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Volumn 288, Issue 43, 2013, Pages 31042-31051

A non-classical assembly pathway of Escherichia coli pore-forming toxin Cytolysin A

Author keywords

[No Author keywords available]

Indexed keywords

INTRINSIC FLUORESCENCE; OLIGOMERIC STRUCTURE; OUTER MEMBRANE VESICLES; PATHOGENIC ESCHERICHIA COLI; PHYSIOLOGICAL TEMPERATURE; SALMONELLA ENTERICA; TRANS-MEMBRANE PORES; WATER-SOLUBLE OLIGOMERS;

EID: 84886681946     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.475350     Document Type: Article
Times cited : (37)

References (47)
  • 2
    • 9244241054 scopus 로고    scopus 로고
    • Pore-forming protein toxins: From structure to function
    • Parker, M. W., and Feil, S. C. (2005) Pore-forming protein toxins: from structure to function. Prog. Biophys. Mol. Biol. 88, 91-142
    • (2005) Prog. Biophys. Mol. Biol. , vol.88 , pp. 91-142
    • Parker, M.W.1    Feil, S.C.2
  • 3
    • 33645978129 scopus 로고    scopus 로고
    • The mechanism of pore formation by bacterial toxins
    • Tilley, S. J., and Saibil, H. R. (2006) The mechanism of pore formation by bacterial toxins. Curr. Opin. Struct. Biol. 16, 230-236
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 230-236
    • Tilley, S.J.1    Saibil, H.R.2
  • 4
    • 0032995242 scopus 로고    scopus 로고
    • Identification of a new Escherichia coli She haemolysin homolog in avian E
    • Reingold, J., Starr, N., Maurer, J., and Lee, M. D. (1999) Identification of a new Escherichia coli She haemolysin homolog in avian E. coli. Vet. Microbiol. 66, 125-134
    • (1999) Coli. Vet. Microbiol. , vol.66 , pp. 125-134
    • Reingold, J.1    Starr, N.2    Maurer, J.3    Lee, M.D.4
  • 5
    • 0029867360 scopus 로고    scopus 로고
    • Induction of haemolytic activity in Escherichia coli by the slyA gene product
    • Oscarsson, J., Mizunoe, Y., Uhlin, B. E., and Haydon, D. J. (1996) Induction of haemolytic activity in Escherichia coli by the slyA gene product. Mol. Microbiol. 20, 191-199
    • (1996) Mol. Microbiol. , vol.20 , pp. 191-199
    • Oscarsson, J.1    Mizunoe, Y.2    Uhlin, B.E.3    Haydon, D.J.4
  • 6
    • 0032927728 scopus 로고    scopus 로고
    • Analysis of the SlyA-controlled expression, subcellular localization and pore-forming activity of a 34 kDa haemolysin (ClyA) from Escherichia coli K-12
    • Ludwig, A., Bauer, S., Benz, R., Bergmann, B., and Goebel, W. (1999) Analysis of the SlyA-controlled expression, subcellular localization and pore-forming activity of a 34 kDa haemolysin (ClyA) from Escherichia coli K-12. Mol. Microbiol. 31, 557-567
    • (1999) Mol. Microbiol. , vol.31 , pp. 557-567
    • Ludwig, A.1    Bauer, S.2    Benz, R.3    Bergmann, B.4    Goebel, W.5
  • 7
    • 77955901062 scopus 로고    scopus 로고
    • Hemolysin E (HlyE, ClyA, SheA) and related toxins
    • Hunt, S., Green, J., and Artymiuk, P. J. (2010) Hemolysin E (HlyE, ClyA, SheA) and related toxins. Adv. Exp. Med. Biol. 677, 116-126
    • (2010) Adv. Exp. Med. Biol. , vol.677 , pp. 116-126
    • Hunt, S.1    Green, J.2    Artymiuk, P.J.3
  • 8
    • 0030749399 scopus 로고    scopus 로고
    • The Escherichia coli K-12 sheA gene encodes a 34-kDa secreted haemolysin
    • del Castillo, F. J., Leal, S. C., Moreno, F., and del Castillo, I. (1997) The Escherichia coli K-12 sheA gene encodes a 34-kDa secreted haemolysin. Mol. Microbiol. 25, 107-115
    • (1997) Mol. Microbiol. , vol.25 , pp. 107-115
    • Del Castillo, F.J.1    Leal, S.C.2    Moreno, F.3    Del Castillo, I.4
  • 10
    • 0034695613 scopus 로고    scopus 로고
    • E. Coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy
