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Volumn 135, Issue 2, 2005, Pages 107-115

Role of lipopolysaccharide on the structure and function of α-hemolysin from Escherichia coli

Author keywords

Bacterial toxins; Lipid protein interaction; Lipopolysaccharide; Protein fluorescence; Protein stability

Indexed keywords

ALPHA HEMOLYSIN; CALCIUM; CATION; HEMOLYSIN; LIPOPOLYSACCHARIDE; TOXIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 19744371191     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2005.02.009     Document Type: Article
Times cited : (14)

References (37)
  • 1
    • 0027987495 scopus 로고
    • Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy
    • J.L. Arrondo, J. Castresana, J.M. Valpuesta, and F.M. Goñi Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy Biochemistry 33 1994 11650 11655
    • (1994) Biochemistry , vol.33 , pp. 11650-11655
    • Arrondo, J.L.1    Castresana, J.2    Valpuesta, J.M.3    Goñi, F.M.4
  • 3
    • 0032545776 scopus 로고    scopus 로고
    • Calcium-dependent conformation of E. coli alpha-haemolysin. Implications for the mechanism of membrane insertion and lysis
    • L. Bakás, M. Veiga, A. Soloaga, H. Ostolaza, and F. Goñi Calcium-dependent conformation of E. coli alpha-haemolysin. Implications for the mechanism of membrane insertion and lysis Biochim. Biophys. Acta 1368 1998 225 234
    • (1998) Biochim. Biophys. Acta , vol.1368 , pp. 225-234
    • Bakás, L.1    Veiga, M.2    Soloaga, A.3    Ostolaza, H.4    Goñi, F.5
  • 4
    • 0030976392 scopus 로고    scopus 로고
    • Pleiotropic effects of a mutation in rfaC on Escherichia coli hemolysin
    • M.E. Bauer, and R.A. Welch Pleiotropic effects of a mutation in rfaC on Escherichia coli hemolysin Infect. Inmunol. 65 1997 218 224
    • (1997) Infect. Inmunol. , vol.65 , pp. 218-224
    • Bauer, M.E.1    Welch, R.A.2
  • 5
    • 0021765180 scopus 로고
    • Fluorescence characterization of the low pH-induced change in diphtheria toxin conformation: Effect of salt
    • M.G. Blewit, J.M. Zhao, B. Mc Keever, R. Sarma, and E. London Fluorescence characterization of the low pH-induced change in diphtheria toxin conformation: effect of salt Biochem. Biophys. Res. Commun. 120 1984 286 290
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 286-290
    • Blewit, M.G.1    Zhao, J.M.2    Mc Keever, B.3    Sarma, R.4    London, E.5
  • 6
    • 0033601291 scopus 로고    scopus 로고
    • Lipid-assisted protein folding
    • M. Bogdanov, and W. Dowhan Lipid-assisted protein folding J. Biol. Chem. 271 1999 36287 36830
    • (1999) J. Biol. Chem. , vol.271 , pp. 36287-36830
    • Bogdanov, M.1    Dowhan, W.2
  • 7
    • 0022414174 scopus 로고
    • Chemical and inmunological analysis of the complex structure of Escherichia coli hemolysin
    • G.A. Bohach, and I.S. Snyder Chemical and inmunological analysis of the complex structure of Escherichia coli hemolysin J. Bacteriol. 164 1985 1071 1080
    • (1985) J. Bacteriol. , vol.164 , pp. 1071-1080
    • Bohach, G.A.1    Snyder, I.S.2
  • 8
    • 0030060225 scopus 로고    scopus 로고
    • Random and directed mutagenesis to elucidate the functional importance of helix II anf F-989 in the C-terminal secretion signal of Escherichia coli hemolysin
    • C. Chevaux, and I. Holland Random and directed mutagenesis to elucidate the functional importance of helix II anf F-989 in the C-terminal secretion signal of Escherichia coli hemolysin J. Bacteriol. 178 1996 1232 1236
    • (1996) J. Bacteriol. , vol.178 , pp. 1232-1236
