1887

Abstract

Summary

Clostridium sordellii produces two toxins, designated HT (haemorrhagic toxin) and LT (lethal toxin), that are similar to toxins A and B of The physicochemical properties of toxins HT and A were remarkably similar. The specific biological activities of toxin HT were almost the same as those of toxin A, and their NH-terminal sequences shared close homology. The properties of toxins LT and B were similar, as were their NH-terminal sequences, but toxin B was much more cytotoxic than toxin LT. Immunodiffusion analysis with specific antibodies showed that although toxins B and LT shared major antigenic determinants, each had unique epitopes. The results suggest that toxins B and LT have diverged more than toxins A and HT. Immunoblotting with antibodies to the toxins of showed that toxins HT and LT had common antigenic determinants.

Loading

Article metrics loading...

/content/journal/jmm/10.1099/00222615-36-1-30
1992-01-01
2024-04-23
Loading full text...

Full text loading...

/deliver/fulltext/jmm/36/1/medmicro-36-1-30.html?itemId=/content/journal/jmm/10.1099/00222615-36-1-30&mimeType=html&fmt=ahah

References

  1. Al-Mashat R. R., Taylor D. J. Clostridium sordellii in enteritis in an adult sheep. Vet Rec 1983; 112:19
    [Google Scholar]
  2. Popoff M. R. Bacteriological examination in enterotoxaemia of sheep and lamb. Vet Rec 1984; 114:324
    [Google Scholar]
  3. Richards S. M., Hunt B. W. Clostridium sordellii in lambs. Vet Rec 1982; 111:22
    [Google Scholar]
  4. Hogan S. F., Ireland K. Fatal acute spontaneous endometritis resulting from Clostridium sordellii. Am J Clin Pathol 1989; 91:104–106
    [Google Scholar]
  5. McGregor J. A., Lovell G. L., Soper D. Clostridium sordellii mediated toxic shock and myonecrosis. Abstracts of the Annual Meeting of the American Society for Microbiology 1988
    [Google Scholar]
  6. Alio M., Silva J., Fekety R., Rifkin G. D., Waskin H. Prevention of clindamycin-induced colitis in hamsters by Clostridium sordellii antitoxin. Gastroenterology 1979; 76:351–355
    [Google Scholar]
  7. Larson H. E., Price A. B. Pseudomembranous colitis: presence of clostridial toxin. Lancet 1977; 2:1312–1314
    [Google Scholar]
  8. Rifkin G. D., Fekety F. R., Silva J., Sack R. B. Antibiotic-induced colitis. Implication of a toxin neutralised by Clostridium sordellii antitoxin. Lancet 1977; 2:1103–1106
    [Google Scholar]
  9. 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 1978; 298:531–534
    [Google Scholar]
  10. George R. H., Symonds J. M., Dimock F. Identification of Clostridium difficile as a cause of pseudomembranous colitis. Br Med J 1978; 1:695
    [Google Scholar]
  11. Larson H. E., Honour P., Price A. B., Borriello S. P. Clostridium difficile and the aetiology of pseudomembranous colitis. Lancet 1978; 1:1063–1066
    [Google Scholar]
  12. Chang T.-W., Gorbach S. L., Bartlett J. G. Neutralization of Clostridium difficile toxin by Clostridium sordelli antitoxins. Infect Immun 1978; 22:418–422
    [Google Scholar]
  13. Rifkin G. D., Fekety R., Silva J. Neutralization by Clostridium sordellii antitoxin of toxins implicated in clindamycininduced cecitis in the hamster. Gastroenterology 1978; 75:422–424
    [Google Scholar]
  14. Banno Y., Kobayashi T., Watanabe K., Ueno K., Nozawa Y. Two toxins (D-l and D-2) of Clostridium difficile causing antibiotic-associated colitis: purification and some characterization. Biochem Int 1981; 2:629–635
    [Google Scholar]
  15. Sullivan N. M., Pellett S., Wilkins T. D. Purification and characterization of toxins A and B of Clostridium difficile. Infect Immun 1982; 35:1032–1040
    [Google Scholar]
  16. Taylor N. S., Thome G. M., Bartlett J. G. Comparison of two toxins produced by Clostridium difficile. Infect Immun 1981; 34:1036–1043
    [Google Scholar]
  17. Libby J. M., Jortner B. S., Wilkins T. D. Effects of the two toxins of Clostridium difficile in antibiotic-associated cecitis in hamsters. Infect Immun 1982; 36:822–829
    [Google Scholar]
  18. Lyerly D. M., Lockwood D. E., Richardson S. H., Wilkins T. D. Biological activities of toxins A and B of Clostridium difficile. Infect Immun 1982; 35:1147–1150
    [Google Scholar]
  19. Lyerly D. M., Saum K. E., MacDonald D. K., Wilkins T. D. Effects of Clostridium difficile toxins given intragastrically to animals. Infect Immun 1985; 47:349–352
    [Google Scholar]
  20. Arseculeratne S. N., Pannabokke R. G., Wijesundera S. The toxins responsible for the lesions of Clostridium sordellii gas gangrene. J Med Microbiol 1969; 2:37–53
    [Google Scholar]
  21. Martinez R. D., Wilkins T. D. Purification and characterization of Clostridium sordelli hemorrhagic toxin and cross-reactivity with Clostridium difficile toxin A (enterotoxin). Infect Immun 1988; 56:1215–1221
    [Google Scholar]
