Autocatalytic cleavage of Clostridium difficile toxin B

Nature

Volumn 446, Issue 7134, 2007, Pages 415-419

  Reineke, Jessica ^a   Tenzer, Stefan ^a   Rupnik, Maja ^b,c   Koschinski, Andreas ^d   Hasselmayer, Oliver ^a   Schrattenholz, André ^e   Schild, Hansjörg ^a   Von Eichel Streiber, Christoph ^a  

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

^b UNIVERSITY OF MARIBOR   (Slovenia)

^c Institute of Public Health Maribor   (Slovenia)

^d JUSTUS LIEBIG UNIVERSITY GIESSEN   (Germany)

^e PROTEOSYS AG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; CLOSTRIDIUM DIFFICILE TOXIN B; CYTOTOXIN; INOSITOL PHOSPHATE;

BACTERIUM; CATALYSIS; CLEAVAGE; DIARRHEAL DISEASE; ENZYME; INHIBITOR; MICROBIAL ACTIVITY; TOXIN; VIRULENCE;

ARTICLE; CATALYSIS; CELL CULTURE; CLOSTRIDIUM DIFFICILE; ENZYME ACTIVITY; EUKARYOTE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION;

BACTERIA (MICROORGANISMS); CLOSTRIDIUM DIFFICILE; EUKARYOTA;

ANIMALS; ASPARTIC ACID ENDOPEPTIDASES; BACTERIAL PROTEINS; BACTERIAL TOXINS; BINDING SITES; BIOLOGICAL FACTORS; CATALYSIS; CELL EXTRACTS; CELL LINE; CLOSTRIDIUM DIFFICILE; EPOXY COMPOUNDS; NITROPHENOLS; PHYTIC ACID; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN TRANSPORT; SPLEEN; SWINE; VIRULENCE FACTORS;

EID: 33947502604     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05622     Document Type: Article

References (46)