    • Chevaux, C.1    Holland, I.2
  • 9
    • 0028811427 scopus 로고
    • Biological effects of RTX toxins: The possible role of lipopolysaccharide
    • C.J. Czuprynski, and R.A. Welch Biological effects of RTX toxins: the possible role of lipopolysaccharide Trends Microbiol. 12 1995 480 483
    • (1995) Trends Microbiol. , vol.12 , pp. 480-483
    • Czuprynski, C.J.1    Welch, R.A.2
  • 10
    • 0034830405 scopus 로고    scopus 로고
    • Identification of phospolipids as new components that assist the in vitro trimerization of a bacterial pore protein
    • H. De Cock, M. Pasveer, J. Tommasen, and E. Bouveret Identification of phospolipids as new components that assist the in vitro trimerization of a bacterial pore protein Eur. J. Biochem. 268 2001 865 875
    • (2001) Eur. J. Biochem. , vol.268 , pp. 865-875
    • De Cock, H.1    Pasveer, M.2    Tommasen, J.3    Bouveret, E.4
  • 11
    • 0023354335 scopus 로고
    • Alkaline phosphatase which lacks its own signal sequence becomes enzymatically active when fused to N-terminal sequences of Escherichia coli a-hemolysin (HlyA)
    • K. Erb, M. Vogel, W. Wagner, and W. Goebel Alkaline phosphatase which lacks its own signal sequence becomes enzymatically active when fused to N-terminal sequences of Escherichia coli a-hemolysin (HlyA) Mol. Gen. Genet 208 1987 88 93
    • (1987) Mol. Gen. Genet , vol.208 , pp. 88-93
    • Erb, K.1    Vogel, M.2    Wagner, W.3    Goebel, W.4
  • 12
    • 0025245593 scopus 로고
    • Modification of the silver staining technique to detect lipopolysaccharide in polyacrylamide gels
    • A. Fomsgaard, M. Freudenberg, and C. Galanos Modification of the silver staining technique to detect lipopolysaccharide in polyacrylamide gels J. Clin. Microbiol. 28 1990 2627 2631
    • (1990) J. Clin. Microbiol. , vol.28 , pp. 2627-2631
    • Fomsgaard, A.1    Freudenberg, M.2    Galanos, C.3
  • 14
    • 1542319821 scopus 로고    scopus 로고
    • Lipopolysaccharide 3-deoxy-d-manno-octulosonic acid (Kdo) core determines bacterial association of secreted toxins
    • A. Horstman, S. Bauman, and M. Kuehn Lipopolysaccharide 3-deoxy-d-manno-octulosonic acid (Kdo) core determines bacterial association of secreted toxins J. Biol. Chem. 279 2004 8070 8075
    • (2004) J. Biol. Chem. , vol.279 , pp. 8070-8075
    • Horstman, A.1    Bauman, S.2    Kuehn, M.3
  • 15
    • 0018087520 scopus 로고
    • A new and improved microassay to determine 2-keto-3-deoxyoctonate in lipopolisaccharide of Gram-negative bacteria
    • A.D. Karkhanis, J.Y. Zeltner, and D.J.C. Carlo A new and improved microassay to determine 2-keto-3-deoxyoctonate in lipopolisaccharide of Gram-negative bacteria Anal. Biochem. 85 1978 595 601
    • (1978) Anal. Biochem. , vol.85 , pp. 595-601
    • Karkhanis, A.D.1    Zeltner, J.Y.2    Carlo, D.J.C.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0033021088 scopus 로고    scopus 로고
    • Lipopolysacharide complexes with Pasteurella haemolytica leucotoxin
    • J. Li, and K. Clinkenbeard Lipopolysacharide complexes with Pasteurella haemolytica leucotoxin Infect. Immunol. 67 1999 2920 2927
    • (1999) Infect. Immunol. , vol.67 , pp. 2920-2927
    • Li, J.1    Clinkenbeard, K.2
  • 19
    • 0025288364 scopus 로고
    • The repeat domain of Escherichia coli a-haemolysin is responsible for its Ca-dependent binding to erythrocyte
    • A. Ludwig, T. Jarchau, R. Benz, and W. Goebel The repeat domain of Escherichia coli a-haemolysin is responsible for its Ca-dependent binding to erythrocyte Infect. Immunol. 58 1990 1959 1964
