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Volumn 180, Issue 6, 1998, Pages 1368-1374

Contribution of the disulfide bond of the A subunit to the action of Escherichia coli heat-labile enterotoxin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; CYCLIC AMP; CYSTEINE; ESCHERICHIA COLI ENTEROTOXIN; OLIGOMER;

EID: 0031942258     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.6.1368-1374.1998     Document Type: Article
Times cited : (11)

References (30)
  • 1
    • 0018688158 scopus 로고
    • Cistron encoding Escherichia coli heat-labile toxin
    • Dallas, W. S., D. M. Gill, and S. Falkow. 1979. Cistron encoding Escherichia coli heat-labile toxin. J. Bacteriol. 139:850-858.
    • (1979) J. Bacteriol. , vol.139 , pp. 850-858
    • Dallas, W.S.1    Gill, D.M.2    Falkow, S.3
  • 2
    • 0025951531 scopus 로고
    • Characterization of the binding site for Escherichia coli heat-labile toxin type I in intestinal brush borders
    • Griffiths, S. L., and D. R. Critchley. 1991. Characterization of the binding site for Escherichia coli heat-labile toxin type I in intestinal brush borders. Biochim. Biophys. Acta 1075:154-161.
    • (1991) Biochim. Biophys. Acta , vol.1075 , pp. 154-161
    • Griffiths, S.L.1    Critchley, D.R.2
  • 3
    • 0002588630 scopus 로고
    • Coordinated assembly of multisubunit proteins: Oligomerization of bacterial enterotoxins in vivo and in vitro
    • Hardy, S. J. S., J. Holmgren, S. Johansson, J. Sanchez, and T. R. Hirst. 1988. Coordinated assembly of multisubunit proteins: oligomerization of bacterial enterotoxins in vivo and in vitro. Proc. Natl. Acad. Sci. USA 85:7109-7113.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7109-7113
    • Hardy, S.J.S.1    Holmgren, J.2    Johansson, S.3    Sanchez, J.4    Hirst, T.R.5
  • 4
    • 0003122268 scopus 로고
    • Biogenesis of cholera toxin and related oligomeric enterotoxins
    • J. Moss, B. Iglewski, M. Vaughan, and A. T. Tu (ed.), Marcel Dekker, Inc., New York, N.Y.
    • Hirst, T. R. 1995. Biogenesis of cholera toxin and related oligomeric enterotoxins, p. 123-184. In J. Moss, B. Iglewski, M. Vaughan, and A. T. Tu (ed.), Bacterial toxins and virulence factors in disease. Marcel Dekker, Inc., New York, N.Y.
    • (1995) Bacterial Toxins and Virulence Factors in Disease , pp. 123-184
    • Hirst, T.R.1
  • 5
    • 0020534204 scopus 로고
    • Assembly in vivo of enterotoxin from Escherichia coli: Formation of the B subunit oligomer
    • Hirst, T. R., S. J. S. Hardy, and L. L. Randall. 1983. Assembly in vivo of enterotoxin from Escherichia coli: formation of the B subunit oligomer. J. Bacteriol. 153:21-26.
    • (1983) J. Bacteriol. , vol.153 , pp. 21-26
    • Hirst, T.R.1    Hardy, S.J.S.2    Randall, L.L.3
  • 6
    • 0021702380 scopus 로고
    • Kinetics of synthesis, processing, and membrane transport of heat-labile enterotoxin, a periplasmic protein in Escherichia coli
    • Hofstra, H., and B. Witholt. 1984. Kinetics of synthesis, processing, and membrane transport of heat-labile enterotoxin, a periplasmic protein in Escherichia coli. J. Biol. Chem. 259:15182-15187.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15182-15187
    • Hofstra, H.1    Witholt, B.2
  • 7
    • 0022373611 scopus 로고
    • Heat-labile enterotoxin in Escherichia coli: Kinetics of association of subunits into periplasmic holotoxin
    • Hofstra, H., and B. Witholt. 1985. Heat-labile enterotoxin in Escherichia coli: kinetics of association of subunits into periplasmic holotoxin. J. Biol. Chem. 260:16037-16044.
    • (1985) J. Biol. Chem. , vol.260 , pp. 16037-16044
    • Hofstra, H.1    Witholt, B.2
  • 8
    • 0000287302 scopus 로고
    • Structure and function of E. coli heat-labile enterotoxin and cholera toxin B pentamer
    • J. Moss. B. Iglewski, M. Vaughan, and A. T. Tu (ed.), Marcel Dekker, Inc., New York, N.Y.
    • Hol, W. G. J., T. K. Sixma, and E. A. Merritt. 1995. Structure and function of E. coli heat-labile enterotoxin and cholera toxin B pentamer, p. 185-223. In J. Moss. B. Iglewski, M. Vaughan, and A. T. Tu (ed.), Bacterial toxins and virulence factors in disease. Marcel Dekker, Inc., New York, N.Y.
