Identification of a lambda toxin-negative Clostridium perfringens strain that processes and activates epsilon prototoxin intracellularly

Anaerobe

Volumn 18, Issue 5, 2012, Pages 546-552

  Harkness, Justine M ^a   Li, Jihong ^a   McClane, Bruce A ^a  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

Author keywords

Clostridium perfringens; Epsilon toxin; Toxin proteolytic processing

Indexed keywords

BACTERIAL TOXIN; EPSILON PROTOTOXIN; PROTEINASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BACTERIAL CELL; BACTERIUM IDENTIFICATION; CLOSTRIDIUM PERFRINGENS; CONTROLLED STUDY; CYTOLYSIS; CYTOTOXICITY TEST; GENOTYPE; NONHUMAN; PRIORITY JOURNAL; SUPERNATANT; TOXIN ANALYSIS; TOXIN SYNTHESIS;

ANIMALS; BACTERIAL TOXINS; CELL LINE; CELL SURVIVAL; CLOSTRIDIUM PERFRINGENS; DNA, BACTERIAL; DOGS; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; SEQUENCE ANALYSIS, DNA;

ANIMALIA; BACTERIA (MICROORGANISMS); CLOSTRIDIUM PERFRINGENS;

EID: 84867337992     PISSN: 10759964     EISSN: 10958274     Source Type: Journal    
DOI: 10.1016/j.anaerobe.2012.09.001     Document Type: Article

References (24)

1. Songer J.G. Clostridial enteric diseases of domestic animals. Clin Microbiol Rev 1996, 9(2):216-234.
2. McClane B.A., Uzal F.A., Miyakawa M.F., Lyerly D., Wilkins T. The enterotoxic clostridia. The prokaryotes: a handbook on the biology of bacteria 2006, 698-752. Springer-Verlag, NY. M. Dworkin, S. Falkow, E. Rosenburg, H. Schleifer, E. Stackebrandt (Eds.).
3. Daube G., Simon P., Limbourg B., Manteca C., Manil J., Kaeckenbeeck A. Typing of Clostridium perfringens by in vitro amplification of toxin genes. J Appl Bacteriol 1994, 77(6):650-655.
4. Uzal F.A., Kelly W.R., Morris W.E., Bermudez J., Baison M. The pathology of peracute experimental Clostridium perfringens type D enterotoxemia in sheep. J Vet Diagn Invest 2004, 16(5):403-411.
5. Petit L., Gibert M., Gillet D., Laurent-Winter C., Boquet P., Popoff M.R. Clostridium perfringens epsilon-toxin acts on MDCK cells by forming a large membrane complex. J Bacteriol 1997, 179(20):6480-6487.
6. Robertson S.L., Li J., Uzal F.A., McClane B.A. Evidence for a prepore stage in the action of Clostridium perfringens epsilon toxin. PLoS One 2011, 6(7):e22053.
7. Nagahama M., Ochi S., Sakurai J. Assembly of Clostridium perfringens epsilon-toxin on MDCK cell membrane. J Nat Toxin 1998, 7(3):291-302.
8. Petit L., Maier E., Gibert M., Popoff M.R., Benz R. Clostridium perfringens epsilon toxin induces a rapid change of cell membrane permeability to ions and forms channels in artificial lipid bilayers. J Biol Chem 2001, 276(19):15736-15740.
9. Chassin C., Bens M., de Barry J., Courjaret R., Bossu J.L., Cluzeaud F., et al. Pore-forming epsilon toxin causes membrane permeabilization and rapid ATP depletion-mediated cell death in renal collecting duct cells. Am J Physiol Ren Physiol 2007, 293(3):927-937.
10. Habeeb A.F. Studies on epsilon-prototoxin of Clostridium perfringens type D. Physicochemical and chemical properties of epsilon-prototoxin. Biochim Biophys Acta 1975, 412(1):62-69.
11. Hunter S.E., Clarke I.N., Kelley D.C., Titball R.W. Cloning and nucleotide sequencing of the Clostridium perfringens epsilon-toxin gene and its expression in Escherichia coli. Infect Immun 1992, 60(1):102-110.
12. Miyata S., Minami J., Tamia E., Matsushita P., Shimamoto S., Okabe A. Cleavage of a C-terminal peptide is essential for heptamerization of Clostridium perfringens epsilon-toxin in the synaptosomal membrane. J Biol Chem 2001, 276(17):13778-13783.
13. Jin F., Matsushita P., Katayama S., Jin S., Matsushita S., Minami J., et al. Purification, characterization, and primary structure of Clostridium perfringens lambda-toxin, a thermolysin-like metalloprotease. Infect Immun 1996, 64(1):230-237.
14. Minami J., Katayama S., Matsushita O., Matsushita C., Okabe A. Lambda-toxin of Clostridium perfringens activates the precursor of epsilon-toxin by releasing its N- and C-terminal peptides. Microbiol Immunol 1997, 41(7):527-535.
15. Willis A. Clostridia of wound infections 1969, Butterworth and Company, London.
16. Hughes M.L., Poon R., Adams V., Sayeed S., Saputo J., Uzal F.A., et al. Epsilon-toxin plasmids of Clostridium perfringens type D are conjugative. J Bacteriol 2007, 189(21):7531-7538.
17. Sayeed S., Li J., McClane B.A. Characterization of virulence plasmid diversity among Clostridium perfringens type B isolates. Infect Immun 2010, 78(1):495-504.
18. Li J., Miyamoto K., McClane B.A. Comparison of virulence plasmids among Clostridium perfringens type E isolates. Infect Immun 2007, 75(4):1811-1819.
19. Sayeed S., Fernandez-Miyakawa M.E., Fisher D.J., Adams V., Poon R., Rood J.I., et al. Epsilon-toxin is required for most Clostridium perfringens type D vegetative culture supernatants to cause lethality in the mouse intravenous injection model. Infect Immun 2005, 73(11):7413-7421.
20. Sayeed S., Li J., McClane B.A. Virulence plasmid diversity in Clostridium perfringens type D isolates. Infect Immun 2007, 75(5):2391-2398.
21. Goldstein J., Morris W.E., Loidl C.F., Tironi-Farinetti C., McClane B.A., Uzal F.A., et al. Clostridium perfringens epsilon toxin increases the small intestinal permeability in mice and rats. PLoS One 2009, 4(9):e7065.
22. Hunter S.E., Brown J.E., Oynston P.C.F., Sakurai J., Titball R.W. Molecular genetic analysis of beta-toxin of Clostridium perfringens reveals sequence homology with alpha-toxin, gamma-toxin, and leukocidin of Staphylococcus aureus. Infect Immun 1993, 61(9):3958-3965.
23. McDonel J.L. Toxins of Clostridium perfringens (types A, B, C, D and E). Pharmacology of bacterial toxins 1986, 477-528. Pergamon Press, Oxford. F. Dorner, J. Drews (Eds.).
24. Miyamoto K., Li J., Sayeed S., Akiomoto S., McClane B.A. Sequencing and diversity analyses reveal extensive similarities between some epsilon-toxin-encoding plasmids and the pCPF5603 Clostridium perfringens enterotoxin plasmid. J Bacteriol 2008, 190(21):7178-7188.