메뉴 건너뛰기




Volumn 1, Issue 8, 2010, Pages

The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ANTIGEN; STAPHYLOCOCCAL ENTEROTOXIN H; STAPHYLOCOCCUS ENTEROTOXIN; SUPERANTIGEN; T LYMPHOCYTE RECEPTOR; TERNARY COMPLEX FACTOR; UNCLASSIFIED DRUG;

EID: 78650074574     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms1117     Document Type: Article
Times cited : (50)

References (45)
  • 1
    • 70450178469 scopus 로고    scopus 로고
    • Staphylococcus aureus: The toxic presence of a pathogen extraordinaire
    • Larkin, E. A., Carman, R. J., Krakauer, T. & Stiles, B. G. Staphylococcus aureus: The toxic presence of a pathogen extraordinaire. Curr. Med. Chem. 16, 4003-4019 (2009).
    • (2009) Curr. Med. Chem. , vol.16 , pp. 4003-4019
    • Larkin, E.A.1    Carman, R.J.2    Krakauer, T.3    Stiles, B.G.4
  • 2
    • 0025367679 scopus 로고
    • The staphylococcal enterotoxins and their relatives
    • Marrack, P. & Kappler, J. The staphylococcal enterotoxins and their relatives. Science 248, 705-711 (1990).
    • (1990) Science , vol.248 , pp. 705-711
    • Marrack, P.1    Kappler, J.2
  • 3
    • 1842633622 scopus 로고    scopus 로고
    • Interplay between superantigens and immunoreceptors
    • Petersson, K., Forsberg, G. & Walse, B. Interplay between superantigens and immunoreceptors. Scand. J. Immunol. 59, 345-355 (2004).
    • (2004) Scand. J. Immunol. , vol.59 , pp. 345-355
    • Petersson, K.1    Forsberg, G.2    Walse, B.3
  • 5
    • 33847723413 scopus 로고    scopus 로고
    • Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens
    • Brouillard, J. N. et al. Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens. J. Mol. Biol. 367, 925-934 (2007).
    • (2007) J. Mol. Biol. , vol.367 , pp. 925-934
    • Brouillard, J.N.1
  • 6
    • 0035796399 scopus 로고    scopus 로고
    • Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence
    • Petersson, K. et al. Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence. EMBO. J. 20, 3306-3312 (2001).
    • (2001) EMBO. J. , vol.20 , pp. 3306-3312
    • Petersson, K.1
  • 7
    • 0029985104 scopus 로고    scopus 로고
    • Crystal structure of a T-cell receptor beta-chain complexed with a superantigen
    • Fields, B. A. et al. Crystal structure of a T-cell receptor beta-chain complexed with a superantigen. Nature 384, 188-192 (1996).
    • (1996) Nature , vol.384 , pp. 188-192
    • Fields, B.A.1
  • 9
    • 0032412391 scopus 로고    scopus 로고
    • Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B
    • Li, H. et al. Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B. Immunity 9, 807-816 (1998).
    • (1998) Immunity , vol.9 , pp. 807-816
    • Li, H.1
  • 10
    • 33847209552 scopus 로고    scopus 로고
    • Structural basis of T-cell specificity and activation by the bacterial superantigen TSST-1
    • Moza, B. et al. Structural basis of T-cell specificity and activation by the bacterial superantigen TSST-1. EMBO. J. 26, 1187-1197 (2007).
    • (2007) EMBO. J. , vol.26 , pp. 1187-1197
    • Moza, B.1
  • 11
    • 0036091233 scopus 로고    scopus 로고
    • Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes
    • Sundberg, E. J. et al. Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes. Structure (Camb) 10, 687-699 (2002).
    • (2002) Structure (Camb) , vol.10 , pp. 687-699
    • Sundberg, E.J.1
  • 12
    • 0142215405 scopus 로고    scopus 로고
    • Stable, soluble T-cell receptor molecules for crystallization and therapeutics
    • Boulter, J. M. et al. Stable, soluble T-cell receptor molecules for crystallization and therapeutics. Protein Eng. 16, 707-711 (2003).
    • (2003) Protein Eng. , vol.16 , pp. 707-711
    • Boulter, J.M.1
  • 13
    • 0033084056 scopus 로고    scopus 로고
    • Empty and peptide-loaded class II major histocompatibility complex proteins produced by expression in Escherichia coli and folding in vitro
    • Frayser, M., Sato, A. K., Xu, L. & Stern, L. J. Empty and peptide-loaded class II major histocompatibility complex proteins produced by expression in Escherichia coli and folding in vitro. Protein Expr. Purif. 15, 105-114 (1999).