    • (1990) Infect. Immunol. , vol.58 , pp. 1959-1964
    • Ludwig, A.1    Jarchau, T.2    Benz, R.3    Goebel, W.4
  • 20
    • 4143096133 scopus 로고    scopus 로고
    • Role of apolipoprotein A-I in protecting against endotoxin toxicity
    • J. Ma, X. Liao, B. Lou, and M. Wu Role of apolipoprotein A-I in protecting against endotoxin toxicity Acta Biochim. Biophys. Sinica 36 2004 419 424
    • (2004) Acta Biochim. Biophys. Sinica , vol.36 , pp. 419-424
    • Ma, J.1    Liao, X.2    Lou, B.3    Wu, M.4
  • 22
    • 0030804938 scopus 로고    scopus 로고
    • Balance of electrostatic and hydrophobic interactions in the lysis of model membranes by E. coli alpha-haemolysin
    • H. Ostolaza, L. Bakas, and F. Goñi Balance of electrostatic and hydrophobic interactions in the lysis of model membranes by E. coli alpha-haemolysin J. Membr. Biol. 158 1997 137 145
    • (1997) J. Membr. Biol. , vol.158 , pp. 137-145
    • Ostolaza, H.1    Bakas, L.2    Goñi, F.3
  • 24
    • 0029084310 scopus 로고
    • Interaction of the bacterial protein toxin alpha-haemolysin with model membranes: Protein binding does not always lead to lytic activity
    • H. Ostolaza, and F.M. Goñi Interaction of the bacterial protein toxin alpha-haemolysin with model membranes: protein binding does not always lead to lytic activity FEBS Lett. 371 1995 303 306
    • (1995) FEBS Lett. , vol.371 , pp. 303-306
    • Ostolaza, H.1    Goñi, F.M.2
  • 25
    • 0027166219 scopus 로고
    • Selective removal of free dodecyl sulfate from 2-mercaptoethanol-SDS- solubilized proteins before KDS-protein precipitation
    • M. Sandri, C. Rizzi, C. Catani, and U. Carraro Selective removal of free dodecyl sulfate from 2-mercaptoethanol-SDS-solubilized proteins before KDS-protein precipitation Anal. Biochem. 213 1993 34 39
    • (1993) Anal. Biochem. , vol.213 , pp. 34-39
    • Sandri, M.1    Rizzi, C.2    Catani, C.3    Carraro, U.4
  • 26
    • 0027202811 scopus 로고
    • Genetics of lipopysaccharide biosynthesis in enteric bacteria
    • C.A. Schnaitman, and J.D. Klena Genetics of lipopysaccharide biosynthesis in enteric bacteria Microbiol. Rev. 57 1993 655 682
    • (1993) Microbiol. Rev. , vol.57 , pp. 655-682
    • Schnaitman, C.A.1    Klena, J.D.2
  • 27
    • 19744380722 scopus 로고
    • The dispersion of Gram negative lipopolisaccharide by deoxycolate
    • J. Shauds, and P. Chun The dispersion of Gram negative lipopolisaccharide by deoxycolate J. Biol. Chem. 255 1980 121 126
    • (1980) J. Biol. Chem. , vol.255 , pp. 121-126
    • Shauds, J.1    Chun, P.2
  • 28
    • 0014438695 scopus 로고
    • Some factors affecting production and assay of Escherichia coli hemolysin
    • I.S. Snyder, and P. Zwadyk Some factors affecting production and assay of Escherichia coli hemolysin J. Gen. Microbiol. 5 1969 133 143
    • (1969) J. Gen. Microbiol. , vol.5 , pp. 133-143
    • Snyder, I.S.1    Zwadyk, P.2
  • 29
    • 0344404206 scopus 로고    scopus 로고
    • Reversible denaturation, self aggregation and membrane activity of Escherichia coli a-Hemolysin, a protein stable in 6 M urea
    • A. Soloaga, J.M. Ramirez, and F.M. Goñi Reversible denaturation, self aggregation and membrane activity of Escherichia coli a-Hemolysin, a protein stable in 6 M urea Biochemistry 37 1998 6387 6393
    • (1998) Biochemistry , vol.37 , pp. 6387-6393
    • Soloaga, A.1    Ramirez, J.M.2    Goñi, F.M.3
  • 30
    • 0033032585 scopus 로고    scopus 로고
