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Volumn 159, Issue PART7, 2013, Pages 1254-1266

A novel approach to generate a recombinant toxoid vaccine against Clostridium difficile

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL VACCINE; BACTERIUM LYSATE; CHLORAMPHENICOL ACETYLTRANSFERASE; CLOSTRIDIUM DIFFICILE TOXIN A; CLOSTRIDIUM DIFFICILE TOXIN B; CLOSTRIDIUM DIFFICILE TOXOID A; CLOSTRIDIUM DIFFICILE TOXOID B; GLUCOSYLTRANSFERASE; RECOMBINANT VACCINE; TOXIN ANTIBODY; TOXOID; UNCLASSIFIED DRUG;

EID: 84879819430     PISSN: 13500872     EISSN: 14652080     Source Type: Journal    
DOI: 10.1099/mic.0.066712-0     Document Type: Article
Times cited : (78)

References (40)
  • 2
    • 0035815642 scopus 로고    scopus 로고
    • Low pH-induced formation of ion channels by Clostridium difficile toxin B in target cells
    • Barth, H., Pfeifer, G., Hofmann, F., Maier, E., Benz, R. & Aktories, K. (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
  • 3
    • 0030605226 scopus 로고    scopus 로고
    • Definition of the single integration site of the pathogenicity locus in Clostridium difficile
    • Braun, V., Hundsberger, T., Leukel, P., Sauerborn, M. & von Eichel-Streiber, C. (1996). Definition of the single integration site of the pathogenicity locus in Clostridium difficile. Gene 181, 29-38.
    • (1996) Gene , vol.181 , pp. 29-38
    • Braun, V.1    Hundsberger, T.2    Leukel, P.3    Sauerborn, M.4    von Eichel-Streiber, C.5
  • 4
    • 0032584665 scopus 로고    scopus 로고
    • A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins
    • Busch, C., Hofmann, F., Selzer, J., Munro, S., Jeckel, D. & Aktories, K. (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
  • 7
    • 34548472183 scopus 로고    scopus 로고
    • Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity
    • Egerer, M., Giesemann, T., Jank, T., Satchell, K. J. F. & Aktories, K. (2007). Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity. J Biol Chem 282, 25314-25321.
    • (2007) J Biol Chem , vol.282 , pp. 25314-25321
    • Egerer, M.1    Giesemann, T.2    Jank, T.3    Satchell, K.J.F.4    Aktories, K.5
  • 8
    • 69449083997 scopus 로고    scopus 로고
    • Production of Clostridium difficile toxin in a medium totally free of both animal and dairy proteins or digests
    • Fang, A., Gerson, D. F. & Demain, A. L. (2009). Production of Clostridium difficile toxin in a medium totally free of both animal and dairy proteins or digests. Proc Natl Acad Sci U S A 106, 13225-13229.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13225-13229
    • Fang, A.1    Gerson, D.F.2    Demain, A.L.3
  • 9
    • 79952418425 scopus 로고    scopus 로고
    • Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B
    • Genisyuerek, S., Papatheodorou, P., Guttenberg, G., Schubert, R., Benz, R. & Aktories, K. (2011). Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B. Mol Microbiol 79, 1643-1654.
    • (2011) Mol Microbiol , vol.79 , pp. 1643-1654
    • Genisyuerek, S.1    Papatheodorou, P.2    Guttenberg, G.3    Schubert, R.4    Benz, R.5    Aktories, K.6
  • 10
    • 45249093628 scopus 로고    scopus 로고
    • Glucosylation of Rho GTPases by Clostridium difficile toxin A triggers apoptosis in intestinal epithelial cells
    • Gerhard, R., Nottrott, S., Schoentaube, J., Tatge, H., Olling, A. & Just, I. (2008). Glucosylation of Rho GTPases by Clostridium difficile toxin A triggers apoptosis in intestinal epithelial cells. J Med Microbiol 57, 765-770.
    • (2008) J Med Microbiol , vol.57 , pp. 765-770
    • Gerhard, R.1    Nottrott, S.2    Schoentaube, J.3    Tatge, H.4    Olling, A.5    Just, I.6
  • 12
    • 2442420091 scopus 로고    scopus 로고
    • Prevalence and characterization of a binary toxin (actin-specific ADP-ribosyltransferase) from Clostridium difficile
