Abstract

Rabbit antisera were raised against an antigen present in Schistosoma mansoni adult worms and eggs, and were shown to yield a single immunoprecipitin arc in immunoelectrophoresis and immunodiffusion against S. mansoni egg and worm antigen extracts. The antisera conferred partial but significant protection (22-30%) against a S. mansoni challenge when transferred to mice five and six days after the mice had been infected percutaneously with 200 cercariae. The egg and the worm forms of the antigen were immunologically cross-reactive, but the egg antigen possessed peptidolytic activity that could be inhibited with serine protease inhibitors. In indirect immunofluorescence the rabbit antisera reacted with surfaces of cercariae, five-day old lung-stage schistosomula, miracidia and praziquantel-treated adult worms. Gel-filtration chromatography demonstrated a relative molecular size of approximately 480 kDa for both the egg and worm forms of the antigen, and lectin-affinity chromatography indicated both were glycosylated. The serine protease activity and large relative molecular size of egg Sm480 were confirmed by a combination of radiolabelling with tritiated di-isopropyl fluorophosphate, immunoelectrophoresis and polyacrylamide gel electrophoresis.

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