메뉴 건너뛰기




Volumn 383, Issue 3, 2008, Pages 603-614

Structure of Staphylococcus aureus EsxA Suggests a Contribution to Virulence by Action as a Transport Chaperone and/or Adaptor Protein

Author keywords

adaptor protein; chaperone; helical bundle; secretion system; virulence factor

Indexed keywords

ACID PROTEIN; ADAPTOR PROTEIN; BACTERIAL PROTEIN; CHAPERONE; CULTURE FILTRATE PROTEIN 10; EARLY SECRETORY ANTIGENIC TARGET 6; HOMODIMER; PROTEIN ESXA; PROTEIN ESXB; UNCLASSIFIED DRUG;

EID: 52949152375     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.08.047     Document Type: Article
Times cited : (68)

References (60)
  • 1
    • 0031925769 scopus 로고    scopus 로고
    • Staphylococcus aureus: a well-armed pathogen
    • Archer G.L. Staphylococcus aureus: a well-armed pathogen. Clin. Infect. Dis. 26 (1998) 1179-1181
    • (1998) Clin. Infect. Dis. , vol.26 , pp. 1179-1181
    • Archer, G.L.1
  • 2
    • 35349005704 scopus 로고    scopus 로고
    • Antimicrobial resistance, it's not just for hospitals
    • Bancroft E.A. Antimicrobial resistance, it's not just for hospitals. J. Am. Med. Assoc. 298 (2007) 1803-1804
    • (2007) J. Am. Med. Assoc. , vol.298 , pp. 1803-1804
    • Bancroft, E.A.1
  • 3
    • 0038665502 scopus 로고    scopus 로고
    • Antimicrobial resistance: the example of Staphylococcus aureus
    • Lowy F.D. Antimicrobial resistance: the example of Staphylococcus aureus. J. Clin. Invest. 111 (2003) 1265-1273
    • (2003) J. Clin. Invest. , vol.111 , pp. 1265-1273
    • Lowy, F.D.1
  • 4
    • 35748958975 scopus 로고    scopus 로고
    • Late stage antibacterial drugs in the clinical pipeline
    • Projan S.J., and Bradford P.A. Late stage antibacterial drugs in the clinical pipeline. Curr. Opin. Microbiol. 10 (2007) 441-446
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 441-446
    • Projan, S.J.1    Bradford, P.A.2
  • 5
    • 0030790687 scopus 로고    scopus 로고
    • Common themes in microbial pathogenicity revisited
    • Finlay B.B., and Falkow S. Common themes in microbial pathogenicity revisited. Microbiol. Mol. Biol. Rev. 61 (1997) 136-169
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 136-169
    • Finlay, B.B.1    Falkow, S.2
  • 6
    • 0036076014 scopus 로고    scopus 로고
    • Internalization of Staphylococcus aureus by human corneal epithelial cells: role of bacterial fibronectin-binding protein and host cell factors
    • Jett B.D., and Gilmore M.S. Internalization of Staphylococcus aureus by human corneal epithelial cells: role of bacterial fibronectin-binding protein and host cell factors. Infect. Immun. 70 (2002) 4697-4700
    • (2002) Infect. Immun. , vol.70 , pp. 4697-4700
    • Jett, B.D.1    Gilmore, M.S.2
  • 8
    • 0033396514 scopus 로고    scopus 로고
    • Bacterial fibronectin-binding proteins and endothelial cell surface fibronectin mediate adherence of Staphylococcus aureus to resting human endothelial cells
    • Peacock S.J., Foster T.J., Cameron B.J., and Berendt A.R. Bacterial fibronectin-binding proteins and endothelial cell surface fibronectin mediate adherence of Staphylococcus aureus to resting human endothelial cells. Microbiology 145 (1999) 3477-3486
    • (1999) Microbiology , vol.145 , pp. 3477-3486
    • Peacock, S.J.1    Foster, T.J.2    Cameron, B.J.3    Berendt, A.R.4
  • 9
    • 4644360265 scopus 로고    scopus 로고