    • (1999) Protein Expr. Purif. , vol.15 , pp. 105-114
    • Frayser, M.1    Sato, A.K.2    Xu, L.3    Stern, L.J.4
  • 14
    • 21444445173 scopus 로고    scopus 로고
    • Directed evolution of human T-cell receptors with picomolar affinities by phage display
    • Li, Y. et al. Directed evolution of human T-cell receptors with picomolar affinities by phage display. Nat. Biotechnol. 23, 349-354 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , pp. 349-354
    • Li, Y.1
  • 15
    • 0344718622 scopus 로고    scopus 로고
    • Staphylococcal enterotoxin H displays unique MHC class II-binding properties
    • Nilsson, H., Bjork, P., Dohlsten, M. & Antonsson, P. Staphylococcal enterotoxin H displays unique MHC class II-binding properties. J. Immunol. 163, 6686-6693 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 6686-6693
    • Nilsson, H.1    Bjork, P.2    Dohlsten, M.3    Antonsson, P.4
  • 16
    • 0034703273 scopus 로고    scopus 로고
    • The crystal structure of staphylococcal enterotoxin H: Implications for binding properties to MHC class II and TcR molecules
    • Hakansson, M. et al. The crystal structure of staphylococcal enterotoxin H: Implications for binding properties to MHC class II and TcR molecules. J. Mol. Biol. 302, 527-537 (2000).
    • (2000) J. Mol. Biol. , vol.302 , pp. 527-537
    • Hakansson, M.1
  • 17
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
    • Stern, L. J. et al. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 368, 215-221 (1994).
    • (1994) Nature , vol.368 , pp. 215-221
    • Stern, L.J.1
  • 19
    • 33748749713 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal enterotoxin I (SEI) in complex with a human major histocompatibility complex class II molecule
    • Fernandez, M. M., Guan, R., Swaminathan, C. P., Malchiodi, E. L. & Mariuzza, R. A. Crystal structure of staphylococcal enterotoxin I (SEI) in complex with a human major histocompatibility complex class II molecule. J. Biol. Chem. 281, 25356-25364 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 25356-25364
    • Fernandez, M.M.1    Guan, R.2    Swaminathan, C.P.3    Malchiodi, E.L.4    Mariuzza, R.A.5
  • 21
    • 0024309955 scopus 로고
    • V beta-specific stimulation of human T cells by staphylococcal toxins
    • Kappler, J. et al. V beta-specific stimulation of human T cells by staphylococcal toxins. Science 244, 811-813 (1989).
    • (1989) Science , vol.244 , pp. 811-813
    • Kappler, J.1
  • 22
    • 52049123299 scopus 로고    scopus 로고
    • The bacterial superantigen and superantigen-like proteins
    • Fraser, J. D. & Proft, T. The bacterial superantigen and superantigen-like proteins. Immunol. Rev. 225, 226-243 (2008).
    • (2008) Immunol. Rev. , vol.225 , pp. 226-243
    • Fraser, J.D.1    Proft, T.2
  • 23
    • 0037446529 scopus 로고    scopus 로고
    • Staphylococcal enterotoxin h induces valpha-specific expansion of T cells
    • Petersson, K., Pettersson, H., Skartved, N. J., Walse, B. & Forsberg, G. Staphylococcal enterotoxin h induces valpha-specific expansion of T cells. J. Immunol. 170, 4148-4154 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 4148-4154
    • Petersson, K.1    Pettersson, H.2    Skartved, N.J.3    Walse, B.4    Forsberg, G.5
  • 24
    • 38449085891 scopus 로고    scopus 로고
    • Cutting edge: Evidence of direct TCR alpha-chain interaction with superantigen
    • Pumphrey, N. et al. Cutting edge: Evidence of direct TCR alpha-chain interaction with superantigen. J. Immunol. 179, 2700-2704 (2007).
    • (2007) J. Immunol. , vol.179 , pp. 2700-2704
    • Pumphrey, N.1
  • 25
    • 33846977011 scopus 로고    scopus 로고
    • Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC
    • Wang, L. et al. Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC. Nat. Struct. Mol. Biol. 14, 169-171 (2007).
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 169-171
    • Wang, L.1
  • 26
    • 52049123299 scopus 로고    scopus 로고
    • The bacterial superantigen and superantigen-like proteins
    • Fraser, J. D. & Proft, T. The bacterial superantigen and superantigen-like proteins. Immunol. Rev. 225, 226-243 (2008).
    • (2008) Immunol. Rev. , vol.225 , pp. 226-243
    • Fraser, J.D.1    Proft, T.2
  • 27
    • 0031030791 scopus 로고    scopus 로고
    • V alpha domain modulates the multiple topologies of mouse T cell receptor V beta20/staphylococcal enterotoxins A and E complexes
    • Bravo de Alba, Y. et al. V alpha domain modulates the multiple topologies of mouse T cell receptor V beta20/staphylococcal enterotoxins A and E complexes. Eur. J. Immunol. 27, 92-99 (1997).
