Binding and entry of Clostridium difficile toxin B is mediated by multiple domains

FEBS Letters

Volumn 589, Issue 24, 2015, Pages 3945-3951

  Manse, Jared S ^a   Baldwin, Michael R ^a  

^a University of Missouri   (United States)

Author keywords

Binding; Clostridium difficile; Clostridium difficile toxin B; Combined repetitive oligopeptide; Modular binding motif (MBM); Toxicity

Indexed keywords

CLOSTRIDIUM DIFFICILE TOXIN B; GLYCOPROTEIN; POLIOVIRUS RECEPTOR LIKE 3 PROTEIN; UNCLASSIFIED DRUG; BACTERIAL TOXIN; CELL ADHESION MOLECULE; CLOSTRIDIUM DIFFICILE LETHAL TOXIN B; HYBRID PROTEIN; NECTINS; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN;

ANIMAL CELL; ARTICLE; CELL TRANSPORT; CONTROLLED STUDY; CYTOTOXICITY; FEMALE; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; INTERNALIZATION; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN TRANSPORT; RESIDUE ANALYSIS; TOXIN ANALYSIS; ABSORPTION; AMINO ACID SEQUENCE; ANIMAL; CELL SURVIVAL; CHEMICAL STRUCTURE; CHEMISTRY; CHLOROCEBUS AETHIOPS; CHO CELL LINE; CRICETULUS; DRUG EFFECTS; GENE DELETION; GENETICS; METABOLISM; PEPTOCLOSTRIDIUM DIFFICILE; TRANSPORT AT THE CELLULAR LEVEL; TUMOR CELL LINE; VERO CELL LINE;

ABSORPTION, PHYSIOLOGICAL; ANIMALS; BACTERIAL TOXINS; BIOLOGICAL TRANSPORT; CELL ADHESION MOLECULES; CELL LINE, TUMOR; CELL SURVIVAL; CERCOPITHECUS AETHIOPS; CHO CELLS; CLOSTRIDIUM DIFFICILE; CRICETULUS; GENE DELETION; HUMANS; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN INTERACTION DOMAINS AND MOTIFS; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; REPETITIVE SEQUENCES, AMINO ACID; VERO CELLS;

EID: 84955254203     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.11.017     Document Type: Article

References (26)