    • (1995) Bacterial Toxins and Virulence Factors in Disease , pp. 185-223
    • Hol, W.G.J.1    Sixma, T.K.2    Merritt, E.A.3
  • 9
    • 0002893654 scopus 로고
    • Cholera toxin and related enterotoxins of gram-negative bacteria. Biogenesis of cholera toxin and related oligomeric enterotoxins
    • J. Moss, B. Iglewski, M. Vaughan, and A. T. Tu (ed.), Marcel Dekker, Inc., New York, N.Y.
    • Holmes, R. K., M. G. Jobling, and T. D. Connell. 1995. Cholera toxin and related enterotoxins of gram-negative bacteria. Biogenesis of cholera toxin and related oligomeric enterotoxins, p. 225-255. In J. Moss, B. Iglewski, M. Vaughan, and A. T. Tu (ed.), Bacterial toxins and virulence factors in disease. Marcel Dekker, Inc., New York, N.Y.
    • (1995) Bacterial Toxins and Virulence Factors in Disease , pp. 225-255
    • Holmes, R.K.1    Jobling, M.G.2    Connell, T.D.3
  • 10
    • 0002976376 scopus 로고
    • Oligonucleotide directed site-specific mutagenesis using double-stranded plasmid DNA
    • S. A. Narang (ed.). Academic Press, Inc., New York, N.Y.
    • Inouye, S., and M. Inouye. 1987. Oligonucleotide directed site-specific mutagenesis using double-stranded plasmid DNA, p. 181-206. In S. A. Narang (ed.). Synthesis and application of DNA and RNA. Academic Press, Inc., New York, N.Y.
    • (1987) Synthesis and Application of DNA and RNA , pp. 181-206
    • Inouye, S.1    Inouye, M.2
  • 11
    • 0026489949 scopus 로고
    • Fusion proteins containing the A2 domain of cholera toxin assemble with B polypeptides of cholera toxin to form immunoreactive and functional holotoxin-like chimeras
    • Jobling, M. G., and R. K. Holmes. 1992. Fusion proteins containing the A2 domain of cholera toxin assemble with B polypeptides of cholera toxin to form immunoreactive and functional holotoxin-like chimeras. Infect. Immun. 60:4915-4924.
    • (1992) Infect. Immun. , vol.60 , pp. 4915-4924
    • Jobling, M.G.1    Holmes, R.K.2
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0027955887 scopus 로고
    • Structure of partially-activated E. coli heat-labile enterotoxin (LT) at 2.6 Å resolution
    • Merritt, E. A., S. P. Pronk, T. K. Sixma, K. H. Kalk, B. A. M. van Zanten, and W. G. J. Hol. 1994. Structure of partially-activated E. coli heat-labile enterotoxin (LT) at 2.6 Å resolution. FEBS Lett. 337:88-92.
    • (1994) FEBS Lett. , vol.337 , pp. 88-92
    • Merritt, E.A.1    Pronk, S.P.2    Sixma, T.K.3    Kalk, K.H.4    Van Zanten, B.A.M.5    Hol, W.G.J.6
  • 16
    • 0028123001 scopus 로고
    • Galactose binding site in E. coli heat-labile enterotoxin (LT) and cholera toxin (CT)
    • Merritt, E. A., T. K. Sixma, K. H. Kalk, B. A. M. van Zanten, and W. G. J, Hol. 1994. Galactose binding site in E. coli heat-labile enterotoxin (LT) and cholera toxin (CT). Mol. Microbiol. 13:745-753.
    • (1994) Mol. Microbiol. , vol.13 , pp. 745-753
    • Merritt, E.A.1    Sixma, T.K.2    Kalk, K.H.3    Van Zanten, B.A.M.4    Hol, W.G.J.5
  • 17
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Miller, J. 1972. Experiments in molecular genetics, p. 431-433. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics , pp. 431-433
    • Miller, J.1
  • 18
    • 0023928970 scopus 로고
    • Effect of substitution of glycine for arginine at position 146 of the A1 subunit on biological activity of Escherichia coli heat-labile enterotoxin
    • Okamoto, K., K. Okamoto, A. Miyama, T. Tsuji, T. Honda, and T. Miwatani. 1988. Effect of substitution of glycine for arginine at position 146 of the A1 subunit on biological activity of Escherichia coli heat-labile enterotoxin. J. Bacteriol. 170:2208-2211.