    • Gonçalves, C., Decré, D., Barbut, F., Burghoffer, B. & Petit, J.-C. (2004). Prevalence and characterization of a binary toxin (actin-specific ADP-ribosyltransferase) from Clostridium difficile. J Clin Microbiol 42, 1933-1939.
    • (2004) J Clin Microbiol , vol.42 , pp. 1933-1939
    • Gonçalves, C.1    Decré, D.2    Barbut, F.3    Burghoffer, B.4    Petit, J.-C.5
  • 13
    • 84864073540 scopus 로고    scopus 로고
    • Secretion of Clostridium difficile toxins A and B requires the holin-like protein TcdE
    • Govind, R. & Dupuy, B. (2012). Secretion of Clostridium difficile toxins A and B requires the holin-like protein TcdE. PLoS Pathog 8, e1002727.
    • (2012) PLoS Pathog , vol.8
    • Govind, R.1    Dupuy, B.2
  • 17
    • 15544377092 scopus 로고    scopus 로고
    • Generation of an erythromycin-sensitive derivative of Clostridium difficile strain 630 (630Derm) and demonstration that the conjugative transposon Tn916DE enters the genome of this strain at multiple sites
    • Hussain, H. A., Roberts, A. P. & Mullany, P. (2005). Generation of an erythromycin-sensitive derivative of Clostridium difficile strain 630 (630Derm) and demonstration that the conjugative transposon Tn916DE enters the genome of this strain at multiple sites. J Med Microbiol 54, 137-141.
    • (2005) J Med Microbiol , vol.54 , pp. 137-141
    • Hussain, H.A.1    Roberts, A.P.2    Mullany, P.3
  • 18
    • 42749095602 scopus 로고    scopus 로고
    • Structure and mode of action of clostridial glucosylating toxins: The ABCD model
    • Jank, T. & Aktories, K. (2008). Structure and mode of action of clostridial glucosylating toxins: the ABCD model. Trends Microbiol 16, 222-229.
    • (2008) Trends Microbiol , vol.16 , pp. 222-229
    • Jank, T.1    Aktories, K.2
  • 19
    • 33947260554 scopus 로고    scopus 로고
    • Rho-glucosylating Clostridium difficile toxins A and B: New insights into structure and function
    • Jank, T., Giesemann, T. & Aktories, K. (2007a). Rho-glucosylating Clostridium difficile toxins A and B: new insights into structure and function. Glycobiology 17, 15R-22R.
    • (2007) Glycobiology , vol.17
    • Jank, T.1    Giesemann, T.2    Aktories, K.3
  • 20
    • 36849050145 scopus 로고    scopus 로고
    • Clostridium difficile glucosyltransferase toxin B-essential amino acids for substrate binding
    • Jank, T., Giesemann, T. & Aktories, K. (2007b). Clostridium difficile glucosyltransferase toxin B-essential amino acids for substrate binding. J Biol Chem 282, 35222-35231.
    • (2007) J Biol Chem , vol.282 , pp. 35222-35231
    • Jank, T.1    Giesemann, T.2    Aktories, K.3
  • 21
    • 79960133978 scopus 로고    scopus 로고
    • The xCELLigence system for real-time and label-free monitoring of cell viability
    • Ke, N., Wang, X., Xu, X. & Abassi, Y. A. (2011). The xCELLigence system for real-time and label-free monitoring of cell viability. Methods Mol Biol 740, 33-43.
    • (2011) Methods Mol Biol , vol.740 , pp. 33-43
    • Ke, N.1    Wang, X.2    Xu, X.3    Abassi, Y.A.4
  • 23
    • 84878122416 scopus 로고    scopus 로고
    • Cytotoxicity of Clostridium difficile toxin B does not require cysteine protease-mediated autocleavage and release of the glucosyltransferase domain into the host cell cytosol
    • Li, S., Shi, L., Yang, Z. & Feng, H. (2013). Cytotoxicity of Clostridium difficile toxin B does not require cysteine protease-mediated autocleavage and release of the glucosyltransferase domain into the host cell cytosol. Pathog Dis 67, 11-18.
    • (2013) Pathog Dis , vol.67 , pp. 11-18
    • Li, S.1    Shi, L.2    Yang, Z.3    Feng, H.4
  • 24
    • 0020029308 scopus 로고
    • Effects of the two toxins of Clostridium difficile in antibiotic-associated cecitis in hamsters
    • Libby, J. M., Jortner, B. S. & Wilkins, T. D. (1982). Effects of the two toxins of Clostridium difficile in antibiotic-associated cecitis in hamsters. Infect Immun 36, 822-829.
    • (1982) Infect Immun , vol.36 , pp. 822-829
