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The secreted and somatic proteinases of the bovine lungworm Dictyocaulus viviparus and their inhibition by antibody from infected and vaccinated animals

Published online by Cambridge University Press:  06 April 2009

C. Britton ,
D. P. Knox ,
G. J. Canto ,
G.M. Urquhart  and
M. W. Kennedy
C. Britton
Affiliation:
Wellcome Laboratories for Experimental Parasitology, University of Glasgow
D. P. Knox
Affiliation:
Moredun Research Institute, Edinburgh
G. J. Canto
Affiliation:
Department of Veterinary Parasitology, University of Glasgow, Glasgow
G.M. Urquhart
Affiliation:
Department of Veterinary Parasitology, University of Glasgow, Glasgow
M. W. Kennedy
Affiliation:
Wellcome Laboratories for Experimental Parasitology, University of Glasgow
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Summary

Proteinase activities were examined in extracts and excretory–secretory (ES) products of the infective and adult stages of the cattle lungworm, Dictyocaulus viviparus. Multiple enzyme activities were identified from each source, as defined by pH optima, substrate specificities, inhibitor effects and substrate gel electrophoresis. Serine-, cysteine- and metalloproteinases were identified, secreted materials being more active against protein substrates per unit protein than were extracts, and the particular proteinases produced varied with the developmental stage of the parasite. The antigenicity of these parasite proteinases was demonstrated by the inhibition of enzymic activity with Protein G-purified serum IgG antibody from both infected and vaccinated hosts and in the retardation of enzyme migration on electrophoresis of enzyme–antibody complexes. For the adult products, this confirmed that the enzymes concerned were of parasite origin, and not host-derived. These results argue for investigation of D. viviparus proteinases as targets for the antibody response in the limitation of parasite-mediated tissue damage and as the active principle behind the anti-D. viviparus vaccine.

Keywords

Dictyocaulus viviparusnematodesexcretory–secretory productsproteinasesantibody inhibition
Type
Research Article
Information
Parasitology , Volume 105 , Issue 2 , October 1992 , pp. 325 - 333
Copyright
Copyright © Cambridge University Press 1992

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