    • (1997) Eur. J. Immunol. , vol.27 , pp. 92-99
    • Bravo De Alba, Y.1
  • 28
    • 0028363831 scopus 로고
    • Binary and ternary complexes between T-cell receptor, class II MHC and superantigen in vitro
    • Seth, A. et al. Binary and ternary complexes between T-cell receptor, class II MHC and superantigen in vitro. Nature 369, 324-327 (1994).
    • (1994) Nature , vol.369 , pp. 324-327
    • Seth, A.1
  • 29
    • 0033119268 scopus 로고    scopus 로고
    • Role of the T cell receptor alpha chain in stabilizing TCR-superantigen-MHC class II complexes
    • Andersen, P. S. et al. Role of the T cell receptor alpha chain in stabilizing TCR-superantigen-MHC class II complexes. Immunity 10, 473-483 (1999).
    • (1999) Immunity , vol.10 , pp. 473-483
    • Andersen, P.S.1
  • 30
    • 0033168149 scopus 로고    scopus 로고
    • Cutting edge: Trimolecular interaction of TCR with MHC class II and bacterial superantigen shows a similar affinity to MHC: Peptide ligands
    • Redpath, S., Alam, S. M., Lin, C. M., O'Rourke, A. M. & Gascoigne, N. R. Cutting edge: Trimolecular interaction of TCR with MHC class II and bacterial superantigen shows a similar affinity to MHC: Peptide ligands. J. Immunol. 163, 6-10 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 6-10
    • Redpath, S.1    Alam, S.M.2    Lin, C.M.3    O'Rourke, A.M.4    Gascoigne, N.R.5
  • 31
    • 38649139095 scopus 로고    scopus 로고
    • Comprehensive analysis of the functional TCR repertoire at the single-cell level
    • Ozawa, T., Tajiri, K., Kishi, H. & Muraguchi, A. Comprehensive analysis of the functional TCR repertoire at the single-cell level. Biochem. Biophys. Res. Commun. 367, 820-825 (2008).
    • (2008) Biochem. Biophys. Res. Commun. , vol.367 , pp. 820-825
    • Ozawa, T.1    Tajiri, K.2    Kishi, H.3    Muraguchi, A.4
  • 32
    • 0032796508 scopus 로고    scopus 로고
    • T-cell repertoire analysis in chronic plaque psoriasis suggests an antigen-specific immune response
    • Bour, H. et al. T-cell repertoire analysis in chronic plaque psoriasis suggests an antigen-specific immune response. Hum. Immunol. 60, 665-676 (1999).
    • (1999) Hum. Immunol. , vol.60 , pp. 665-676
    • Bour, H.1
  • 33
    • 33750056963 scopus 로고    scopus 로고
    • Superantigens and chronic rhinosinusitis: Skewing of T-cell receptor V beta-distributions in polyp-derived CD4+ and CD8+ T cells
    • Conley, D. B. et al. Superantigens and chronic rhinosinusitis: Skewing of T-cell receptor V beta-distributions in polyp-derived CD4+ and CD8+ T cells. Am. J. Rhinol. 20, 534-539 (2006).
    • (2006) Am. J. Rhinol. , vol.20 , pp. 534-539
    • Conley, D.B.1
  • 34
    • 34548532890 scopus 로고    scopus 로고
    • Bacterial superantigens and T cell receptor beta-chain-bearing T cells in the immunopathogenesis of ulcerative colitis
    • Shiobara, N. et al. Bacterial superantigens and T cell receptor beta-chain-bearing T cells in the immunopathogenesis of ulcerative colitis. Clin. Exp. Immunol. 150, 13-21 (2007).
    • (2007) Clin. Exp. Immunol. , vol.150 , pp. 13-21
    • Shiobara, N.1
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number
    • Collaborative Computational Project, Number. The CCP4 suite: Programs for protein crystallography. Acta. Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta. Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 37
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 40
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta. Crystallogr. D Biol. Crystallogr. 54 (Part 5), 905-921 (1998).
    • (1998) Acta. Crystallogr. D Biol. Crystallogr. , vol.54 , Issue.PART 5 , pp. 905-921
    • Brunger, A.T.1
  • 41
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26, 795-800 (1993).
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 43
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple protein sequence and structure alignments
    • Pei, J., Kim, B. H. & Grishin, N. V. PROMALS3D: A tool for multiple protein sequence and structure alignments. Nucleic Acids Res. 36, 2295-2300 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3
  • 44
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F. et al. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 45
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: Development of a software pipeline
    • Vranken, W. F. et al. The CCPN data model for NMR spectroscopy: Development of a software pipeline. Proteins 59, 687-696 (2005).
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.