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Volumn 100, Issue 7, 1997, Pages 1734-1741

Toxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cells

Author keywords

Cultured tumor cells; Glucosyltransferase; Lung fibroblasts; Pseudomembranous enterocolitis; Ras proteins

Indexed keywords

CLOSTRIDIUM DIFFICILE TOXIN A; CLOSTRIDIUM DIFFICILE TOXIN B; GLUCOSYLTRANSFERASE; RAS PROTEIN;

EID: 0030931082     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI119698     Document Type: Article
Times cited : (123)

References (31)
  • 1
    • 0030271882 scopus 로고    scopus 로고
    • Large clostridial cytotoxins - A family of glycosyltransferases modifying smalt GTP-binding proteins
    • von Eichel-Streiber, C., P. Boquet, M. Sauerhorn, and M. Thelestam. 1996. Large clostridial cytotoxins - a family of glycosyltransferases modifying smalt GTP-binding proteins. Trends Microbiol. 4:375-382.
    • (1996) Trends Microbiol. , vol.4 , pp. 375-382
    • Von Eichel-Streiber, C.1    Boquet, P.2    Sauerhorn, M.3    Thelestam, M.4
  • 2
  • 4
    • 0026764540 scopus 로고
    • Localization of two epitopes recognized by monoclonal antibody PCG-4 on Clostridium difficile toxin A
    • Frey, S.M., and T.D. Wilkins. 1992. Localization of two epitopes recognized by monoclonal antibody PCG-4 on Clostridium difficile toxin A. Infect. Immun. 60:2488-2492.
    • (1992) Infect. Immun. , vol.60 , pp. 2488-2492
    • Frey, S.M.1    Wilkins, T.D.2
  • 5
    • 0026565693 scopus 로고
    • Comparison of Clostridium sordellii toxins HT and LT with toxins A and B of C. difficile
    • Martinez, R.D., and T.D. Wilkins. 1992. Comparison of Clostridium sordellii toxins HT and LT with toxins A and B of C. difficile. J. Med. Microbiol. 36:30-36.
    • (1992) J. Med. Microbiol. , vol.36 , pp. 30-36
    • Martinez, R.D.1    Wilkins, T.D.2
  • 8
    • 0031003475 scopus 로고    scopus 로고
    • Bacterial toxins that target Rho proteins
    • Aktories, K. 1997. Bacterial toxins that target Rho proteins. J. Clin. Invest. 99:827-829.
    • (1997) J. Clin. Invest. , vol.99 , pp. 827-829
    • Aktories, K.1
  • 9
    • 0028790399 scopus 로고
    • Monoglucosylation of low-molecular-mass GTP-binding Rho proteins by clostridial cytotoxins
    • Aktories, K., and I. Just. 1995. Monoglucosylation of low-molecular-mass GTP-binding Rho proteins by clostridial cytotoxins. Trends Cell Biol. 5:441-443.
    • (1995) Trends Cell Biol. , vol.5 , pp. 441-443
    • Aktories, K.1    Just, I.2
  • 10
    • 0021108235 scopus 로고
    • Internalization of Clostridium difficile cytotoxin into cultured human lung fibroblasts
    • Florin, I., and M. Thelestam. 1983. Internalization of Clostridium difficile cytotoxin into cultured human lung fibroblasts. Biochim. Biophys. Acta. 763: 383-392.
    • (1983) Biochim. Biophys. Acta , vol.763 , pp. 383-392
    • Florin, I.1    Thelestam, M.2
  • 11
    • 0023269823 scopus 로고
    • Cellular internalisation of Clostridium difficile toxin A
    • Henriques, B., I. Florin, and M. Thelestam. 1987. Cellular internalisation of Clostridium difficile toxin A. Microb. Pathog. 2:455-463.
    • (1987) Microb. Pathog. , vol.2 , pp. 455-463
    • Henriques, B.1    Florin, I.2    Thelestam, M.3
  • 12
    • 0029854589 scopus 로고    scopus 로고
    • Molecular mimicry in the recognition of glycosphingolipids by Galα3Galβ4GlcNAcβ-binding Clostridium difficile toxin A, human natural anti α-galactosyl IgG and the monoclonal antibody Gal-13: Characterization of a binding-active human glycosphingolipid, non-identical with the animal receptor
