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Volumn 192, Issue 15, 2010, Pages 4001-4011

Mutations affecting export and activity of cytolysin A from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CYTOLYSIN; CYTOLYSIN A; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; HEMOLYSIN; HLYE PROTEIN, E COLI;

EID: 77955284761     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01283-09     Document Type: Article
Times cited : (18)

References (49)
  • 4
    • 0018139740 scopus 로고
    • Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli
    • Benz, R., K. Janko, W. Boos, and P. Läuger. 1978. Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim. Biophys. Acta 511:305-319. (Pubitemid 8404294)
    • (1978) Biochimica et Biophysica Acta , vol.511 , Issue.3 , pp. 305-319
    • Benz, R.1    Janko, K.2    Boos, W.3    Laeuger, P.4
  • 6
    • 0034091493 scopus 로고    scopus 로고
    • Characterization of the genes encoding the SheA haemolysin in Escherichia coli O157:H7 and Shigella flexneri 2a
    • del Castillo, F. J., F. Moreno, and I. del Castillo. 2000. Characterization of the genes encoding the SheA haemolysin in Escherichia coli O157:H7 and Shigella flexneri 2a. Res. Microbiol. 151:229-230.
    • (2000) Res. Microbiol. , vol.151 , pp. 229-230
    • Del Castillo, F.J.1    Moreno, F.2    Del Castillo, I.3
  • 7
    • 0035856571 scopus 로고    scopus 로고
    • Secretion of the Escherichia coli K-12 SheA hemolysin is independent of its cytolytic activity
    • del Castillo, F. J., F. Moreno, and I. del Castillo. 2001. Secretion of the Escherichia coli K-12 SheA hemolysin is independent of its cytolytic activity. FEMS Microbiol. Lett. 204:281-285.
    • (2001) FEMS Microbiol. Lett. , vol.204 , pp. 281-285
    • Del Castillo, F.J.1    Moreno, F.2    Del Castillo, I.3
  • 8
    • 0030749399 scopus 로고    scopus 로고
    • The Escherichia coli K-12 sheA gene encodes a 34-kDa secreted haemolysin
    • del Castillo, F. J., S. C. Leal, F. Moreno, and I. del Castillo. 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
    • 62249137129 scopus 로고    scopus 로고
    • A novel PhoP-regulated locus encoding the cytolysin ClyA and the secreted invasin TaiA of Salmonella enterica serovar Typhi is involved in virulence
    • Faucher, S. P., C. Forest, M. Béland, and F. Daigle. 2009. A novel PhoP-regulated locus encoding the cytolysin ClyA and the secreted invasin TaiA of Salmonella enterica serovar Typhi is involved in virulence. Microbiology 155:477-488.
    • (2009) Microbiology , vol.155 , pp. 477-488
    • Faucher, S.P.1    Forest, C.2    Béland, M.3    Daigle, F.4
  • 11
    • 32444446344 scopus 로고    scopus 로고
    • Transcriptome of Salmonella enterica serovar Typhi within macrophages revealed through the selective capture of transcribed sequences
    • Faucher, S. P., S. Porwollik, C. M. Dozois, M. McClelland, and F. Daigle. 2006. Transcriptome of Salmonella enterica serovar Typhi within macrophages revealed through the selective capture of transcribed sequences. Proc. Natl. Acad. Sci. U. S. A. 103:1906-1911.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 1906-1911
    • Faucher, S.P.1    Porwollik, S.2    Dozois, C.M.3    McClelland, M.4    Daigle, F.5
  • 12
    • 0032213047 scopus 로고    scopus 로고
    • Regulation of the Escherichia coli sheA gene and characterization of its encoded hemolytic activity
    • Fernandez, S. V., J. Xing, V. Kapur, S. J. Libby, R. G. Barletta, and R. A. Moxley. 1998. Regulation of the Escherichia coli sheA gene and characterization of its encoded hemolytic activity. FEMS Microbiol. Lett. 168:85-90.
    • (1998) FEMS Microbiol. Lett. , vol.168 , pp. 85-90
    • Fernandez, S.V.1    Xing, J.2    Kapur, V.3    Libby, S.J.4    Barletta, R.G.5    Moxley, R.A.6
  • 13
    • 44649196521 scopus 로고    scopus 로고
    • The Salmonella Typhi hlyE gene plays a role in invasion of cultured epithelial cells and its functional transfer to S. Typhimurium promotes deep organ infection in mice
    • Fuentes, J. A., N. Villagra, M. Castillo-Ruiz, and G. C. Mora. 2008. The Salmonella Typhi hlyE gene plays a role in invasion of cultured epithelial cells and its functional transfer to S. Typhimurium promotes deep organ infection in mice. Res. Microbiol. 159:279-287.
    • (2008) Res. Microbiol. , vol.159 , pp. 279-287
    • Fuentes, J.A.1    Villagra, N.2    Castillo-Ruiz, M.3    Mora, G.C.4
  • 14
    • 0031450904 scopus 로고    scopus 로고
    • The molecular basis for the differential regulation of the hlyE-encoded haemolysin of Escherichia coli by FNR and HlyX lies in the improved activating region 1 contact of HlyX
    • Green, J., and M. L. Baldwin. 1997. The molecular basis for the differential regulation of the hlyE-encoded haemolysin of Escherichia coli by FNR and HlyX lies in the improved activating region 1 contact of HlyX. Microbiology 143:3785-3793.