  22. Popoff M. R. Purification and characterization of Clostridium sordellii lethal toxin and cross-reactivity with Clostridium difficile cytotoxin. Infect Immun 1987; 55:35–43
    [Google Scholar]
  23. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248–254
    [Google Scholar]
  24. Holdeman L. V., Cato E. P., Moore W. E. C. Anaerobe laboratory manual. 4th edn Blacksburg, Virginia Polytechnic Institute and State University: 1977
    [Google Scholar]
  25. Sterne M., Wentzel L. M. A new method for the large-scale production of high-titre botulinum formol-toxoid types C and D. J Immunol 1950; 65:175–183
    [Google Scholar]
  26. Ehrich M., Van Tassell R. L., Libby J. M., Wilkins T. D. Production of Clostridium difficile antitoxin. Infect Immun 1980; 28:1041–1043
    [Google Scholar]
  27. Lyerly D. M., Phelps C. J., Wilkins T. D. Monoclonal and specific polyclonal antibodies for immunoassay of Clostridium difficile toxin A. J Clin Microbiol 1985; 21:12–14
    [Google Scholar]
  28. Yamakawa K., Nakamura S., Nishida S. Separation of two cytotoxins of Clostridium sordellii strains. Microbiol Immunol 1985; 29:553–557
    [Google Scholar]
  29. Lyerly D. M., Phelps C. J., Toth J., Wilkins T. D. Characterization of toxins A and B of Clostridium difficile with monoclonal antibodies. Infect Immun 1986; 54:70–76
    [Google Scholar]
  30. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680–685
    [Google Scholar]
  31. Lyerly D. M., Sullivan N. M., Wilkins T. D. Enzyme-linked immunosorbent assay for Clostridium difficile toxin A. J Clin Microbiol 1983; 17:72–78
    [Google Scholar]
  32. Spackman D. H., Stein W. H., Moore S. Automatic recording apparatus for use in the chromatography of amino acids. Anal Chem 1958; 30:1190–1206
    [Google Scholar]
  33. Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 1967; 6:1948–1954
    [Google Scholar]
  34. Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 1987; 262:10035–10038
    [Google Scholar]
  35. Libby J. M., Wilkins T. D. Production of antitoxins to two toxins of Clostridium difficile and immunological comparison of the toxins by cross-neutralization studies. Infect Immun 1982; 35:374–376
    [Google Scholar]
  36. Tucker K. D., Carrig P. E., Wilkins T. D. Toxin A of Clostridium difficile is a potent cytotoxin. J Clin Microbiol 1990; 28:869–871
    [Google Scholar]
  37. Krivan H. C., Clark G. F., Smith D. F., Wilkins T. D. Cell surfacebinding site for Clostridium difficile enterotoxin: evidence for a glycoconjugate containing the sequence Gal al-3 Gal /Sl-4GlcNAc. Infect Immun 1986; 53:573–581
    [Google Scholar]
  38. Dove C. H., Wang S.-Z., Price S. B. Molecular characterizationof the Clostridium difficile toxin A gene. Infect Immun 1990; 58:480–488
    [Google Scholar]
  39. Meador I. J., Tweten R. K. Purification and characterization oftoxin B from Clostridium difficile. Infect Immun 1988; 56:1708–1714
    [Google Scholar]
  40. Von Eichel-Streiber C., Laufenberg-Feldmann R., Sartingen S., Schulze J., Sauerbom M. Cloning of Clostridium difficile toxin B gene and demonstration of high N-terminal homology between toxin A and toxin B. Med Microbiol Immunol 1990; 179:271–279
    [Google Scholar]
  41. Lyerly D. M., Roberts M. D., Phelps C. J., Wilkins T. D. Purification and properties of toxin A and toxin B of Clostridium difficile. FEMS Microbiol Lett 1986; 33:31–35
    [Google Scholar]
  42. Barroso L. A., Wang S.-Z., Phelps C. J., Johnson J. L., Wilkins T. D. Nucleotide sequence of Clostridium difficile toxin B gene. Nucl Acids Res 1990; 18:4004
    [Google Scholar]
  43. Krivan H. C., Wilkins T. D. Purification of Clostridium difficile toxin A by affinity chromatography on immobilized thyroglobulin. Infect Immun 1987; 55:1873–1877
    [Google Scholar]
  44. Price S. B., Phelps C. J., Wilkins T. D., Johnson J. L. Cloning of the carbohydrate-binding portion of the toxin A gene of Clostridium difficile. Curr Microbiol 1987; 16:55–60
    [Google Scholar]
  45. Spero L., Morlock B. A., Metzger J. F. On the cross-reactivity of staphylococcal enterotoxins A, B, and C. J Immunol 1978; 120:86–89
    [Google Scholar]
  46. Strockbine N. A., Marques L. R. M., Newland J. W., Smith H. W., Holmes R. K., O’Brien A. D. Two toxin-converting phages from Escherichia coli 0157:H7 strain 933 encode antigenically distinct toxins with similar biologic activities. Infect Immun 1986; 53:135–140
    [Google Scholar]
  47. Jackson M. P., Neill R. J., O’Brien A. D., Holmes R. K., Newland J. W. Nucleotide sequence analysis and comparison of the structural genes for shiga-like toxin I and shiga-like toxin II encoded by bacteriophages from Escherichia coli 933. FEMS Microbiol Lett 1987; 44:109–114
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-36-1-30
Loading
/content/journal/jmm/10.1099/00222615-36-1-30
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error