    • (1988) J. Bacteriol. , vol.170 , pp. 2208-2211
    • Okamoto, K.1    Okamoto, K.2    Miyama, A.3    Tsuji, T.4    Honda, T.5    Miwatani, T.6
  • 19
    • 0031048978 scopus 로고    scopus 로고
    • Protein-disulfide isomerase-mediated reduction of the A subunit of cholera toxin in a human intestinal cell line
    • Orlandi, P. A. 1997. Protein-disulfide isomerase-mediated reduction of the A subunit of cholera toxin in a human intestinal cell line. J. Biol. Chem. 272:4591-4599.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4591-4599
    • Orlandi, P.A.1
  • 20
    • 0027314536 scopus 로고
    • Brefeldin A blocks the response of cultured cells to cholera toxin. Implications for intracellular trafficking in toxin action
    • Orlandi, P. A., P. K. Curran, and P. H. Fishman. 1993. Brefeldin A blocks the response of cultured cells to cholera toxin. Implications for intracellular trafficking in toxin action. J. Biol. Chem. 268:12010-12016.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12010-12016
    • Orlandi, P.A.1    Curran, P.K.2    Fishman, P.H.3
  • 21
    • 0029783552 scopus 로고    scopus 로고
    • Assembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin
    • Ruddock, L. W., J. J. F. Coen, C. Cheesman, R. B. Freedman, and T. R. Hirst. 1996. Assembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. J. Biol. Chem. 271:19118-19123.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19118-19123
    • Ruddock, L.W.1    Coen, J.J.F.2    Cheesman, C.3    Freedman, R.B.4    Hirst, T.R.5
  • 22
    • 0029610368 scopus 로고
    • Kinetics of acid-mediated disassembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin
    • Ruddock, L. W., S. P. Ruston, S. M. Kelly, N. C. Price, R. B. Freedman, and T. R. Hirst. 1995. Kinetics of acid-mediated disassembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. J. Biol. Chem. 270: 29953-29958.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29953-29958
    • Ruddock, L.W.1    Ruston, S.P.2    Kelly, S.M.3    Price, N.C.4    Freedman, R.B.5    Hirst, T.R.6
  • 23
  • 25
    • 0020325261 scopus 로고
    • Escherichia coli heat-labile enterotoxin, nucleotide sequence of the A subunit gene
    • Spicer, E. K., and J. A. Nobel. 1982. Escherichia coli heat-labile enterotoxin, nucleotide sequence of the A subunit gene. J. Biol. Chem. 257:5716-5721.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5716-5721
    • Spicer, E.K.1    Nobel, J.A.2
  • 26
    • 0027102749 scopus 로고
    • Intermolecular interactions between the A and B subunits of heat-labile enterotoxin from Escherichia coli promote holotoxin assembly and stability in vivo
    • Streatfleld, S. J., M. Sandkvist, T. K. Sixma, M. Bagdasarian, W. G. J. Hol, and T. R. Hirst. 1992. Intermolecular interactions between the A and B subunits of heat-labile enterotoxin from Escherichia coli promote holotoxin assembly and stability in vivo. Proc. Natl. Acad. Sci. USA 89:12140-12144.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 12140-12144
    • Streatfleld, S.J.1    Sandkvist, M.2    Sixma, T.K.3    Bagdasarian, M.4    Hol, W.G.J.5    Hirst, T.R.6
  • 28
    • 0028296259 scopus 로고
    • Simple method of purification of Escherichia coli heat-labile enterotoxin and cholera toxin using immobilized galactose
    • Uesaka, Y., Y. Otsuka, Z. Lin, S. Yamasaki, J. Yamaoka, H. Kurazono, and Y. Takeda. 1994. Simple method of purification of Escherichia coli heat-labile enterotoxin and cholera toxin using immobilized galactose. Microb. Pathog. 16:71-76.
    • (1994) Microb. Pathog. , vol.16 , pp. 71-76
    • Uesaka, Y.1    Otsuka, Y.2    Lin, Z.3    Yamasaki, S.4    Yamaoka, J.5    Kurazono, H.6    Takeda, Y.7
  • 29
    • 0004755957 scopus 로고
    • ADP-ribosylation factors: A family of guanine nucleotide-binding proteins that activate cholera toxin and . regulate vesicular transport
    • J. Moss, B. Iglewski, M. Vaughan, and A. T. Tu (ed.), Marcel Dekker, Inc., New York, N.Y.
    • Welsh, C. F., J. Moss, and M. Vaughan. 1995. ADP-ribosylation factors: a family of guanine nucleotide-binding proteins that activate cholera toxin and . regulate vesicular transport, p. 257-280. In J. Moss, B. Iglewski, M. Vaughan, and A. T. Tu (ed.), Bacterial toxins and virulence factors in disease. Marcel Dekker, Inc., New York, N.Y.
    • (1995) Bacterial Toxins and Virulence Factors in Disease , pp. 257-280
    • Welsh, C.F.1    Moss, J.2    Vaughan, M.3
  • 30
    • 0021368685 scopus 로고
    • Primary structure of heat-labile enterotoxin produced by Escherichia coli pathogenic for humans
    • Yamamoto, T., T. Tamura, and T. Yokota. 1984. Primary structure of heat-labile enterotoxin produced by Escherichia coli pathogenic for humans. J. Biol. Chem. 259:5037-5044.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5037-5044
    • Yamamoto, T.1    Tamura, T.2    Yokota, T.3


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