    • (1997) Microbiology , vol.143 , pp. 3785-3793
    • Green, J.1    Baldwin, M.L.2
  • 16
  • 19
    • 35448991375 scopus 로고    scopus 로고
    • Alternate SlyA and H-NS nucleoprotein complexes control hlyE expression in Escherichia coli K-12
    • Lithgow, J. K., F. Haider, I. S. Roberts, and J. Green. 2007. Alternate SlyA and H-NS nucleoprotein complexes control hlyE expression in Escherichia coli K-12. Mol. Microbiol. 66:685-698.
    • (2007) Mol. Microbiol. , vol.66 , pp. 685-698
    • Lithgow, J.K.1    Haider, F.2    Roberts, I.S.3    Green, J.4
  • 20
    • 0029589218 scopus 로고
    • SlyA, a regulatory protein from Salmonella typhimurium, induces a haemolytic and pore-forming protein in Escherichia coli
    • DOI 10.1007/BF00290573
    • Ludwig, A., C. Tengel, S. Bauer, A. Bubert, R. Benz, H.-J. Mollenkopf, and W. Goebel. 1995. SlyA, a regulatory protein of Salmonella typhimurium, induces a haemolytic and pore-forming protein in Escherichia coli. Mol. Gen. Genet. 249:474-486. (Pubitemid 26019057)
    • (1995) Molecular and General Genetics , vol.249 , Issue.5 , pp. 474-486
    • Ludwig, A.1    Tengel, C.2    Bauer, S.3    Bubert, A.4    Benz, R.5    Mollenkopf, H.-J.6    Goebel, W.7
  • 21
    • 44349093724 scopus 로고    scopus 로고
    • Release of latent ClyA cytolysin from Escherichia coli mediated by a bacteriophage-associated putative holin (BlyA) from Borrelia burgdorferi
    • DOI 10.1016/j.ijmm.2007.07.014, PII S1438422107001476
    • Ludwig, A., C. von Rhein, A. Mischke, and V. Brade. 2008. Release of latent ClyA cytolysin from Escherichia coli mediated by a bacteriophage- associated putative holin (BlyA) from Borrelia burgdorferi. Int. J. Med. Microbiol. 298: 473-481. (Pubitemid 351734794)
    • (2008) International Journal of Medical Microbiology , vol.298 , Issue.5-6 , pp. 473-481
    • Ludwig, A.1    Von Rhein, C.2    Mischke, A.3    Brade, V.4
  • 22
    • 3843127450 scopus 로고    scopus 로고
    • Molecular analysis of cytolysin A (ClyA) in pathogenic Escherichia coli strains
    • Ludwig, A., C. von Rhein, S. Bauer, C. Hüttinger, and W. Goebel. 2004. Molecular analysis of cytolysin A (ClyA) in pathogenic Escherichia coli strains. J. Bacteriol. 186:5311-5320.
    • (2004) J. Bacteriol. , vol.186 , pp. 5311-5320
    • Ludwig, A.1    Von Rhein, C.2    Bauer, S.3    Hüttinger, C.4    Goebel, W.5
  • 23
    • 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
    • DOI 10.1046/j.1365-2958.1999.01196.x
    • Ludwig, A., S. Bauer, R. Benz, B. Bergmann, and W. Goebel. 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. (Pubitemid 29046097)
    • (1999) Molecular Microbiology , vol.31 , Issue.2 , pp. 557-567
    • Ludwig, A.1    Bauer, S.2    Benz, R.3    Bergmann, B.4    Goebel, W.5
  • 24
    • 0000632797 scopus 로고
    • TnphoA: A transposon probe for protein export signals
    • Manoil, C., and J. Beckwith. 1985. TnphoA: a transposon probe for protein export signals. Proc. Natl. Acad. Sci. U. S. A. 82:8129-8133.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 8129-8133
    • Manoil, C.1    Beckwith, J.2
  • 25
    • 66649132042 scopus 로고    scopus 로고
    • The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism
    • Mueller, M., U. Grauschopf, T. Maier, R. Glockshuber, and N. Ban. 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
  • 26
    • 0015523228 scopus 로고
    • Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane
    • Osborn, M. J., J. E. Gander, E. Parisi, and J. Carson. 1972. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J. Biol. Chem. 247: 3962-3972.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3962-3972
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3    Carson, J.4
  • 29
    • 0029867360 scopus 로고    scopus 로고
    • Induction of haemolytic activity in Escherichia coli by the slyA gene product
    • Oscarsson, J., Y. Mizunoe, B. E. Uhlin, and D. J. Haydon. 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
  • 30
  • 31
    • 9244241054 scopus 로고    scopus 로고
    • Pore-forming protein toxins: From structure to function
    • Parker, M. W., and S. C. Feil. 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
  • 32
    • 0032168748 scopus 로고    scopus 로고
    • Altering the anaerobic transcription factor FNR confers a hemolytic phenotype on Escherichia coli K12
    • Ralph, E. T., J. R. Guest, and J. Green. 1998. Altering the anaerobic transcription factor FNR confers a hemolytic phenotype on Escherichia coli K12. Proc. Natl. Acad. Sci. U. S. A. 95:10449-10452.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 10449-10452
    • Ralph, E.T.1    Guest, J.R.2    Green, J.3
  • 33
    • 0032995242 scopus 로고    scopus 로고
    • Identification of a new Escherichia coli She haemolysin homolog in avian E. coli
    • Reingold, J., N. Starr, J. Maurer, and M. D. Lee. 1999. Identification of a new Escherichia coli She haemolysin homolog in avian E. coli. Vet. Microbiol. 66:125-134.