    • The N-terminal A domain of fibronectin-binding proteins A and B promotes adhesion of Staphylococcus aureus to elastin
    • Roche F.M., Downer R., Keane F., Speziale P., Park P.W., and Foster T.J. The N-terminal A domain of fibronectin-binding proteins A and B promotes adhesion of Staphylococcus aureus to elastin. J. Biol. Chem. 279 (2004) 38433-38440
    • (2004) J. Biol. Chem. , vol.279 , pp. 38433-38440
    • Roche, F.M.1    Downer, R.2    Keane, F.3    Speziale, P.4    Park, P.W.5    Foster, T.J.6
  • 10
    • 0032809760 scopus 로고    scopus 로고
    • Following the leader: bacterial protein export through the Sec pathway
    • Economou A. Following the leader: bacterial protein export through the Sec pathway. Trends Microbiol. 7 (1999) 315-320
    • (1999) Trends Microbiol. , vol.7 , pp. 315-320
    • Economou, A.1
  • 11
    • 34248680765 scopus 로고    scopus 로고
    • Protein secretion systems in Mycobacteria
    • Champion P.A., and Cox J.S. Protein secretion systems in Mycobacteria. Cell. Microbiol. 9 (2007) 1376-1384
    • (2007) Cell. Microbiol. , vol.9 , pp. 1376-1384
    • Champion, P.A.1    Cox, J.S.2
  • 12
    • 12844288619 scopus 로고    scopus 로고
    • EsxA and EsxB are secreted by an ESAT-6-like system that is required for the pathogenesis of Staphylococcus aureus infections
    • Burts M.L., Williams W.A., DeBord K., and Missiakas D.M. EsxA and EsxB are secreted by an ESAT-6-like system that is required for the pathogenesis of Staphylococcus aureus infections. Proc. Natl Acad. Sci. USA 102 (2005) 1169-1174
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 1169-1174
    • Burts, M.L.1    Williams, W.A.2    DeBord, K.3    Missiakas, D.M.4
  • 13
    • 0028966384 scopus 로고
    • Purification and characterization of a low-molecular-mass T-cell antigen secreted by Mycobacterium tuberculosis
    • Sorensen A.L., Nagai S., Houen G., Andersen P., and Andersen A.B. Purification and characterization of a low-molecular-mass T-cell antigen secreted by Mycobacterium tuberculosis. Infect. Immun. 63 (1995) 1710-1717
    • (1995) Infect. Immun. , vol.63 , pp. 1710-1717
    • Sorensen, A.L.1    Nagai, S.2    Houen, G.3    Andersen, P.4    Andersen, A.B.5
  • 15
    • 0031767535 scopus 로고    scopus 로고
    • A Mycobacterium tuberculosis operon encoding ESAT-6 and a novel low-molecular-mass culture filtrate protein (CFP-10)
    • Berthet F.X., Rasmussen P.B., Rosenkrands I., Andersen P., and Gicquel B. A Mycobacterium tuberculosis operon encoding ESAT-6 and a novel low-molecular-mass culture filtrate protein (CFP-10). Microbiology 144 (1998) 3195-3203
    • (1998) Microbiology , vol.144 , pp. 3195-3203
    • Berthet, F.X.1    Rasmussen, P.B.2    Rosenkrands, I.3    Andersen, P.4    Gicquel, B.5
  • 16
    • 0030025636 scopus 로고    scopus 로고
    • Evidence for occurrence of the ESAT-6 protein in Mycobacterium tuberculosis and virulent Mycobacterium bovis and for its absence in Mycobacterium bovis BCG
    • Harboe M., Oettinger T., Wiker H.G., Rosenkrands I., and Andersen P. Evidence for occurrence of the ESAT-6 protein in Mycobacterium tuberculosis and virulent Mycobacterium bovis and for its absence in Mycobacterium bovis BCG. Infect. Immun. 64 (1996) 16-22
    • (1996) Infect. Immun. , vol.64 , pp. 16-22
    • Harboe, M.1    Oettinger, T.2    Wiker, H.G.3    Rosenkrands, I.4    Andersen, P.5
  • 17
  • 18
    • 0036437048 scopus 로고    scopus 로고