    • Teneberg, S., I. Lönnroth, J.F. Torres Lopez, U. Galili, M.O. Halvarsson, J. Ångström, and K.A. Karlsson. 1996. Molecular mimicry in the recognition of glycosphingolipids by Galα3Galβ4GlcNAcβ-binding Clostridium difficile toxin A, human natural anti α-galactosyl IgG and the monoclonal antibody Gal-13: characterization of a binding-active human glycosphingolipid, non-identical with the animal receptor. Glycobiology. 6:599-609.
    • (1996) Glycobiology , vol.6 , pp. 599-609
    • Teneberg, S.1    Lönnroth, I.2    Torres Lopez, J.F.3    Galili, U.4    Halvarsson, M.O.5    Ångström, J.6    Karlsson, K.A.7
  • 13
    • 0021995801 scopus 로고
    • Effects of Clostridium difficile toxins given intragastrically to animals
    • Lyerly, D.M., K.E. Saum, D.K. MacDonald, and T.D. Wilkins. 1985. Effects of Clostridium difficile toxins given intragastrically to animals. Infect. Immun. 47:349-352.
    • (1985) Infect. Immun. , vol.47 , pp. 349-352
    • Lyerly, D.M.1    Saum, K.E.2    MacDonald, D.K.3    Wilkins, T.D.4
  • 14
    • 0002011582 scopus 로고
    • Clostridium difficile
    • M.J. Blaser, P.D. Smith, J.I. Ravdin, H.B. Greenberg, and R.L. Guerrant, editors. Raven Press, Ltd., New York
    • Lyerly, D.M., and T.D. Wilkins. 1995. Clostridium difficile. In Infections of the Gastrointestinal Tract. M.J. Blaser, P.D. Smith, J.I. Ravdin, H.B. Greenberg, and R.L. Guerrant, editors. Raven Press, Ltd., New York. 867-891.
    • (1995) Infections of the Gastrointestinal Tract , pp. 867-891
    • Lyerly, D.M.1    Wilkins, T.D.2
  • 15
    • 0025272689 scopus 로고
    • Toxin A of Clostridium difficile is a potent cytotoxin
    • Tucker, K.D., P.E. Carrig, and T.D. Wilkins. 1990. Toxin A of Clostridium difficile is a potent cytotoxin. J. Clin. Microbiol. 28:869-871.
    • (1990) J. Clin. Microbiol. , vol.28 , pp. 869-871
    • Tucker, K.D.1    Carrig, P.E.2    Wilkins, T.D.3
  • 16
    • 0023175490 scopus 로고
    • Purification of two high molecular weight toxins of Clostridium difficile which are antigenically related
    • von Eichel-Streiber, C., U. Harperath, D. Bosse, and U. Hadding. 1987. Purification of two high molecular weight toxins of Clostridium difficile which are antigenically related. Microb. Pathog. 2:307-318.
    • (1987) Microb. Pathog. , vol.2 , pp. 307-318
    • Von Eichel-Streiber, C.1    Harperath, U.2    Bosse, D.3    Hadding, U.4
  • 17
    • 0025614767 scopus 로고
    • Microfilament-disrupting Clostridiutn difficile toxin B causes multinucleation of transformed cells but does not block capping of membrane Ig
    • Shoshan, M.C., P. Aman, S. Skog, I. Florin, and M. Thelestam. 1990. Microfilament-disrupting Clostridiutn difficile toxin B causes multinucleation of transformed cells but does not block capping of membrane Ig. Eur. J. Cell Biol. 53:357-363.
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 357-363
    • Shoshan, M.C.1    Aman, P.2    Skog, S.3    Florin, I.4    Thelestam, M.5
  • 18
    • 0029924167 scopus 로고    scopus 로고
    • UDP-glucose deficiency in a mutant cell line protects against glucosyltransferase toxins from Clostridium difficile and Clostridium sordellii
    • Chaves-Olarte, E., I. Florin, P. Boquet, M. Popoff, C. von Eichel-Streiber, and M. Thelestam. 1996. UDP-glucose deficiency in a mutant cell line protects against glucosyltransferase toxins from Clostridium difficile and Clostridium sordellii. J. Biol. Chem. 271:6925-6932.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6925-6932
