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Volumn 71, Issue 6, 2003, Pages 3294-3301

Mutational analysis of the enzymatic domain of Clostridium difficile toxin B reveals novel inhibitors of the wild-type toxin

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TOXIN; ANTHRAX TOXIN; CLOSTRIDIUM DIFFICILE TOXIN B; CLOSTRIDIUM TOXIN; ENZYME; ENZYME INHIBITOR; GLUCOSYLTRANSFERASE; GUANINE NUCLEOTIDE BINDING PROTEIN; HYDROLASE; LETHAL TOXIN; PROTEIN CDC42; RAC PROTEIN; RHO FACTOR; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 0037767234     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.71.6.3294-3301.2003     Document Type: Article
Times cited : (14)

References (31)
  • 1
    • 0026741811 scopus 로고
    • Fusions of anthrax toxin lethal factor to the ADP-ribosylation domain of Pseudomonas exotoxin A are potent cytotoxins which are translocated to the cytosol of mammalian cells
    • Arora, N., K. R. Klimpel, Y. Singh, and S. H. Leppla. 1992. Fusions of anthrax toxin lethal factor to the ADP-ribosylation domain of Pseudomonas exotoxin A are potent cytotoxins which are translocated to the cytosol of mammalian cells. J. Biol. Chem. 267:15542-15548.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15542-15548
    • Arora, N.1    Klimpel, K.R.2    Singh, Y.3    Leppla, S.H.4
  • 2
    • 0028072074 scopus 로고
    • Fusions of anthrax toxin lethal factor with Shiga toxin and diphtheria toxin enzymatic domains are toxic to mammalian cells
    • Arora, N., and S. H. Leppla. 1994. Fusions of anthrax toxin lethal factor with Shiga toxin and diphtheria toxin enzymatic domains are toxic to mammalian cells. Infect. Immun. 62:4955-4961.
    • (1994) Infect. Immun. , vol.62 , pp. 4955-4961
    • Arora, N.1    Leppla, S.H.2
  • 3
    • 0027403919 scopus 로고
    • Residues 1-254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides
    • Arora, N., and S. H. Leppla. 1993. Residues 1-254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides. J. Biol. Chem. 268:3334-3341.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3334-3341
    • Arora, N.1    Leppla, S.H.2
  • 4
    • 0027973442 scopus 로고
    • Cytotoxic effects of a chimeric protein consisting of tetanus toxin light chain and anthrax toxin lethal factor in non-neuronal cells
    • Arora, N., L. C. Williamson, S. H. Leppla, and J. L. Halpern. 1994. Cytotoxic effects of a chimeric protein consisting of tetanus toxin light chain and anthrax toxin lethal factor in non-neuronal cells. J. Biol. Chem. 269:26165-26171.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26165-26171
    • Arora, N.1    Williamson, L.C.2    Leppla, S.H.3    Halpern, J.L.4
  • 5
    • 0029914034 scopus 로고    scopus 로고
    • Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo
    • Ballard, J. D., R. J. Collier, and M. N. Starnbach. 1996. Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo. Proc. Natl. Acad. Sci. USA 93:12531-12534.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12531-12534
    • Ballard, J.D.1    Collier, R.J.2    Starnbach, M.N.3
  • 6
    • 0035815642 scopus 로고    scopus 로고
    • Low pH-induced formation of ion channels by Clostridium difficile toxin B in target cells
    • Barth, H., G. Pfeifer, F. Hofmann, E. Maier, R. Benz, and K. Aktories. 2001. Low pH-induced formation of ion channels by Clostridium difficile toxin B in target cells. J. Biol. Chem. 276:10670-10676.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10670-10676
    • Barth, H.1    Pfeifer, G.2    Hofmann, F.3    Maier, E.4    Benz, R.5    Aktories, K.6
  • 7
    • 0033427140 scopus 로고    scopus 로고
    • Bacterial toxins inhibiting or activating small GTP-binding proteins
    • Boquet, P. 1999. Bacterial toxins inhibiting or activating small GTP-binding proteins. Ann. N. Y. Acad. Sci. 886:83-90.
    • (1999) Ann. N. Y. Acad. Sci. , vol.886 , pp. 83-90
    • Boquet, P.1
  • 8
    • 0034607988 scopus 로고    scopus 로고
    • Involvement of a conserved tryptophan residue in the UDP-glucose binding of large clostridial cytotoxin glycosyltransferases
    • Busch, C., F. Hofmann, R. Gerhard, and K. Aktories. 2000. Involvement of a conserved tryptophan residue in the UDP-glucose binding of large clostridial cytotoxin glycosyltransferases. J. Biol. Chem. 275:13228-13234.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13228-13234
    • Busch, C.1    Hofmann, F.2    Gerhard, R.3    Aktories, K.4
  • 9
    • 0032584665 scopus 로고    scopus 로고
    • A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins
    • Busch, C., F. Hofmann, J. Selzer, S. Munro, D. Jeckel, and K. Aktories. 1998. A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins. J. Biol. Chem. 273:19566-19572.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19566-19572
    • Busch, C.1    Hofmann, F.2    Selzer, J.3    Munro, S.4    Jeckel, D.5    Aktories, K.6
  • 10
    • 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
  • 11
    • 0032568829 scopus 로고    scopus 로고
    • Clostridium difficile toxins A and B are cation-dependent UDP-glucose hydrolases with differing catalytic activities
    • Ciesla, W. P., Jr., and D. A. Bobak. 1998. Clostridium difficile toxins A and B are cation-dependent UDP-glucose hydrolases with differing catalytic activities. J. Biol. Chem. 273:16021-16026.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16021-16026
    • Ciesla W.P., Jr.1    Bobak, D.A.2
  • 12
    • 0036286070 scopus 로고    scopus 로고
    • Experimental effects of Saccharomyces boulardii on diarrheal pathogens
    • Czerucka, D., and P. Rampal. 2002. Experimental effects of Saccharomyces boulardii on diarrheal pathogens. Microbes Infect. 4:733-739.