1. S.R. Eaton, J.E. Mazuski, Overview of severe Clostridium difficile infection. Crit. Care Clin., 29, (2013), 827-839.
2. D. Lyras, Toxin B is essential for virulence of Clostridium difficile. Nature, 458, (2009), 1176-1179.
3. S.H. Cohen, Y.J. Tang, B. Hansen, J. Silva Jr., Isolation of a toxin B-deficient mutant strain of Clostridium difficile in a case of recurrent C. difficile-associated diarrhea. Clin. Infect. Dis., 26, (1998), 410-412.
4. C. von Eichel-Streiber, P. Boquet, M. Sauerborn, M. Thelestam, Large clostridial cytotoxins-a family of glycosyltransferases modifying small GTP-binding proteins. Trends Microbiol., 4, (1996), 375-382.
5. T. Jank, K. Aktories, Structure and mode of action of clostridial glucosylating toxins: the ABCD model. Trends Microbiol., 16, (2008), 222-229.
6. K. Wohlan, S. Goy, A. Olling, S. Srivaratharajan, H. Tatge, H. Genth, R. Gerhard, Pyknotic cell death induced by Clostridium difficile TcdB: chromatin condensation and nuclear blister are induced independently of the glucosyltransferase activity. Cell. Microbiol., (2014)
7. R.N. Pruitt, D.B. Lacy, Toward a structural understanding of Clostridium difficile toxins A and B. Front. Cell. Infect. Microbiol., 2, (2012), 28 -
8. S. Genisyuerek, P. Papatheodorou, G. Guttenberg, R. Schubert, R. Benz, K. Aktories, Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B. Mol. Microbiol., 79, (2011), 1643-1654.
9. B. Schorch, LRP1 is a receptor for Clostridium perfringens TpeL toxin indicating a two-receptor model of clostridial glycosylating toxins. Proc. Natl. Acad. Sci. U.S.A., 111, (2014), 6431-6436.
10. L.A. Barroso, J.S. Moncrief, D.M. Lyerly, T.D. Wilkins, Mutagenesis of the Clostridium difficile toxin B gene and effect on cytotoxic activity. Microb. Pathog., 16, (1994), 297-303.
11. A. Olling, S. Goy, F. Hoffmann, H. Tatge, I. Just, R. Gerhard, The repetitive oligopeptide sequences modulate cytopathic potency but are not crucial for cellular uptake of Clostridium difficile toxin A. PLoS ONE, 6, (2011), e17623 -
12. R. Gerhard, E. Frenzel, S. Goy, A. Olling, Cellular uptake of Clostridium difficile TcdA and truncated TcdA lacking the receptor binding domain. J. Med. Microbiol., 62, (2013), 1414-1422.
13. Z. Zhang, M. Park, J. Tam, A. Auger, G.L. Beilhartz, D.B. Lacy, R.A. Melnyk, Translocation domain mutations affecting cellular toxicity identify the Clostridium difficile toxin B pore, in: Proceedings of the National Academy of Sciences of the United States of America, 2014.
14. R.N. Pruitt, M.G. Chambers, K.K. Ng, M.D. Ohi, D.B. Lacy, Structural organization of the functional domains of Clostridium difficile toxins A and B. Proc. Natl. Acad. Sci. U.S.A., 107, (2010), 13467-13472.
15. P. Yuan, Chondroitin sulfate proteoglycan 4 functions as the cellular receptor for Clostridium difficile toxin B. Cell Res., 25, (2015), 157-168.
16. M.E. LaFrance, M.A. Farrow, R. Chandrasekaran, J. Sheng, D.H. Rubin, D.B. Lacy, Identification of an epithelial cell receptor responsible for Clostridium difficile TcdB-induced cytotoxicity. Proc. Natl. Acad. Sci. U.S.A., 112, (2015), 7073-7078.
17. N.M. Chumbler, M.A. Farrow, L.A. Lapierre, J.L. Franklin, D.B. Haslam, J.R. Goldenring, D.B. Lacy, Clostridium difficile Toxin B causes epithelial cell necrosis through an autoprocessing-independent mechanism. PLoS Pathog., 8, (2012), e1003072 -
18. S.D. Goy, A. Olling, D. Neumann, A. Pich, R. Gerhard, Human neutrophils are activated by a peptide fragment of Clostridium difficile toxin B presumably via formyl peptide receptor. Cell. Microbiol., 17, (2015), 893-909.
19. T. Dingle, Functional properties of the carboxy-terminal host cell-binding domains of the two toxins, TcdA and TcdB, expressed by Clostridium difficile. Glycobiology, 18, (2008), 698-706.
20. A. El-Hawiet, Binding of Clostridium difficile toxins to human milk oligosaccharides. Glycobiology, 21, (2011), 1217-1227.
21. I. Just, J. Selzer, M. Wilm, C.V. Eichel-Streiber, M. Mann, K. Aktories, Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature, 375, (1995), 500-503.
22. F. Hofmann, C. Busch, U. Prepens, I. Just, K. Aktories, 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.
23. M. Egerer, T. Giesemann, T. Jank, K.J. Satchell, K. Aktories, Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity. J. Biol. Chem., 282, (2007), 25314-25321.
24. J. Reineke, S. Tenzer, M. Rupnik, A. Koschinski, O. Hasselmayer, A. Schrattenholz, H. Schild, C. von Eichel-Streiber, Autocatalytic cleavage of Clostridium difficile toxin B. Nature, 446, (2007), 415-419.
25. S. Li, L. Shi, Z. Yang, H. Feng, 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, (2013), 11-18.
26. P. Papatheodorou, C. Zamboglou, S. Genisyuerek, G. Guttenberg, K. Aktories, Clostridial glucosylating toxins enter cells via clathrin-mediated endocytosis. PLoS ONE, 5, (2010), e10673 -