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Volumn 134, Issue 7, 2008, Pages 2049-2058

Human α-Defensins Inhibit Clostridium difficile Toxin B

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA DEFENSIN; BETA DEFENSIN 1; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CELL PROTEIN; CLOSTRIDIUM DIFFICILE TOXIN A; CLOSTRIDIUM DIFFICILE TOXIN B; HUMAN NEUTROPHIL PROTEIN 1; HUMAN NEUTROPHIL PROTEIN 2; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; URIDINE DIPHOSPHATE GLUCOSE;

EID: 44649117522     PISSN: 00165085     EISSN: None     Source Type: Journal    
DOI: 10.1053/j.gastro.2008.03.008     Document Type: Article
Times cited : (102)

References (32)
  • 1
    • 28844460476 scopus 로고    scopus 로고
    • The new Clostridium difficile-what does it mean?
    • Bartlett J.G., and Perl T.M. The new Clostridium difficile-what does it mean?. N Engl J Med 353 (2005) 2503-2505
    • (2005) N Engl J Med , vol.353 , pp. 2503-2505
    • Bartlett, J.G.1    Perl, T.M.2
  • 2
    • 0018075343 scopus 로고
    • Role of Clostridium difficile in antibiotic-associated pseudomembranous colitis
    • Bartlett J.G., Moon N., Chang T.W., et al. Role of Clostridium difficile in antibiotic-associated pseudomembranous colitis. Gastroenterology 75 (1978) 778-782
    • (1978) Gastroenterology , vol.75 , pp. 778-782
    • Bartlett, J.G.1    Moon, N.2    Chang, T.W.3
  • 3
    • 0031958706 scopus 로고    scopus 로고
    • Clostridium difficile infection
    • Kelly C.P., and LaMont J.T. Clostridium difficile infection. Annu Rev Med 49 (1998) 375-390
    • (1998) Annu Rev Med , vol.49 , pp. 375-390
    • Kelly, C.P.1    LaMont, J.T.2
  • 4
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins: mechanism of action and role in disease
    • Voth D.E., and Ballard J.D. Clostridium difficile toxins: mechanism of action and role in disease. Clin Microbiol Rev 18 (2005) 247-263
    • (2005) Clin Microbiol Rev , vol.18 , pp. 247-263
    • Voth, D.E.1    Ballard, J.D.2
  • 6
    • 0033926830 scopus 로고    scopus 로고
    • Cytotoxic effects of the Clostridium difficile toxins
    • Thelestam M., and Chaves-Olarte E. Cytotoxic effects of the Clostridium difficile toxins. Curr Top Microbiol Immunol 250 (2000) 85-96
    • (2000) Curr Top Microbiol Immunol , vol.250 , pp. 85-96
    • Thelestam, M.1    Chaves-Olarte, E.2
  • 7
    • 34547626991 scopus 로고    scopus 로고
    • Clostridium difficile toxins A and B directly stimulate human mast cells
    • Meyer G.K., Neetz A., Brandes G., et al. Clostridium difficile toxins A and B directly stimulate human mast cells. Infect Immun 75 (2007) 3868-3876
    • (2007) Infect Immun , vol.75 , pp. 3868-3876
    • Meyer, G.K.1    Neetz, A.2    Brandes, G.3
  • 8
    • 0037657907 scopus 로고    scopus 로고
    • Human intestinal epithelial and smooth muscle cells are potent producers of IL-6
    • Ng E.K., Panesar N., Longo W.E., et al. Human intestinal epithelial and smooth muscle cells are potent producers of IL-6. Mediators Inflamm 12 (2003) 3-8
    • (2003) Mediators Inflamm , vol.12 , pp. 3-8
    • Ng, E.K.1    Panesar, N.2    Longo, W.E.3
  • 9
    • 28044441113 scopus 로고    scopus 로고
    • Human mucosa/submucosa interactions during intestinal inflammation: involvement of the enteric nervous system in interleukin-8 secretion
    • Tixier E., Lalanne F., Just I., et al. Human mucosa/submucosa interactions during intestinal inflammation: involvement of the enteric nervous system in interleukin-8 secretion. Cell Microbiol 7 (2005) 1798-1810
    • (2005) Cell Microbiol , vol.7 , pp. 1798-1810
    • Tixier, E.1    Lalanne, F.2    Just, I.3
  • 10
    • 19044386605 scopus 로고    scopus 로고
    • The role of leukotriene B4 in Clostridium difficile toxin A-induced ileitis in rats
    • McVey D.C., and Vigna S.R. The role of leukotriene B4 in Clostridium difficile toxin A-induced ileitis in rats. Gastroenterology 128 (2005) 1306-1316
    • (2005) Gastroenterology , vol.128 , pp. 1306-1316