1. Tenover, F. C. Mechanisms of antimicrobial resistance in bacteria. Am. J. Infect. Control 34, S3-S10 (2006).
2. Fishman, N. Antimicrobial stewardship. Am. J. Infect. Control 34, S55-S63 (2006).
3. Bartlett, J. G., Chang, T. W., Gurwith, M., Gorbach, S. L. & Onderdonk, A. B. Antibiotic-associated pseudomembranous colitis due to toxin-producing Clostridia. N. Engl. J. Med. 298, 531-534 (1978).
4. George, R. H. et al. Identification of Clostridium difficile as a cause of pseudomembranous colitis. Br. Med. J. 1, 695 (1978).
5. Gorbach, S. L. Antibiotics and Clostridium difficile. N. Engl. J. Med. 341, 1690-1691 (1999).
6. Davey, P. et al. Systematic review of antimicrobial drug prescribing in hospitals. Emerg. Infect. Dis. 12, 211-216 (2006).
7. Lyerly, D. M., Krivan, H. C. & Wilkins, T. D. Clostridium difficile: its disease and toxins. Clin. Microbiol. Rev. 1, 1-18 (1988).
8. Voth, D. E. & Ballard, J. D. Clostridium difficile toxins: mechanism of action and role in disease. Clin. Microbiol. Rev. 18, 247-263 (2005).
9. Eichel-Streiber, C., Laufenberg-Feldmann, R., Sartingen, S., Schulze, J. & Sauerborn, M. Comparative sequence analysis of the Clostridium difficile toxins A and B. Mol. Gen. Genet. 233, 260-268 (1992).
10. Green, G. A., Schue, V. & Monteil, H. Cloning and characterization of the cytotoxin L-encoding gene of Clostridium sordellii: homology with Clostridium difficile cytotoxin B. Gene 161, 57-61 (1995).
11. Hofmann, F., Herrmann, A., Habermann, E. & Eichel-Streiber, C. Sequencing and analysis of the gene encoding the α-toxin of Clostridium novyi proves its homology to toxins A and B of Clostridium difficile. Mol. Gen. Genet. 247, 670-679 (1995).
12. Eichel-Streiber, C., Boquet, P., Sauerborn, M. & Thelestam, M. Large clostridial cytotoxins - a family of glycosyltransferases modifying small GTP-binding proteins. Trends Microbiol. 4, 375-382 (1996).
13. Rupnik, M. et al. Revised nomenclature of Clostridium difficile toxins and associated genes. J. Med. Microbiol. 54, 113-117 (2005).
14. Loo, V. G. et al. A predominantly clonal multi-institutional outbreak of Clostridium difficile-associated diarrhea with high morbidity and mortality. N. Engl. J. Med. 353, 2442-2449 (2005).
15. McDonald, L. C. et al. An epidemic, toxin gene-variant strain of Clostridium difficile. N. Engl. J. Med. 353, 2433-2441 (2005).
16. Centers for Disease Control and Prevention (CDC). Severe Clostridium difficile-associated disease in populations previously at low risk - four states, 2005. Morb. Mortal. Wkly Rep. 54, 1201-1205 (2005).
17. Kuijper, E. J., Coignard, B. & Tull, P. Emergence of Clostridium difficile-associated disease in North America and Europe. Clin. Microbiol. Infect. 12 (Suppl. 6), 2-18 (2006).
18. McDonald, L. C. Clostridium difficile: responding to a new threat from an old enemy. Infect. Control Hosp. Epidemiol. 26, 672-675 (2005).
19. Eichel-Streiber, C., Sauerborn, M. & Kuramitsu, H. K. Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus mutans glucosyltransferases. J. Bacteriol. 174, 6707-6710 (1992).
20. Pfeifer, G. et al. Cellular uptake of Clostridium difficile toxin B. Translocation of the N-terminal catalytic domain into the cytosol of eukaryotic cells. J. Biol. Chem. 278, 44535-44541 (2003).
21. Hofmann, F., Busch, C., Prepens, U., Just, I. & Aktories, K. 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).
22. Tucker, K. D. & Wilkins, T. D. Toxin A of Clostridium difficile binds to the human carbohydrate antigens I, X, and Y. Infect. Immun. 59, 73-78 (1991).
23. Karlsson, K. A. Microbial recognition of target-cell glycoconjugates. Curr. Opin. Struct. Biol. 5, 622-635 (1995).
24. Florin, I. & Thelestam, M. Internalization of Clostridium difficile cytotoxin into cultured human lung fibroblasts. Biochim. Biophys. Acta 763, 383-392 (1983).
25. Florin, I. & Thelestam, M. Lysosomal involvement in cellular intoxication with Clostridium difficile toxin B. Microb. Pathog. 1, 373-385 (1986).
26. Henriques, B., Florin, I. & Thelestam, M. Cellular internalisation of Clostridium difficile toxin A. Microb. Pathog. 2, 455-463 (1987).
27. Giesemann, T. et al. Cholesterol-dependent pore formation of Clostridium difficile toxin A. J. Biol. Chem. 281, 10808-10815 (2006).
28. Qa'Dan, M., Spyres, L. M. & Ballard, J. D. pH-induced conformational changes in Clostridium difficile toxin B. Infect. Immun. 68, 2470-2474 (2000).
29. Rupnik, M. et al. Characterization of the cleavage site and function of resulting cleavage fragments after limited proteolysis of Clostridium difficile toxin B (TcdB) by host cells. Microbiology 151, 199-208 (2005).
30. Sehr, P. et al. Glucosylation and ADP ribosylation of Rho proteins: effects on nucleotide binding, GTPase activity, and effector coupling. Biochemistry 37, 5296-5304 (1998).
31. Just, I. et al. Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature 375, 500-503 (1995).
32. Moos, M. & Eichel-Streiber, C. Purification and evaluation of large clostridial cytotoxins that inhibit small GTPases of Rho and Ras subfamilies. Methods Enzymol. 325, 114-125 (2000).
33. Hsu, F. F., Turk, J. & Gross, M. L. Structural distinction among inositol phosphate isomers using high-energy and low-energy collisional- activated dissociation tandem mass spectrometry with electrospray ionization. J. Mass Spectrom. 38, 447-457 (2003).
34. Fernandez-Patron, C., Hardy, E., Sosa, A., Seoane, J. & Castellanos, L. Double staining of Coomassie blue-stained polyacrylamide gels by imidazole-sodium dodecyl sulfate-zinc reverse staining: sensitive detection of Coomassie blue-undetected proteins. Anal. Biochem. 224, 263-269 (1995).
35. Shears, S. B. Assessing the omnipotence of inositol hexakisphosphate. Cell. Signal. 13, 151-158 (2001).
36. Saiardi, A., Bhandari, R., Resnick, A. C., Snowman, A. M. & Snyder, S. H. Phosphorylation of proteins by inositol pyrophosphates. Science 306, 2101-2105 (2004).
37. Sauerborn, M., Hegenbarth, S., Laufenberg-Feldmann, R., Leukel, P. & von Eichel-Streiber, C. Monoclonal antibodies discriminating between Clostridium difficile toxins A and B. Int. J. Med. Microbiol. 24 (Suppl.), 510-511 (1994).
38. Sebaihia, M. et al. The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome. Nature Genet. 38, 779-786 (2006).
39. Rao, M. B., Tanksale, A. M., Ghatge, M. S. & Deshpande, V. V. Molecular and biotechnological aspects of microbial proteases. Microbiol. Mol. Biol. Rev. 62, 597-635 (1998).
40. Just, I. & Gerhard, R. Large clostridial cytotoxins. Rev. Physiol. Biochem. Pharmacol. 152, 23-47 (2004).
41. Barth, H. et al. Low pH-induced formation of ion channels by Clostridium difficile toxin B in target cells. J. Biol. Chem. 276, 10670-10676 (2001).
42. Macbeth, M. R. et al. Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing. Science 309, 1534-1539 (2005).
43. 6 inhibits Ku mobility. Nucleic Acids Res. 32, 2776-2784 (2004).
44. York, J. D., Guo, S., Odom, A. R., Spiegelberg, B. D. & Stolz, L. E. An expanded view of inositol signaling. Adv. Enzyme Regul. 41, 57-71 (2001).
45. Braun, V. & von Eichel-Streiber, C. Virulence-associated mobile elements in Bacilli and Clostridia. In Pathogenicity Islands and Other Mobile Elements (American Society of Microbiology, Washington DC, 1999).
46. Braun, V., Hundsberger, T., Leukel, P., Sauerborn, M. & Eichel-Streiber, C. Definition of the single integration site of the pathogenicity locus in Clostridium difficile. Gene 181, 29-38 (1996).