receptors. Nat. Immunol. 11, 373-384
    • (2010) Nat. Immunol. , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 2
    • 84866953674 scopus 로고    scopus 로고
    • Adaptors in Toll-like receptor signaling and their potential as therapeutic targets
    • Ve, T., Gay, N. J., Mansell, A., Kobe, B., and Kellie, S. (2012) Adaptors in Toll-like receptor signaling and their potential as therapeutic targets. Curr. Drug Targets 13, 1360-1374
    • (2012) Curr. Drug Targets , vol.13 , pp. 1360-1374
    • Ve, T.1    Gay, N.J.2    Mansell, A.3    Kobe, B.4    Kellie, S.5
  • 5
    • 70350208780 scopus 로고    scopus 로고
    • The evolutionary conundrum of pathogen mimicry
    • Elde, N. C., and Malik, H. S. (2009) The evolutionary conundrum of pathogen mimicry. Nat. Rev. Microbiol. 7, 787-797
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 787-797
    • Elde, N.C.1    Malik, H.S.2
  • 10
    • 65649148280 scopus 로고    scopus 로고
    • Brucella TIR domain-containing protein mimics properties of the toll-like receptor adaptor protein TIRAP
    • Radhakrishnan, G. K., Yu, Q., Harms, J. S., and Splitter, G. A. (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
  • 13
    • 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., Manley, J. L., and Tong, L. (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    Manley, J.L.6    Tong, L.7
  • 15
    • 3843055773 scopus 로고    scopus 로고
    • Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1RAPL
    • Khan, J. A., Brint, E. K., O'Neill, L. A., and Tong, L. (2004) Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1RAPL. J. Biol. Chem. 279, 31664-31670
    • (2004) J. Biol. Chem. , vol.279 , pp. 31664-31670
    • Khan, J.A.1    Brint, E.K.2    O'Neill, L.A.3    Tong, L.4
  • 17
    • 84859227566 scopus 로고    scopus 로고
    • Structural insights into TIR domain specificity of the bridging adaptor Mal in TLR4 signaling
    • Lin, Z., Lu, J., Zhou, W., and Shen, Y. (2012) Structural insights into TIR domain specificity of the bridging adaptor Mal in TLR4 signaling. PLoS One 7, e34202
    • (2012) PLoS One , vol.7
    • Lin, Z.1    Lu, J.2    Zhou, W.3    Shen, Y.4
  • 20
    • 75149175757 scopus 로고    scopus 로고
    • The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants
    • Chan, S. L., Mukasa, T., Santelli, E., Low, L. Y., and Pascual, J. (2010) The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants. Protein Sci. 19, 155-161
    • (2010) Protein Sci. , vol.19 , pp. 155-161
    • Chan, S.L.1    Mukasa, T.2    Santelli, E.3    Low, L.Y.4    Pascual, J.5
  • 21
    • 79952643473 scopus 로고    scopus 로고
    • Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation
    • Bernoux, M., Ve, T., Williams, S., Warren, C., Hatters, D., Valkov, E., Zhang, X., Ellis, J. G., Kobe, B., and Dodds, P. N. (2011) Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation. Cell Host Microbe 9, 200-211
    • (2011) Cell Host Microbe , vol.9 , pp. 200-211
    • Bernoux, M.1    Ve, T.2    Williams, S.3    Warren, C.4    Hatters, D.5    Valkov, E.6    Zhang, X.7    Ellis, J.G.8    Kobe, B.9    Dodds, P.N.10
  • 22
    • 84866072549 scopus 로고    scopus 로고
    • Toll/interleukin-1 receptor domain dimers as the platform for activation and enhanced inhibition of Toll-like receptor signaling
    • Fekonja, O., Bencina, M., and Jerala, R. (2012) Toll/interleukin-1 receptor domain dimers as the platform for activation and enhanced inhibition of Toll-like receptor signaling. J. Biol. Chem. 287, 30993-31002
    • (2012) J. Biol. Chem. , vol.287 , pp. 30993-31002
    • Fekonja, O.1    Bencina, M.2    Jerala, R.3
  • 23
    • 84934441968 scopus 로고    scopus 로고
    • A family of LIC vectors for high-throughput cloning and purification of proteins
    • Eschenfeldt, W. H., Lucy, S., Millard, C. S., Joachimiak, A., and Mark, I. D. (2009) A family of LIC vectors for high-throughput cloning and purification of proteins. Methods Mol. Biol. 498, 105-115
    • (2009) Methods Mol. Biol. , vol.498 , pp. 105-115
    • Eschenfeldt, W.H.1    Lucy, S.2    Millard, C.S.3    Joachimiak, A.4    Mark, I.D.5
  • 24