    • Libby, J.M.1    Jortner, B.S.2    Wilkins, T.D.3
  • 27
    • 0021995801 scopus 로고
    • Effects of Clostridium difficile toxins given intragastrically to animals
    • Lyerly, D. M., Saum, K. E., MacDonald, D. K. & Wilkins, T. D. (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
  • 29
    • 67649391053 scopus 로고    scopus 로고
    • Clostridium difficile infection: New developments in epidemiology and pathogenesis
    • Rupnik, M., Wilcox, M. H. & Gerding, D. N. (2009). Clostridium difficile infection: new developments in epidemiology and pathogenesis. Nat Rev Microbiol 7, 526-536.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 526-536
    • Rupnik, M.1    Wilcox, M.H.2    Gerding, D.N.3
  • 31
    • 0037115014 scopus 로고    scopus 로고
    • Colonization for the prevention of Clostridium difficile disease in hamsters
    • Sambol, S. P., Merrigan, M. M., Tang, J. K., Johnson, S. & Gerding, D. N. (2002). Colonization for the prevention of Clostridium difficile disease in hamsters. J Infect Dis 186, 1781-1789.
    • (2002) J Infect Dis , vol.186 , pp. 1781-1789
    • Sambol, S.P.1    Merrigan, M.M.2    Tang, J.K.3    Johnson, S.4    Gerding, D.N.5
  • 35
    • 15944418972 scopus 로고    scopus 로고
    • Molecular insights into the initiation of sporulation in Gram-positive bacteria: New technologies for an old phenomenon
    • Stephenson, K. & Lewis, R. J. (2005). Molecular insights into the initiation of sporulation in Gram-positive bacteria: new technologies for an old phenomenon. FEMS Microbiol Rev 29, 281-301.
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 281-301
    • Stephenson, K.1    Lewis, R.J.2
  • 36
    • 33749257130 scopus 로고    scopus 로고
    • Application of mutated Clostridium difficile toxin A for determination of glucosyltransferase-dependent effects
    • Teichert, M., Tatge, H., Schoentaube, J., Just, I. & Gerhard, R. (2006). Application of mutated Clostridium difficile toxin A for determination of glucosyltransferase-dependent effects. Infect Immun 74, 6006-6010.
    • (2006) Infect Immun , vol.74 , pp. 6006-6010
    • Teichert, M.1    Tatge, H.2    Schoentaube, J.3    Just, I.4    Gerhard, R.5
  • 37
    • 71749105366 scopus 로고    scopus 로고
    • Characterization of the sporulation initiation pathway of Clostridium difficile and its role in toxin production
    • Underwood, S., Guan, S., Vijayasubhash, V., Baines, S. D., Graham, L., Lewis, R. J., Wilcox, M. H. & Stephenson, K. (2009). Characterization of the sporulation initiation pathway of Clostridium difficile and its role in toxin production. J Bacteriol 191, 7296-7305.
    • (2009) J Bacteriol , vol.191 , pp. 7296-7305
    • Underwood, S.1    Guan, S.2    Vijayasubhash, V.3    Baines, S.D.4    Graham, L.5    Lewis, R.J.6    Wilcox, M.H.7    Stephenson, K.8
  • 39
    • 84856978972 scopus 로고    scopus 로고
    • Fidaxomicin for the treatment of Clostridium difficile infections
    • Whitman, C. B. & Czosnowski, Q. A. (2012). Fidaxomicin for the treatment of Clostridium difficile infections. Ann Pharmacother 46, 219-228.
    • (2012) Ann Pharmacother , vol.46 , pp. 219-228
    • Whitman, C.B.1    Czosnowski, Q.A.2
  • 40
    • 77957019627 scopus 로고    scopus 로고
    • Repetitive domain of Clostridium difficile toxin B exhibits cytotoxic effects on human intestinal epithelial cells and decreases epithelial barrier function
    • Zemljic, M., Rupnik, M., Scarpa, M., Anderluh, G., Palù, G. & Castagliuolo, I. (2010). Repetitive domain of Clostridium difficile toxin B exhibits cytotoxic effects on human intestinal epithelial cells and decreases epithelial barrier function. Anaerobe 16, 527-532.
    • (2010) Anaerobe , vol.16 , pp. 527-532
    • Zemljic, M.1    Rupnik, M.2    Scarpa, M.3    Anderluh, G.4    Palù, G.5    Castagliuolo, I.6


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