    • (2002) Microbes Infect. , vol.4 , pp. 733-739
    • Czerucka, D.1    Rampal, P.2
  • 13
    • 0034546376 scopus 로고    scopus 로고
    • Clostridium difficile toxins A and B can alter epithelial permeability and promote bacterial paracellular migration through HT-29 enterocytes
    • Feltis, B. A., S. M. Wiesner, A. S. Kim, S. L. Erlandsen, D. L. Lyerly, T. D. Wilkins, and C. L. Wells. 2000. Clostridium difficile toxins A and B can alter epithelial permeability and promote bacterial paracellular migration through HT-29 enterocytes. Shock 14:629-634.
    • (2000) Shock , vol.14 , pp. 629-634
    • Feltis, B.A.1    Wiesner, S.M.2    Kim, A.S.3    Erlandsen, S.L.4    Lyerly, D.L.5    Wilkins, T.D.6    Wells, C.L.7
  • 15
    • 0029127708 scopus 로고
    • Transient expression of RhoA, -B, and -C GTPases in HeLa cells potentiates resistance to Clostridium difficile toxins A and B but not to Clostridium sordellii lethal toxin
    • Giry, M., M. R. Popoff, C. von Eichel-Streiber, and P. Boquet. 1995. Transient expression of RhoA, -B, and -C GTPases in HeLa cells potentiates resistance to Clostridium difficile toxins A and B but not to Clostridium sordellii lethal toxin. Infect. Immun. 63:4063-4071.
    • (1995) Infect. Immun. , vol.63 , pp. 4063-4071
    • Giry, M.1    Popoff, M.R.2    Von Eichel-Streiber, C.3    Boquet, P.4
  • 16
    • 1842367878 scopus 로고    scopus 로고
    • Rho prevents apoptosis through Bcl-2 expression: Implications for interleukin-2 receptor signal transduction
    • Gomez, J., C. Martinez, M. Giry, A. Garcia, and A. Rebollo. 1997. Rho prevents apoptosis through Bcl-2 expression: implications for interleukin-2 receptor signal transduction. Eur. J. Immunol. 27:2793-2799.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 2793-2799
    • Gomez, J.1    Martinez, C.2    Giry, M.3    Garcia, A.4    Rebollo, A.5
  • 17
    • 0031887901 scopus 로고    scopus 로고
    • Chimeric clostridial cytotoxins: Identification of the N-terminal region involved in protein substrate recognition
    • Hofmann, F., C. Busch, and K. Aktories. 1998. Chimeric clostridial cytotoxins: identification of the N-terminal region involved in protein substrate recognition. Infect. Immun. 66:1076-1081.
    • (1998) Infect. Immun. , vol.66 , pp. 1076-1081
    • Hofmann, F.1    Busch, C.2    Aktories, K.3
  • 19
    • 0028941839 scopus 로고
    • Protective antigen-binding domain of anthrax lethal factor mediates translocation of a heterologous protein fused to its amino- or carboxy-terminus
    • Milne, J. C., S. R. Blanke, P. C. Hanna, and R. J. Collier. 1995. Protective antigen-binding domain of anthrax lethal factor mediates translocation of a heterologous protein fused to its amino- or carboxy-terminus. Mol. Microbiol. 15:661-666.
    • (1995) Mol. Microbiol. , vol.15 , pp. 661-666
    • Milne, J.C.1    Blanke, S.R.2    Hanna, P.C.3    Collier, R.J.4
  • 20
    • 0035952233 scopus 로고    scopus 로고
    • Clostridium difficile-associated diarrhea: A review
    • Mylonakis, E., E. T. Ryan, and S. B. Calderwood. 2001. Clostridium difficile-associated diarrhea: a review. Arch. Intern. Med. 161:525-533.
    • (2001) Arch. Intern. Med. , vol.161 , pp. 525-533
    • Mylonakis, E.1    Ryan, E.T.2    Calderwood, S.B.3
  • 21
    • 0035112067 scopus 로고    scopus 로고
    • Clostridium difficile toxins disrupt epithelial barrier function by altering membrane microdomain localization of tight junction proteins
    • Nusrat, A., C. von Eichel-Streiber, J. R. Turner, P. Verkade, J. L. Madara, and C. A. Parkos. 2001. Clostridium difficile toxins disrupt epithelial barrier function by altering membrane microdomain localization of tight junction proteins. Infect. Immun. 69:1329-1336.
