Inactivation of Clostridium difficile cytotoxin by the neutrophil myeloperoxidase system

W. Ooi, H. G. Levine, J. T. LaMont, R. A. Clark

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

The cytotoxin of Clostridium difficile was examined for sensitivity to oxidant secretory products of neutrophils. Exposure to myeloperoxidase, H2O2, and a halide resulted in loss of toxin activity measured by tissue-culture cytotoxicity. The peroxide requirement was provided by reagent H2O2, a peroxide-generating enzyme (glucose oxidase), or a peroxide-producing intestinal microorganism, Lactobacillus acidophilus. Human neutrophils stimulated by phorbol myristate acetate caused similar toxin inactivation. In both the cell-free and the neutrophil systems, inactivation of toxin required halides and was abrogated by azide, cyanide, or catalase. Neutrophils from patients with lack of myeloperoxidase or failure to produce H2O2 were impaired in toxin inactivation unless myeloperoxidase or H2O2, respectively, was added. The reducing agent 2-mercaptoethanol enhanced toxin activity. These data suggest a similarity between C difficile cytotoxin and the classic thiol-activated cytolysins. Moreover, they raise the possibility that neutrophils are involved in oxidative detoxification of microbial products.

Original languageEnglish (US)
Pages (from-to)215-219
Number of pages5
JournalJournal of Infectious Diseases
Volume149
Issue number2
DOIs
StatePublished - Jan 1 1984
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Infectious Diseases

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