    • Loss of RD1 contributed to the attenuation of the live tuberculosis vaccines Mycobacterium bovis BCG and Mycobacterium microti
    • Pym A.S., Brodin P., Brosch R., Huerre M., and Cole S.T. Loss of RD1 contributed to the attenuation of the live tuberculosis vaccines Mycobacterium bovis BCG and Mycobacterium microti. Mol. Microbiol. 46 (2002) 709-717
    • (2002) Mol. Microbiol. , vol.46 , pp. 709-717
    • Pym, A.S.1    Brodin, P.2    Brosch, R.3    Huerre, M.4    Cole, S.T.5
  • 19
    • 0038751936 scopus 로고    scopus 로고
    • Recombinant BCG exporting ESAT-6 confers enhanced protection against tuberculosis
    • Pym A.S., Brodin P., Majlessi L., Brosch R., Demangel C., Williams A., et al. Recombinant BCG exporting ESAT-6 confers enhanced protection against tuberculosis. Nat. Med. 9 (2003) 533-539
    • (2003) Nat. Med. , vol.9 , pp. 533-539
    • Pym, A.S.1    Brodin, P.2    Majlessi, L.3    Brosch, R.4    Demangel, C.5    Williams, A.6
  • 21
    • 0036568776 scopus 로고    scopus 로고
    • The ESAT-6/WXG100 superfamily-and a new Gram-positive secretion system?
    • Pallen M.J. The ESAT-6/WXG100 superfamily-and a new Gram-positive secretion system?. Trends Microbiol. 10 (2002) 209-212
    • (2002) Trends Microbiol. , vol.10 , pp. 209-212
    • Pallen, M.J.1
  • 22
    • 0242268398 scopus 로고    scopus 로고
    • Acute infection and macrophage subversion by Mycobacterium tuberculosis require a specialized secretion system
    • Stanley S.A., Raghavan S., Hwang W.W., and Cox J.S. Acute infection and macrophage subversion by Mycobacterium tuberculosis require a specialized secretion system. Proc. Natl Acad. Sci. USA 100 (2003) 13001-13006
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13001-13006
    • Stanley, S.A.1    Raghavan, S.2    Hwang, W.W.3    Cox, J.S.4
  • 23
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 (1998) 537-544
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5    Harris, D.6
  • 24
    • 0037077299 scopus 로고    scopus 로고
    • Conclusive evidence that the major T-cell antigens of the Mycobacterium tuberculosis complex ESAT-6 and CFP-10 form a tight, 1:1 complex and characterization of the structural properties of ESAT-6, CFP-10, and the ESAT-6*CFP-10 complex. Implications for pathogenesis and virulence
    • Renshaw P.S., Panagiotidou P., Whelan A., Gordon S.V., Hewinson R.G., Williamson R.A., and Carr M.D. Conclusive evidence that the major T-cell antigens of the Mycobacterium tuberculosis complex ESAT-6 and CFP-10 form a tight, 1:1 complex and characterization of the structural properties of ESAT-6, CFP-10, and the ESAT-6*CFP-10 complex. Implications for pathogenesis and virulence. J. Biol. Chem. 277 (2002) 21598-21603
    • (2002) J. Biol. Chem. , vol.277 , pp. 21598-21603
    • Renshaw, P.S.1    Panagiotidou, P.2    Whelan, A.3    Gordon, S.V.4    Hewinson, R.G.5    Williamson, R.A.6    Carr, M.D.7
  • 25
    • 33745117262 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis H37Rv ESAT-6-CFP-10 complex formation confers thermodynamic and biochemical stability
    • Meher A.K., Bal N.C., Chary K.V., and Arora A. Mycobacterium tuberculosis H37Rv ESAT-6-CFP-10 complex formation confers thermodynamic and biochemical stability. FEBS J. 273 (2006) 1445-1462
    • (2006) FEBS J. , vol.273 , pp. 1445-1462
    • Meher, A.K.1    Bal, N.C.2    Chary, K.V.3    Arora, A.4
  • 26