    • Insertion of Escherichia coli a-haemolysin in lipid bilayer as a non-transmembrane integral protein: Prediction and experiment
    • A. Soloaga, P. Veiga, L. García Segura, H. Ostolaza, R. Brasseur, and F. Goñi Insertion of Escherichia coli a-haemolysin in lipid bilayer as a non-transmembrane integral protein: prediction and experiment Mol. Microbiol. 31 1999 1013 1024
    • (1999) Mol. Microbiol. , vol.31 , pp. 1013-1024
    • Soloaga, A.1    Veiga, P.2    García Segura, L.3    Ostolaza, H.4    Brasseur, R.5    Goñi, F.6
  • 31
    • 0027489462 scopus 로고
    • Loss of activity in the secreted form of Escherichia coli. Haemolysin caused by and rfaP lesion in core lipopolysacharide assembly
    • P. Standley, P. Diaz, M. Bailey, D. Gygy, A. Juarez, and C. Hughes Loss of activity in the secreted form of Escherichia coli. Haemolysin caused by and rfaP lesion in core lipopolysacharide assembly Mol. Microbiol. 10 1993 781 787
    • (1993) Mol. Microbiol. , vol.10 , pp. 781-787
    • Standley, P.1    Diaz, P.2    Bailey, M.3    Gygy, D.4    Juarez, A.5    Hughes, C.6
  • 32
    • 0029989067 scopus 로고    scopus 로고
    • Independent interaction of the acyltransferase I with the maduration domains of Escherichia coli toxin HlyA
    • P. Standley, V. Koronakis, K. Hardie, and C. Hughes Independent interaction of the acyltransferase I with the maduration domains of Escherichia coli toxin HlyA Mol. Microbiol. 20 1996 813 822
    • (1996) Mol. Microbiol. , vol.20 , pp. 813-822
    • Standley, P.1    Koronakis, V.2    Hardie, K.3    Hughes, C.4
  • 33
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • H. Towbin, T. Staehelin, and J. Gordon Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications Proc. Natl. Acad. Sci. 76 1979 4350 4354
    • (1979) Proc. Natl. Acad. Sci. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 34
    • 0023410985 scopus 로고
    • Tryptophan fluorescence of mitochondrial complex III reconstituted in phosphatidylcholine bilayers
    • J. Valpuesta, F.M. Goñi, and J. Macarulla Tryptophan fluorescence of mitochondrial complex III reconstituted in phosphatidylcholine bilayers Arch. Biochem. Biophys. 257 1987 285 292
    • (1987) Arch. Biochem. Biophys. , vol.257 , pp. 285-292
    • Valpuesta, J.1    Goñi, F.M.2    MacArulla, J.3
  • 35
    • 0027404233 scopus 로고
    • Involvement of lipopolysacharide in the secretion of Escherichia coli a-hemolysin and Erwinia chrysantemi proteases
    • C. Wandersman, and S. Letouffe Involvement of lipopolysacharide in the secretion of Escherichia coli a-hemolysin and Erwinia chrysantemi proteases Mol. Microbiol. 7 1993 141 150
    • (1993) Mol. Microbiol. , vol.7 , pp. 141-150
    • Wandersman, C.1    Letouffe, S.2
  • 36
    • 0034467679 scopus 로고    scopus 로고
    • RTX toxin structure and function: A story of numerous anomalies and few analogies in toxin biology
    • R. Welch RTX toxin structure and function: a story of numerous anomalies and few analogies in toxin biology Curr. Top. Microbiol. Immunol. 257 2001 85 111
    • (2001) Curr. Top. Microbiol. Immunol. , vol.257 , pp. 85-111
    • Welch, R.1
  • 37
    • 0002447206 scopus 로고
    • Bacterial lipopolysaccharides: Extraction with phenol-water and further applications of the procedure
    • Q. Westphal, and K. Jann Bacterial lipopolysaccharides: extraction with phenol-water and further applications of the procedure Methods Carbohydr. Chem. 5 1965 83 89
    • (1965) Methods Carbohydr. Chem. , vol.5 , pp. 83-89
    • Westphal, Q.1    Jann, K.2


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