    • Wallace, A. J., Stillman, T. J., Atkins, A., Jamieson, S. J., Bullough, P. A., Green, J., and Artymiuk, P. J. (2000) E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy. Cell 100, 265-276
    • (2000) Cell , vol.100 , pp. 265-276
    • Wallace, A.J.1    Stillman, T.J.2    Atkins, A.3    Jamieson, S.J.4    Bullough, P.A.5    Green, J.6    Artymiuk, P.J.7
  • 11
    • 0036786521 scopus 로고    scopus 로고
    • Characterization of a poreforming cytotoxin expressed by Salmonella enterica serovars typhi and paratyphi A
    • Oscarsson, J., Westermark, M., Löfdahl, S., Olsen, B., Palmgren, H., Mizunoe, Y., Wai, S. N., and Uhlin, B. E. (2002) Characterization of a poreforming cytotoxin expressed by Salmonella enterica serovars typhi and paratyphi A. Inf. Immun. 70, 5759-5769
    • (2002) Inf. Immun. , vol.70 , pp. 5759-5769
    • Oscarsson, J.1    Westermark, M.2    Löfdahl, S.3    Olsen, B.4    Palmgren, H.5    Mizunoe, Y.6    Wai, S.N.7    Uhlin, B.E.8
  • 12
    • 66649132042 scopus 로고    scopus 로고
    • The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism
    • Mueller, M., Grauschopf, U., Maier, T., Glockshuber, R., and Ban, N. (2009) The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism. Nature 459, 726-730
    • (2009) Nature , vol.459 , pp. 726-730
    • Mueller, M.1    Grauschopf, U.2    Maier, T.3    Glockshuber, R.4    Ban, N.5
  • 14
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • Tweten, R. K. (2005) Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Inf. Immun. 73, 6199-6209
    • (2005) Inf. Immun. , vol.73 , pp. 6199-6209
    • Tweten, R.K.1
  • 15
    • 0035829509 scopus 로고    scopus 로고
    • Identification of the cellular receptor for anthrax toxin
    • Bradley, K. A., Mogridge, J., Mourez, M., Collier, R. J., and Young, J. A. (2001) Identification of the cellular receptor for anthrax toxin. Nature 414, 225-229
    • (2001) Nature , vol.414 , pp. 225-229
    • Bradley, K.A.1    Mogridge, J.2    Mourez, M.3    Collier, R.J.4    Young, J.A.5
  • 16
    • 0037300719 scopus 로고    scopus 로고
    • Anthrax toxin receptor proteins
    • Bradley, K. A., and Young, J. A. (2003) Anthrax toxin receptor proteins. Biochem. Pharmacol. 65, 309-314
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 309-314
    • Bradley, K.A.1    Young, J.A.2
  • 17
    • 21744447839 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore
    • Olson, R., and Gouaux, E. (2005) Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore. J. Mol. Biol. 350, 997-1016
    • (2005) J. Mol. Biol. , vol.350 , pp. 997-1016
    • Olson, R.1    Gouaux, E.2
  • 18
    • 77952302993 scopus 로고    scopus 로고
    • The cholesterol-dependent cytolysin family of gram-positive bacterial toxins
    • Heuck, A. P., Moe, P. C., and Johnson, B. B. (2010) The cholesterol-dependent cytolysin family of gram-positive bacterial toxins. Sub-cellular Biochem. 51, 551-577
    • (2010) Sub-cellular Biochem. , vol.51 , pp. 551-577
    • Heuck, A.P.1    Moe, P.C.2    Johnson, B.B.3
  • 19
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: Receptor binding, internalization, pore formation, and translocation
    • Young, J. A., and Collier, R. J. (2007) Anthrax toxin: receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76, 243-265
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2
  • 20
    • 0025787798 scopus 로고
    • α-Toxin of Staphylococcus aureus
    • Bhakdi, S., and Tranum-Jensen, J. (1991) α-Toxin of Staphylococcus aureus. Microbiol. Rev. 55, 733-751
    • (1991) Microbiol. Rev. , vol.55 , pp. 733-751
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 24
