Schistosoma mansoni surface glycoproteins

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Abstract
Surface glycoproteins from newly transformed schistosomula of Schistosoma mansoni have been identified by surface radioiodination and lectin‐affinity chromatography. From the glycoconjugates bound by the three lectins used, concanavalin A, peanut agglutinin and fucose‐binding protein, only in the concanavalin‐A‐bound fractions were glycoproteins identified. Changes in concanavalin‐A‐binding glycoproteins were detected after transformation and early maturation of the schistosomula.Some glycoproteins disappeared (Mr 38000, 29000 and 25000), some appeared independently of host molecules (Mr 19000), others only appeared after culture in human serum (Mr 45000).Two major glycoproteins of Mr 32000 and 16000 were detected on all stages examined. Within the total set of surface glycoproteins identified on 3‐h schistosomula only the strong Mr‐38000–32000 complex was found to be antigenic. Thus many major low‐molecular‐mass surface glycoproteins of the parasite are not recognised as antigens by immune animals. The separation of only the Mr‐38000–32000 antigens by concanavalin A affinity chromatography indicates the feasibility of using this method in conjunction with immunoaffinity columns to purity these molecules.

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