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier, F. W. (2005) Protein production by auto-induction in high-density shaking cultures. Protein Expr. Purif. 41, 207-234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 25
    • 84885464760 scopus 로고    scopus 로고
    • Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the TIR domain from the Brucella melitensis TIR-domain-containing protein TcpB
    • Alaidarous, M., Ve, T., Ullah, M. O., Valkov, E., Mansell, A., Schembri, M. A., Sweet, M. J., and Kobe, B. (2013) Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the TIR domain from the Brucella melitensis TIR-domain-containing protein TcpB. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69, 1167-1170
    • (2013) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.69 , pp. 1167-1170
    • Alaidarous, M.1    Ve, T.2    Ullah, M.O.3    Valkov, E.4    Mansell, A.5    Schembri, M.A.6    Sweet, M.J.7    Kobe, B.8
  • 32
    • 13244281317 scopus 로고    scopus 로고
    • Coot. Model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot. Model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 36
    • 0033988671 scopus 로고    scopus 로고
    • Size-exclusion chromatographymultiangle laser light scattering analysis of-lactoglobulin and bovine serum albumin in aqueous solution with added salt
    • van Dijk, J. A., and Smit, J. A. (2000) Size-exclusion chromatographymultiangle laser light scattering analysis of-lactoglobulin and bovine serum albumin in aqueous solution with added salt. J. Chromatogr. A 867, 105-112
    • (2000) J. Chromatogr. A , vol.867 , pp. 105-112
    • Van Dijk, J.A.1    Smit, J.A.2
  • 37
    • 4444243454 scopus 로고    scopus 로고
    • Determination of molecular masses of proteins in solution. Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory
    • Folta-Stogniew, E., and Williams, K. R. (1999) Determination of molecular masses of proteins in solution. Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory. J. Biomol. Tech. 10, 51-63
    • (1999) J. Biomol. Tech. , vol.10 , pp. 51-63
    • Folta-Stogniew, E.1    Williams, K.R.2
  • 38
    • 33645214738 scopus 로고    scopus 로고
    • ATSAS, p 2.1, a program package for small-angle scattering data analysis
    • Konarev, P. V., Petoukhov, M. V., Volkov, V. V., and Svergun, D. I. (2006) ATSAS, p 2.1, a program package for small-angle scattering data analysis. J. Appl. Crystallogr. 39, 277-286
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 277-286
    • Konarev, P.V.1    Petoukhov, M.V.2    Volkov, V.V.3    Svergun, D.I.4
  • 41
    • 75649147383 scopus 로고    scopus 로고
    • Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale
    • Fischer, H., De Oliveira Neto, M., Napolitano, H. B., Polikarpov, I., and Craievich, A. F. (2009) Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale. J. Appl. Crystallogr. 43, 101-109
    • (2009) J. Appl. Crystallogr. , vol.43 , pp. 101-109
    • Fischer, H.1    De Oliveira Neto, M.2    Napolitano, H.B.3    Polikarpov, I.4    Craievich, A.F.5
  • 42
    • 0029185933 scopus 로고
    • CRYSOL. A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C., and Koch, M. H. (1995) CRYSOL. A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 43
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid abinitio shape determination in small-angle scattering
    • Svergun, D. I., and Franke, D. (2009) DAMMIF, a program for rapid abinitio shape determination in small-angle scattering. J. Appl. Crystallogr. 42, 342-346
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Svergun, D.I.1    Franke, D.2
  • 44
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab-intio shape determination in small-angle acattering
    • Valkov, V. V., and Svergun, D. I. (2003) Uniqueness of ab-intio shape determination in small-angle acattering. J. Appl. Crystallogr. 36, 860-864
    • (2003) J. Appl. Crystallogr , vol.36 , pp. 860-864
    • Valkov, V.V.1    Svergun, D.I.2
  • 45
    • 77954288774 scopus 로고    scopus 로고
    • Dali server. Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server. Conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 46
    • 16744364738 scopus 로고    scopus 로고
    • Structural complementarity of Toll/interleukin-1 receptor domains in Toll-like receptors and the adaptors Mal and MyD88