    • 77957959533 scopus 로고    scopus 로고
    • Biological functions and biogenesis of secreted bacterial outer membrane vesicles
    • Kulp, A., and Kuehn, M. J. (2010) Biological functions and biogenesis of secreted bacterial outer membrane vesicles. Annu. Rev. Microbiol. 64, 163-184
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 163-184
    • Kulp, A.1    Kuehn, M.J.2
  • 25
    • 27744480818 scopus 로고    scopus 로고
    • Bacterial outer membrane vesicles and the host-pathogen interaction
    • Kuehn, M. J., and Kesty, N. C. (2005) Bacterial outer membrane vesicles and the host-pathogen interaction. Genes Dev. 19, 2645-2655
    • (2005) Genes Dev. , vol.19 , pp. 2645-2655
    • Kuehn, M.J.1    Kesty, N.C.2
  • 26
    • 0029085873 scopus 로고
    • The release of outer membrane vesicles from the strains of enterotoxigenic Escherichia coli
    • Wai, S. N., Takade, A., and Amako, K. (1995) The release of outer membrane vesicles from the strains of enterotoxigenic Escherichia coli. Microbiol. Immunol. 39, 451-456
    • (1995) Microbiol. Immunol. , vol.39 , pp. 451-456
    • Wai, S.N.1    Takade, A.2    Amako, K.3
  • 27
    • 0037031850 scopus 로고    scopus 로고
    • Bacterial surface association of heat-labile enterotoxin through lipopolysaccharide after secretion via the general secretory pathway
    • Horstman, A. L., and Kuehn, M. J. (2002) Bacterial surface association of heat-labile enterotoxin through lipopolysaccharide after secretion via the general secretory pathway. J. Biol. Chem. 277, 32538-32545
    • (2002) J. Biol. Chem. , vol.277 , pp. 32538-32545
    • Horstman, A.L.1    Kuehn, M.J.2
  • 28
    • 0028334116 scopus 로고
    • Assays of hemolytic toxins
    • Rowe, G. E., and Welch, R. A. (1994) Assays of hemolytic toxins. Methods Enzymol. 235, 657-667
    • (1994) Methods Enzymol. , vol.235 , pp. 657-667
    • Rowe, G.E.1    Welch, R.A.2
  • 29
    • 44049102228 scopus 로고    scopus 로고
    • Outer membrane protein G: Engineering a quiet pore for biosensing
    • Chen, M., Khalid, S., Sansom, M. S., and Bayley, H. (2008) Outer membrane protein G: Engineering a quiet pore for biosensing. Proc. Natl. Acad. Sci. U. S. A. 105, 6272-6277
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 6272-6277
    • Chen, M.1    Khalid, S.2    Sansom, M.S.3    Bayley, H.4
  • 30
    • 0028567173 scopus 로고
    • Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: A heptameric transmembrane pore
    • Gouaux, J. E., Braha, O., Hobaugh, M. R., Song, L., Cheley, S., Shustak, C., and Bayley, H. (1994) Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proc. Natl. Acad. Sci. U. S. A. 91, 12828-12831
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 12828-12831
    • Gouaux, J.E.1    Braha, O.2    Hobaugh, M.R.3    Song, L.4    Cheley, S.5    Shustak, C.6    Bayley, H.7
  • 32
    • 79956294243 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins
    • De, S., and Olson, R. (2011) Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins. Proc. Natl. Acad. Sci. U. S. A. 108, 7385-7390
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 7385-7390
    • De, S.1    Olson, R.2
  • 34
    • 0029240394 scopus 로고
    • An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch
    • Walker, B., Braha, O., Cheley, S., and Bayley, H. (1995) An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch. Chem. Biol. 2, 99-105
    • (1995) Chem. Biol. , vol.2 , pp. 99-105
    • Walker, B.1    Braha, O.2    Cheley, S.3    Bayley, H.4
  • 35
    • 0028018856 scopus 로고
    • Anthrax protective antigen forms oligomers during intoxication of mammalian cells
