Peroxidase-mediated toxicity to schistosomula of <i>Schistosoma mansoni</i>.

  • E C Jong
    Department of Medicine, University of Washington School of Medicine , Seattle, WA 98195
  • A A F Mahmoud
    Department of Medicine, University of Washington School of Medicine , Seattle, WA 98195
  • S J Klebanoff
    Department of Medicine, University of Washington School of Medicine , Seattle, WA 98195

書誌事項

公開日
1981-02-01
権利情報
  • https://academic.oup.com/pages/standard-publication-reuse-rights
DOI
  • 10.4049/jimmunol.126.2.468
公開者
Oxford University Press (OUP)

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<jats:title>Abstract</jats:title> <jats:p>Guinea pig eosinophil peroxidase (EPO) was capable of killing schistosomula of Schistosoma mansoni in vitro when combined with hydrogen peroxide and a halide. Killing was measured by 51Cr release, by microscopic evaluation of viability, and by reinfection experiments in mice. Parasite killing was dependent on each component of the EPO-H2O2-halide system, was completely inhibited by catalase and azide, and was partially inhibited by cyanide. The EPO-mediated system required 10(-4) M H2O2 and 10(-4) M iodide at pH 7.0, and the schistosomula were killed with exposure to this system of less than 30 min at 37 degrees C. At pH 6.0, the EPO-mediated system showed significant cidal activity with 10(-6) M iodide. Canine neutrophil peroxidase (myeloperoxidase [MPO]) was also able to kill schistosomula in vitro in the presence of 10(-4) M H2O2 and 10(-4) iodide at pH 7.0 and pH 6.0. Physiologic concentrations of chloride (0.1 M) could substitute for iodide at pH 7.0 and pH 6.0 as the halide cofactor; however, at pH 7.0, a higher concentration of enzyme was required. These findings with isolated enzyme systems are compatible with a role for peroxidase in the host defense against schistosomula.</jats:p>

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