    • Chaves-Olarte, E.1    Florin, I.2    Boquet, P.3    Popoff, M.4    Von Eichel-Streiber, C.5    Thelestam, M.6
  • 19
    • 0017074162 scopus 로고
    • An improved radiochemical assay for uridine diphosphoglucose pyrophosphorylase
    • Hames, B.D. 1976. An improved radiochemical assay for uridine diphosphoglucose pyrophosphorylase. Anal. Biochem. 73:215-219.
    • (1976) Anal. Biochem. , vol.73 , pp. 215-219
    • Hames, B.D.1
  • 20
    • 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 (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0018068693 scopus 로고
    • Association of diphtheria toxin with Vero cells: Demonstration of a receptor
    • Middlebrook, J.L., R.B. Dorland, and S.H. Leppla. 1978. Association of diphtheria toxin with Vero cells: demonstration of a receptor. J. Biol. Chem. 253:7325-7330.
    • (1978) J. Biol. Chem. , vol.253 , pp. 7325-7330
    • Middlebrook, J.L.1    Dorland, R.B.2    Leppla, S.H.3
  • 23
    • 0024204607 scopus 로고
    • Clostridium difficile toxin A perturbs cytoskeletal structure and tight junction permeability of cultured human intestinal epithelial monolayers
    • Hechl, G., C. Pothoulakis, J.T. LaMont, and J.L. Madara. 1988. Clostridium difficile toxin A perturbs cytoskeletal structure and tight junction permeability of cultured human intestinal epithelial monolayers. J. Clin. Invest. 82:1516-1524.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1516-1524
    • Hechl, G.1    Pothoulakis, C.2    Lamont, J.T.3    Madara, J.L.4
  • 24
  • 25
    • 0022443783 scopus 로고
    • Lysosomal involvement in cellular intoxication with Clostridium difficile toxin B
    • Florin, I., and M. Thelestam. 1986. Lysosomal involvement in cellular intoxication with Clostridium difficile toxin B. Microb. Pathog. 1:373-385.
    • (1986) Microb. Pathog. , vol.1 , pp. 373-385
    • Florin, I.1    Thelestam, M.2
  • 26
    • 0030891386 scopus 로고    scopus 로고
    • Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxin
    • Hofmann, F., C. Busch, U. Prepens, I. Just, and K. Aktories. 1997. Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxin. J. Biol. Chem. 272:11074-11078.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11074-11078
    • Hofmann, F.1    Busch, C.2    Prepens, U.3    Just, I.4    Aktories, K.5
  • 27
    • 84954214925 scopus 로고    scopus 로고
    • Clostridium difficile toxins
    • K. Aktories, editor. Chapman & Hall Inc., Weinheim
    • Thelestam, M., I. Florin, and E. Chaves-Olarte. 1997. Clostridium difficile toxins. In Bacterial Toxins. K. Aktories, editor. Chapman & Hall Inc., Weinheim. 141-158.
    • (1997) Bacterial Toxins , pp. 141-158
    • Thelestam, M.1    Florin, I.2    Chaves-Olarte, E.3
  • 28
    • 0026082902 scopus 로고
    • Binding kinetics of Clostridium difficile toxins A and B to intestinal brush border membranes from infant and adult hamsters
    • Rolfe, R.D. 1991. Binding kinetics of Clostridium difficile toxins A and B to intestinal brush border membranes from infant and adult hamsters. Infect. Immun. 59:1223-1230.
    • (1991) Infect. Immun. , vol.59 , pp. 1223-1230
    • Rolfe, R.D.1
  • 29
    • 0029960807 scopus 로고    scopus 로고
    • Clostridium difficile toxins attack Rho
    • Wilkins, T.D., and D.M. Lyerly. 1996. Clostridium difficile toxins attack Rho. Trends Microbiol. 4:49-51.
    • (1996) Trends Microbiol. , vol.4 , pp. 49-51
    • Wilkins, T.D.1    Lyerly, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.