    • 23044505589 scopus 로고    scopus 로고
    • Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6
    • Renshaw P.S., Lightbody K.L., Veverka V., Muskett F.W., Kelly G., Frenkiel T.A., et al. Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6. EMBO J. 24 (2005) 2491-2498
    • (2005) EMBO J. , vol.24 , pp. 2491-2498
    • Renshaw, P.S.1    Lightbody, K.L.2    Veverka, V.3    Muskett, F.W.4    Kelly, G.5    Frenkiel, T.A.6
  • 27
    • 47749092732 scopus 로고    scopus 로고
    • A protein linkage map of the ESAT-6 secretion system 1 (ESX-1) of Mycobacterium tuberculosis
    • Epub ahead of print
    • Teutschbein J., Schumann G., Möllmann U., Grabley S., Cole S.T., and Munder T. A protein linkage map of the ESAT-6 secretion system 1 (ESX-1) of Mycobacterium tuberculosis. Microbiol. Res. (2007) Epub ahead of print
    • (2007) Microbiol. Res.
    • Teutschbein, J.1    Schumann, G.2    Möllmann, U.3    Grabley, S.4    Cole, S.T.5    Munder, T.6
  • 29
    • 0027049823 scopus 로고
    • Relationships between sequence and structure for the four-alpha-helix bundle tertiary motif in proteins
    • Paliakasis C.D., and Kokkinidis M. Relationships between sequence and structure for the four-alpha-helix bundle tertiary motif in proteins. Protein Eng. 5 (1992) 739-748
    • (1992) Protein Eng. , vol.5 , pp. 739-748
    • Paliakasis, C.D.1    Kokkinidis, M.2
  • 30
    • 0029351694 scopus 로고
    • Protein motifs. 7. The four-helix bundle: what determines a fold?
    • Kamtekar S., and Hecht M.H. Protein motifs. 7. The four-helix bundle: what determines a fold?. FASEB J. 9 (1995) 1013-1022
    • (1995) FASEB J. , vol.9 , pp. 1013-1022
    • Kamtekar, S.1    Hecht, M.H.2
  • 31
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., and Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372 (2007) 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 33
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32 (2004) 1792-1797
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 34
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L.J., Bryson K., and Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 16 (2000) 404-405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 35
    • 26644466308 scopus 로고    scopus 로고
    • Functional analysis of early secreted antigenic target-6, the dominant T-cell antigen of Mycobacterium tuberculosis, reveals key residues involved in secretion, complex formation, virulence, and immunogenicity
    • Brodin P., de Jonge M.I., Majlessi L., Leclerc C., Nilges M., Cole S.T., and Brosch R. Functional analysis of early secreted antigenic target-6, the dominant T-cell antigen of Mycobacterium tuberculosis, reveals key residues involved in secretion, complex formation, virulence, and immunogenicity. J. Biol. Chem. 280 (2005) 33953-33959
    • (2005) J. Biol. Chem. , vol.280 , pp. 33953-33959
    • Brodin, P.1    de Jonge, M.I.2    Majlessi, L.3    Leclerc, C.4    Nilges, M.5    Cole, S.T.6    Brosch, R.7
  • 36
    • 33748776564 scopus 로고    scopus 로고
    • C-terminal signal sequence promotes virulence factor secretion in Mycobacterium tuberculosis
    • Champion P.A., Stanley S.A., Champion M.M., Brown E.J., and Cox J.S. C-terminal signal sequence promotes virulence factor secretion in Mycobacterium tuberculosis. Science 313 (2006) 1632-1636
    • (2006) Science , vol.313 , pp. 1632-1636