    • McVey, D.C.1    Vigna, S.R.2
  • 11
    • 1342345853 scopus 로고    scopus 로고
    • Essential involvement of IFN-gamma in Clostridium difficile toxin A-induced enteritis
    • Ishida Y., Maegawa T., Kondo T., et al. Essential involvement of IFN-gamma in Clostridium difficile toxin A-induced enteritis. J Immunol 172 (2004) 3018-3025
    • (2004) J Immunol , vol.172 , pp. 3018-3025
    • Ishida, Y.1    Maegawa, T.2    Kondo, T.3
  • 12
    • 33845329838 scopus 로고    scopus 로고
    • Defensins and cathelicidins in gastrointestinal infections
    • Wehkamp J., Schauber J., and Stange E.F. Defensins and cathelicidins in gastrointestinal infections. Curr Opin Gastroenterol 23 (2007) 32-38
    • (2007) Curr Opin Gastroenterol , vol.23 , pp. 32-38
    • Wehkamp, J.1    Schauber, J.2    Stange, E.F.3
  • 14
    • 29144521244 scopus 로고    scopus 로고
    • Human antimicrobial peptides: defensins, cathelicidins and histatins
    • De S.K., and Contreras R. Human antimicrobial peptides: defensins, cathelicidins and histatins. Biotechnol Lett 27 (2005) 1337-1347
    • (2005) Biotechnol Lett , vol.27 , pp. 1337-1347
    • De, S.K.1    Contreras, R.2
  • 15
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 16
    • 33748569152 scopus 로고    scopus 로고
    • Defensin: a multifunctional molecule lives up to its versatile name
    • Kim C., and Kaufmann S.H. Defensin: a multifunctional molecule lives up to its versatile name. Trends Microbiol 14 (2006) 428-431
    • (2006) Trends Microbiol , vol.14 , pp. 428-431
    • Kim, C.1    Kaufmann, S.H.2
  • 17
    • 35348940762 scopus 로고    scopus 로고
    • Defensins and Paneth cells in inflammatory bowel disease
    • Shi J. Defensins and Paneth cells in inflammatory bowel disease. Inflamm Bowel Dis 13 (2007) 1284-1292
    • (2007) Inflamm Bowel Dis , vol.13 , pp. 1284-1292
    • Shi, J.1
  • 18
    • 16344366178 scopus 로고    scopus 로고
    • Human alpha-defensins neutralize anthrax lethal toxin and protect against its fatal consequences
    • Kim C., Gajendran N., Mittrucker H.W., et al. Human alpha-defensins neutralize anthrax lethal toxin and protect against its fatal consequences. Proc Natl Acad Sci U S A 102 (2005) 4830-4835
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 4830-4835
    • Kim, C.1    Gajendran, N.2    Mittrucker, H.W.3
  • 19
    • 33749989623 scopus 로고    scopus 로고
    • Human alpha-defensins neutralize toxins of the mono-ADP-ribosyltransferase family
    • Kim C., Slavinskaya Z., Merrill A.R., et al. Human alpha-defensins neutralize toxins of the mono-ADP-ribosyltransferase family. Biochem J 399 (2006) 225-229
    • (2006) Biochem J , vol.399 , pp. 225-229
    • Kim, C.1    Slavinskaya, Z.2    Merrill, A.R.3
  • 21
    • 0023388361 scopus 로고
    • Purification of Clostridium difficile toxin A by affinity chromatography on immobilized thyroglobulin
    • Krivan H.C., and Wilkins T.D. Purification of Clostridium difficile toxin A by affinity chromatography on immobilized thyroglobulin. Infect Immun 55 (1987) 1873-1877
    • (1987) Infect Immun , vol.55 , pp. 1873-1877
    • Krivan, H.C.1    Wilkins, T.D.2
  • 22
    • 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., Busch C., Prepens U., et al. Localization of the glucosyltransferase activity of Clostridium difficile toxin B to the N-terminal part of the holotoxin. J Biol Chem 272 (1997) 11074-11078
    • (1997) J Biol Chem , vol.272 , pp. 11074-11078
    • Hofmann, F.1    Busch, C.2    Prepens, U.3
  • 23
    • 0029011449 scopus 로고
    • The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins
    • Just I., Wilm M., Selzer J., et al. The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins. J Biol Chem 270 (1995) 13932-13936
    • (1995) J Biol Chem , vol.270 , pp. 13932-13936
    • Just, I.1    Wilm, M.2    Selzer, J.3
  • 24
    • 33646942752 scopus 로고    scopus 로고
    • Cellular stability of Rho-GTPases glucosylated by Clostridium difficile toxin B