    • Dunne, A., Ejdeback, M., Ludidi, P. L., O'Neill, L. A., and Gay, N. J. (2003) Structural complementarity of Toll/interleukin-1 receptor domains in Toll-like receptors and the adaptors Mal and MyD88. J. Biol. Chem. 278, 41443-41451
    • (2003) J. Biol. Chem. , vol.278 , pp. 41443-41451
    • Dunne, A.1    Ejdeback, M.2    Ludidi, P.L.3    O'Neill, L.A.4    Gay, N.J.5
  • 47
    • 84883438662 scopus 로고    scopus 로고
    • Crystal structure of vaccinia viral A27 protein reveals a novel structure critical for its function and complex formation with A26 protein
    • Chang, T. H., Chang, S. J., Hsieh, F. L., Ko, T. P., Lin, C. T., Ho, M. R., Wang, I., Hsu, S. T., Guo, R. T., Chang, W., and Wang, A. H. (2013) Crystal structure of vaccinia viral A27 protein reveals a novel structure critical for its function and complex formation with A26 protein. PLoS Pathog. 9, e1003563
    • (2013) PLoS Pathog. , vol.9
    • Chang, T.H.1    Chang, S.J.2    Hsieh, F.L.3    Ko, T.P.4    Lin, C.T.5    Ho, M.R.6    Wang, I.7    Hsu, S.T.8    Guo, R.T.9    Chang, W.10    Wang, A.H.11
  • 48
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 49
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web. A case study using the Phyre server
    • Kelley, L. A., and Sternberg, M. J. (2009) Protein structure prediction on the Web. A case study using the Phyre server. Nat. Protoc. 4, 363-371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 50
    • 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, R. M., Salunkhe, P., Godzik, A., and Reed, J. C. (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
  • 51
    • 77955558396 scopus 로고    scopus 로고
    • Microbial Toll/interleukin 1 receptor proteins. A new class of virulence factors
    • Cirl, C., and Miethke, T. (2010) Microbial Toll/interleukin 1 receptor proteins. A new class of virulence factors. Int. J. Med. Microbiol. 300, 396-401
    • (2010) Int. J. Med. Microbiol. , vol.300 , pp. 396-401
    • Cirl, C.1    Miethke, T.2
  • 52
    • 33947356714 scopus 로고    scopus 로고
    • Characterization of a TIR-like protein from Paracoccus denitrificans
    • Low, L. Y., Mukasa, T., Reed, J. C., and 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
  • 53
    • 84871869646 scopus 로고    scopus 로고
    • PTEN regulates TLR5-induced intestinal inflammation by controlling Mal/TIRAP recruitment
    • Choi, Y. J., Jung, J., Chung, H. K., Im, E., and Rhee, S. H. (2013) PTEN regulates TLR5-induced intestinal inflammation by controlling Mal/TIRAP recruitment. FASEB J. 27, 243-254
    • (2013) FASEB J. , vol.27 , pp. 243-254
    • Choi, Y.J.1    Jung, J.2    Chung, H.K.3    Im, E.4    Rhee, S.H.5
  • 56
    • 84886301386 scopus 로고    scopus 로고
    • Structure of the Toll/interleukin 1 receptor (TIR) domain of the immunosuppressive Brucella effector BtpA/Btp1/TcpB
    • Kaplan-Türköz, B., Koelblen, T., Felix, C., Candusso, M. P., O'Callaghan, D., Vergunst, A. C., and Terradot, L. (2013) Structure of the Toll/interleukin 1 receptor (TIR) domain of the immunosuppressive Brucella effector BtpA/Btp1/TcpB. FEBS Lett. 587, 3412-3416
    • (2013) FEBS Lett. , vol.587 , pp. 3412-3416
    • Kaplan-Türköz, B.1    Koelblen, T.2    Felix, C.3    Candusso, M.P.4    O'Callaghan, D.5    Vergunst, A.C.6    Terradot, L.7
  • 58
    • 0030694108 scopus 로고    scopus 로고
    • Pillars article. IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling
    • Muzio, M., Ni, J., Feng, P., and Dixit, V. M. (1997) Pillars article. IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. Science 278, 1612-1615
    • (1997) Science , vol.278 , pp. 1612-1615
    • Muzio, M.1    Ni, J.2    Feng, P.3    Dixit, V.M.4
  • 61
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE. Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004) MUSCLE. Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 62
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript. Extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet, P., Robert, X., and Courcelle, E. (2003) ESPript/ENDscript. Extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res. 31, 3320-3323
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3


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