    • (1999) Vet. Microbiol. , vol.66 , pp. 125-134
    • Reingold, J.1    Starr, N.2    Maurer, J.3    Lee, M.D.4
  • 36
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song, L., M. R. Hobaugh, C. Shustak, S. Cheley, H. Bayley, and J. E. Gouaux. 1996. Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274:1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 39
    • 33750475603 scopus 로고    scopus 로고
    • Serologic evidence for effective production of cytolysin A in Salmonella enterica serovars Typhi and Paratyphi A during human infection
    • von Rhein, C., K.-P. Hunfeld, and A. Ludwig. 2006. Serologic evidence for effective production of cytolysin A in Salmonella enterica serovars Typhi and Paratyphi A during human infection. Infect. Immun. 74:6505-6508.
    • (2006) Infect. Immun. , vol.74 , pp. 6505-6508
    • Von Rhein, C.1    Hunfeld, K.-P.2    Ludwig, A.3
  • 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., S. Bauer, E. J. López Sanjurjo, R. Benz, W. Goebel, and A. Ludwig. 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
    • 51349147187 scopus 로고    scopus 로고
    • Occurrence and characteristics of the cytolysin A gene in Shigella strains and other members of the family Enterobacteriaceae
    • von Rhein, C., S. Bauer, V. Simon, and A. Ludwig. 2008. Occurrence and characteristics of the cytolysin A gene in Shigella strains and other members of the family Enterobacteriaceae. FEMS Microbiol. Lett. 287:143-148.
    • (2008) FEMS Microbiol. Lett. , vol.287 , pp. 143-148
    • Von Rhein, C.1    Bauer, S.2    Simon, V.3    Ludwig, A.4
  • 43
    • 0042838115 scopus 로고    scopus 로고
    • Characterization of dominantly negative mutant ClyA cytotoxin proteins in Escherichia coli
    • Wai, S. N., M. Westermark, J. Oscarsson, J. Jass, E. Maier, R. Benz, and B. E. Uhlin. 2003. Characterization of dominantly negative mutant ClyA cytotoxin proteins in Escherichia coli. J. Bacteriol. 185:5491-5499.
    • (2003) J. Bacteriol. , vol.185 , pp. 5491-5499
    • Wai, S.N.1    Westermark, M.2    Oscarsson, J.3    Jass, J.4    Maier, E.5    Benz, R.6    Uhlin, B.E.7
  • 45
    • 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., T. J. Stillman, A. Atkins, S. J. Jamieson, P. A. Bullough, J. Green, and P. J. Artymiuk. 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
  • 48
    • 1542286940 scopus 로고    scopus 로고
    • Regulation of Escherichia coli Hemolysin e Expression by H-NS and Salmonella SlyA
    • DOI 10.1128/JB.186.6.1620-1628.2004
    • Wyborn, N. R., M. R. Stapleton, V. A. Norte, R. E. Roberts, J. Grafton, and J. Green. 2004. Regulation of Escherichia coli hemolysin E expression by H-NS and Salmonella SlyA. J. Bacteriol. 186:1620-1628. (Pubitemid 38314507)
    • (2004) Journal of Bacteriology , vol.186 , Issue.6 , pp. 1620-1628
    • Wyborn, N.R.1    Stapleton, M.R.2    Norte, V.A.3    Roberts, R.E.4    Grafton, J.5    Green, J.6
  • 49
    • 59249086199 scopus 로고    scopus 로고
    • A peptide derived from the putative transmembrane domain in the tail region of E. coli toxin hemolysin E assembles in phospholipid membrane and exhibits lytic activity to human red blood cells: Plausible implications in the toxic activity of the protein
    • Yadav, S. P., A. Ahmad, B. K. Pandey, D. Singh, N. Asthana, R. Verma, R. K. Tripathi, and J. K. Ghosh. 2009. A peptide derived from the putative transmembrane domain in the tail region of E. coli toxin hemolysin E assembles in phospholipid membrane and exhibits lytic activity to human red blood cells: plausible implications in the toxic activity of the protein. Biochim. Biophys. Acta 1788:538-550.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 538-550
    • Yadav, S.P.1    Ahmad, A.2    Pandey, B.K.3    Singh, D.4    Asthana, N.5    Verma, R.6    Tripathi, R.K.7    Ghosh, J.K.8


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