    • Genth H., Huelsenbeck J., Hartmann B., et al. Cellular stability of Rho-GTPases glucosylated by Clostridium difficile toxin B. FEBS Lett 580 (2006) 3565-3569
    • (2006) FEBS Lett , vol.580 , pp. 3565-3569
    • Genth, H.1    Huelsenbeck, J.2    Hartmann, B.3
  • 25
    • 34548472183 scopus 로고    scopus 로고
    • Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on a cysteine protease activity
    • Egerer M., Giesemann T., Jank T., et al. Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on a cysteine protease activity. J Biol Chem 282 (2007) 25314-25321
    • (2007) J Biol Chem , vol.282 , pp. 25314-25321
    • Egerer, M.1    Giesemann, T.2    Jank, T.3
  • 26
    • 0036079594 scopus 로고    scopus 로고
    • Paneth cell trypsin is the processing enzyme for human defensin-5
    • Ghosh D., Porter E., Shen B., et al. Paneth cell trypsin is the processing enzyme for human defensin-5. Nat Immunol 3 (2002) 583-590
    • (2002) Nat Immunol , vol.3 , pp. 583-590
    • Ghosh, D.1    Porter, E.2    Shen, B.3
  • 27
    • 0022471026 scopus 로고
    • Isolation of Clostridium difficile from human jejunum: identification of a reservoir for disease?
    • Testore G.P., Nardi F., Babudieri S., et al. Isolation of Clostridium difficile from human jejunum: identification of a reservoir for disease?. J Clin Pathol 39 (1986) 861-862
    • (1986) J Clin Pathol , vol.39 , pp. 861-862
    • Testore, G.P.1    Nardi, F.2    Babudieri, S.3
  • 28
    • 0021995801 scopus 로고
    • Effects of Clostridium difficile toxins given intragastrically to animals
    • Lyerly D.M., Saum K.E., MacDonald D.K., et al. Effects of Clostridium difficile toxins given intragastrically to animals. Infect Immun 47 (1985) 349-352
    • (1985) Infect Immun , vol.47 , pp. 349-352
    • Lyerly, D.M.1    Saum, K.E.2    MacDonald, D.K.3
  • 29
    • 0141528564 scopus 로고    scopus 로고
    • High frequency of antibiotic associated diarrhea due to toxin A-negative, toxin B-positive Clostridium difficile in a hospital in Japan and risk factors for infection
    • Komatsu M., Kato H., Aihara M., et al. High frequency of antibiotic associated diarrhea due to toxin A-negative, toxin B-positive Clostridium difficile in a hospital in Japan and risk factors for infection. Eur J Clin Microbiol Infect Dis 22 (2003) 525-529
    • (2003) Eur J Clin Microbiol Infect Dis , vol.22 , pp. 525-529
    • Komatsu, M.1    Kato, H.2    Aihara, M.3
  • 30
    • 0043167963 scopus 로고    scopus 로고
    • Clostridium difficile toxin B is an inflammatory enterotoxin in human intestine
    • Savidge T.C., Pan W.-H., Newman P., et al. Clostridium difficile toxin B is an inflammatory enterotoxin in human intestine. Gastroenterology 125 (2003) 413-420
    • (2003) Gastroenterology , vol.125 , pp. 413-420
    • Savidge, T.C.1    Pan, W.-H.2    Newman, P.3
  • 31
    • 1542723582 scopus 로고    scopus 로고
    • Characterization of toxin A-negative, toxin B-positive Clostridium difficile isolates from outbreaks in different countries by amplified fragment length polymorphism and PCR ribotyping
    • van den Berg R.J., Claas E.C., Oyib D.H., et al. Characterization of toxin A-negative, toxin B-positive Clostridium difficile isolates from outbreaks in different countries by amplified fragment length polymorphism and PCR ribotyping. J Clin Microbiol 42 (2004) 1035-1041
    • (2004) J Clin Microbiol , vol.42 , pp. 1035-1041
    • van den Berg, R.J.1    Claas, E.C.2    Oyib, D.H.3
  • 32
    • 0036070029 scopus 로고    scopus 로고
    • High prevalence of toxin A-negative toxin B-positive Clostridium difficile in hospitalized patients with gastrointestinal disease
    • Samra Z., Talmor S., and Bahar J. High prevalence of toxin A-negative toxin B-positive Clostridium difficile in hospitalized patients with gastrointestinal disease. Diagn Microbiol Infect Dis 43 (2002) 189-192
    • (2002) Diagn Microbiol Infect Dis , vol.43 , pp. 189-192
    • Samra, Z.1    Talmor, S.2    Bahar, J.3


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