    • (2001) Infect. Immun. , vol.69 , pp. 1329-1336
    • Nusrat, A.1    Von Eichel-Streiber, C.2    Turner, J.R.3    Verkade, P.4    Madara, J.L.5    Parkos, C.A.6
  • 22
    • 0034999642 scopus 로고    scopus 로고
    • Microbes and microbial toxins: Paradigms for microbial-mucosal interactions. II. The integrated response of the intestine to Clostridium difficile toxins
    • Pothoulakis, C., and J. T. Lamont. 2001. Microbes and microbial toxins: paradigms for microbial-mucosal interactions. II. The integrated response of the intestine to Clostridium difficile toxins. Am. J. Physiol. Gastrointest. Liver Physiol. 280:G178-G183.
    • (2001) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.280
    • Pothoulakis, C.1    Lamont, J.T.2
  • 23
  • 24
    • 0034877223 scopus 로고    scopus 로고
    • pH-enhanced cytopathic effects of Clostridium sordellii lethal toxin
    • Qa'Dan, M., L. M. Spyres, and J. D. Ballard. 2001. pH-enhanced cytopathic effects of Clostridium sordellii lethal toxin. Infect. Immun. 69:5487-5493.
    • (2001) Infect. Immun. , vol.69 , pp. 5487-5493
    • Qa'Dan, M.1    Spyres, L.M.2    Ballard, J.D.3
  • 25
    • 0034114105 scopus 로고    scopus 로고
    • pH-induced conformational changes in Clostridium difficile toxin B
    • Qa'Dan, M., L. M. Spyres, and J. D. Ballard. 2000. pH-induced conformational changes in Clostridium difficile toxin B. Infect. Immun. 68:2470-2474.
    • (2000) Infect. Immun. , vol.68 , pp. 2470-2474
    • Qa'Dan, M.1    Spyres, L.M.2    Ballard, J.D.3
  • 26
    • 0035957753 scopus 로고    scopus 로고
    • Dominant-negative mutants of a toxin subunit: An approach to therapy of anthrax
    • Sellman, B. R., M. Mourez, and R. J. Collier. 2001. Dominant-negative mutants of a toxin subunit: an approach to therapy of anthrax. Science 292:695-697.
    • (2001) Science , vol.292 , pp. 695-697
    • Sellman, B.R.1    Mourez, M.2    Collier, R.J.3
  • 27
    • 0035159221 scopus 로고    scopus 로고
    • Cytosolic delivery and characterization of the TcdB glucosylating domain by using a heterologous protein fusion
    • Spyres, L. M., M. Qa'Dan, A. Meader, J. J. Tomasek, E. W. Howard, and J. D. Ballard. 2001. Cytosolic delivery and characterization of the TcdB glucosylating domain by using a heterologous protein fusion. Infect. Immun. 69:599-601.
    • (2001) Infect. Immun. , vol.69 , pp. 599-601
    • Spyres, L.M.1    Qa'Dan, M.2    Meader, A.3    Tomasek, J.J.4    Howard, E.W.5    Ballard, J.D.6
  • 28
    • 0027931407 scopus 로고
    • Cells infected with Yersinia present an epitope to class I MHC-restricted CTL
    • Starnbach, M. N., and M. J. Bevan. 1994. Cells infected with Yersinia present an epitope to class I MHC-restricted CTL. J. Immunol. 153:1603-1612.
    • (1994) J. Immunol. , vol.153 , pp. 1603-1612
    • Starnbach, M.N.1    Bevan, M.J.2
  • 30
    • 0030740519 scopus 로고    scopus 로고
    • Delineation of the catalytic domain of Clostridium difficile toxin B-10463 to an enzymatically active N-terminal 467 amino acid fragment
    • Wagenknecht-Wiesner, A., M. Weidmann, V. Braun, P. Leukel, M. Moos, and C. von Eichel-Streiber. 1997. Delineation of the catalytic domain of Clostridium difficile toxin B-10463 to an enzymatically active N-terminal 467 amino acid fragment. FEMS Microbiol. Lett. 152:109-116.
    • (1997) FEMS Microbiol. Lett. , vol.152 , pp. 109-116
    • Wagenknecht-Wiesner, A.1    Weidmann, M.2    Braun, V.3    Leukel, P.4    Moos, M.5    Von Eichel-Streiber, C.6
  • 31
    • 17344374072 scopus 로고    scopus 로고
    • Soluble expression and one-step purification of recombinant Bacillus anthracis protective antigen
    • Whilhite, D. C., and S. R. Blanke. 1998. Soluble expression and one-step purification of recombinant Bacillus anthracis protective antigen. Protein Pept. Lett. 5:273-278.
    • (1998) Protein Pept. Lett. , vol.5 , pp. 273-278
    • Whilhite, D.C.1    Blanke, S.R.2


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