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Superoxide dismutase (SOD) activity of Dictyocaulus viviparus and its inhibition by antibody from infected and vaccinated bovine hosts

Published online by Cambridge University Press:  06 April 2009

C. Britton ,
D. P. Knox  and
M. W. Kennedy
C. Britton
Affiliation:
Wellcome Laboratories for Experimental Parasitology, University of Glasgow, UK
D. P. Knox
Affiliation:
Moredun Research Institute, Edinburgh, UK
M. W. Kennedy
Affiliation:
Wellcome Laboratories for Experimental Parasitology, University of Glasgow, UK
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Summary

The presence of superoxide dismutase (SOD) activity in the bovine lungworm Dictyocaulus viviparus was examined using the xanthine–xanthine oxidase assay system and by non-denaturing PAGE followed by specific enzyme staining. High levels of activity were detected in excretory–secretory (ES) products of adult worms and in soluble extracts of both the L3 and adult stages of the parasite. Stage-specific and ES-specific activities were indicated by differences in SOD isoenzyme profiles between adult and larval parasite extracts and between adult extract and ES products, with a fast migrating activity being specific to ES products. All isoenzymes were sensitive to cyanide, indicating copper/zinc dependency. The antigenicity of ES SOD was demonstrated by a reduction in SOD activity in both the chemical assay and non-denaturing PAGE following incubation of parasite ES products with IgG antibody purified from serum of infected or vaccinated bovine hosts. The high level of SOD activity released by adult D. viviparus may be a reflection of the problems faced by a parasite occupying an oxygen-rich environment. Antibody inhibition of SOD may, therefore, be an important target of protective immunity.

Keywords

Dictyocaulus viviparusnematodesuperoxide dismutaseexcretory–secretory (ES) productsantibody inhibition
Type
Research Article
Information
Parasitology , Volume 109 , Issue 2 , August 1994 , pp. 257 - 263
Copyright
Copyright © Cambridge University Press 1994

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