    • Champion, P.A.1    Stanley, S.A.2    Champion, M.M.3    Brown, E.J.4    Cox, J.S.5
  • 37
    • 34547766513 scopus 로고    scopus 로고
    • ESAT-6 from Mycobacterium tuberculosis dissociates from its putative chaperone CFP-10 under acidic conditions and exhibits membrane-lysing activity
    • de Jonge M.I., Pehau-Arnsudet G., Fretz M.M., Romain F., Bottai D., Brodin P., et al. ESAT-6 from Mycobacterium tuberculosis dissociates from its putative chaperone CFP-10 under acidic conditions and exhibits membrane-lysing activity. J. Bacteriol. 189 (2007) 6028-6034
    • (2007) J. Bacteriol. , vol.189 , pp. 6028-6034
    • de Jonge, M.I.1    Pehau-Arnsudet, G.2    Fretz, M.M.3    Romain, F.4    Bottai, D.5    Brodin, P.6
  • 38
    • 0142059794 scopus 로고    scopus 로고
    • The primary mechanism of attenuation of bacillus Calmette-Guérin is a loss of secreted lytic function required for invasion of lung interstitial tissue
    • Hsu T., Hingley-Wilson S.M., Chen B., Chen M., Dai A.Z., Morin P.M., Marks C.B., et al. The primary mechanism of attenuation of bacillus Calmette-Guérin is a loss of secreted lytic function required for invasion of lung interstitial tissue. Proc. Natl Acad. Sci. USA 100 (2003) 12420-12425
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 12420-12425
    • Hsu, T.1    Hingley-Wilson, S.M.2    Chen, B.3    Chen, M.4    Dai, A.Z.5    Morin, P.M.6    Marks, C.B.7
  • 39
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 40
    • 22544441094 scopus 로고    scopus 로고
    • ProFunc: a server for predicting protein function from 3D structure
    • Laskowski R.A., Watson J.D., and Thornton J.M. ProFunc: a server for predicting protein function from 3D structure. Nucleic Acids Res. 33 (2005) 89-93
    • (2005) Nucleic Acids Res. , vol.33 , pp. 89-93
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 42
    • 32344437432 scopus 로고    scopus 로고
    • Structural and dynamic characterization of a vinculin binding site in the talin rod
    • Gingras A.R., Vogel K.P., Steinhoff H.J., Ziegler W.H., Patel B., Emsley J., et al. Structural and dynamic characterization of a vinculin binding site in the talin rod. Biochemistry 45 (2006) 1805-1817
    • (2006) Biochemistry , vol.45 , pp. 1805-1817
    • Gingras, A.R.1    Vogel, K.P.2    Steinhoff, H.J.3    Ziegler, W.H.4    Patel, B.5    Emsley, J.6
  • 45
  • 46
    • 0033559680 scopus 로고    scopus 로고
    • The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli; a novel combination of domain folds
    • Hall D.R., Gourley D.G., Leonard G.A., Duke E.B.H., Anderson L.A., Boxer D.H., and Hunter W.N. The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli; a novel combination of domain folds. EMBO J. 18 (1999) 1435-1446
    • (1999) EMBO J. , vol.18 , pp. 1435-1446
    • Hall, D.R.1    Gourley, D.G.2    Leonard, G.A.3    Duke, E.B.H.4    Anderson, L.A.5    Boxer, D.H.6    Hunter, W.N.7
  • 50
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 51
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 53
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6 (1999) 458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 56
  • 58
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., and Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr., Sect. D: Biol. Crystallogr. 60 (2004) 2256-2268
    • (2004) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.