    • Milne, J. C., Furlong, D., Hanna, P. C., Wall, J. S., and Collier, R. J. (1994) Anthrax protective antigen forms oligomers during intoxication of mammalian cells. J. Biol. Chem. 269, 20607-20612
    • (1994) J. Biol. Chem. , vol.269 , pp. 20607-20612
    • Milne, J.C.1    Furlong, D.2    Hanna, P.C.3    Wall, J.S.4    Collier, R.J.5
  • 36
    • 0034702810 scopus 로고    scopus 로고
    • The mechanism of pore assembly for a cholesterol-dependent cytolysin: Formation of a large prepore complex precedes the insertion of the transmembrane β-hairpins
    • Shepard, L. A., Shatursky, O., Johnson, A. E., and Tweten, R. K. (2000) The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane β-hairpins. Biochemistry 39, 10284-10293
    • (2000) Biochemistry , vol.39 , pp. 10284-10293
    • Shepard, L.A.1    Shatursky, O.2    Johnson, A.E.3    Tweten, R.K.4
  • 37
    • 39749091187 scopus 로고    scopus 로고
    • The formation and structure of Escherichia coli K-12 haemolysin E pores
    • Hunt, S., Moir, A. J., Tzokov, S., Bullough, P. A., Artymiuk, P. J., and Green, J. (2008) The formation and structure of Escherichia coli K-12 haemolysin E pores. Microbiology 154, 633-642
    • (2008) Microbiology , vol.154 , pp. 633-642
    • Hunt, S.1    Moir, A.J.2    Tzokov, S.3    Bullough, P.A.4    Artymiuk, P.J.5    Green, J.6
  • 39
    • 84866309637 scopus 로고    scopus 로고
    • An engineered ClyA nanopore detects folded target proteins by selective external association and pore entry
    • Soskine, M., Biesemans, A., Moeyaert, B., Cheley, S., Bayley, H., and Maglia, G. (2012) An engineered ClyA nanopore detects folded target proteins by selective external association and pore entry. Nano Letters 12, 4895-4900
    • (2012) Nano Letters , vol.12 , pp. 4895-4900
    • Soskine, M.1    Biesemans, A.2    Moeyaert, B.3    Cheley, S.4    Bayley, H.5    Maglia, G.6
  • 40
    • 56949085001 scopus 로고    scopus 로고
    • ClyA cytolysin from Salmonella: Distribution within the genus, regulation of expression by SlyA, and pore-forming characteristics
    • von Rhein, C., Bauer, S., López Sanjurjo, E. J., Benz, R., Goebel, W., and Ludwig, A. (2009) ClyA cytolysin from Salmonella: distribution within the genus, regulation of expression by SlyA, and pore-forming characteristics. Int. J. Med. Microbiol. 299, 21-35
    • (2009) Int. J. Med. Microbiol. , vol.299 , pp. 21-35
    • Von Rhein, C.1    Bauer, S.2    López Sanjurjo, E.J.3    Benz, R.4    Goebel, W.5    Ludwig, A.6
  • 41
    • 82955206472 scopus 로고    scopus 로고
    • Rapid assembly of a multimeric membrane protein pore
    • Thompson, J. R., Cronin, B., Bayley, H., and Wallace, M. I. (2011) Rapid assembly of a multimeric membrane protein pore. Biophys. J. 101, 2679-2683
    • (2011) Biophys. J. , vol.101 , pp. 2679-2683
    • Thompson, J.R.1    Cronin, B.2    Bayley, H.3    Wallace, M.I.4
  • 42
    • 84861389565 scopus 로고    scopus 로고
    • Disulfide bonding in protein biophysics
    • Fass, D. (2012) Disulfide bonding in protein biophysics. Annu. Rev. Biophys. 41, 63-79
    • (2012) Annu. Rev. Biophys. , vol.41 , pp. 63-79
    • Fass, D.1
  • 46
    • 0033031407 scopus 로고    scopus 로고
    • Molecular analysis of the cytolytic protein ClyA (SheA) from Escherichia coli
    • Oscarsson, J., Mizunoe, Y., Li, L., Lai, X. H., Wieslander, A., and Uhlin, B. E. (1999) Molecular analysis of the cytolytic protein ClyA (SheA) from Escherichia coli. Mol. Microbiol. 32, 1226-1238
    • (1999) Mol. Microbiol. , vol.32 , pp. 1226-1238
    • Oscarsson, J.1    Mizunoe, Y.2    Li, L.3    Lai, X.H.4    Wieslander, A.5    Uhlin, B.E.6


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