Abstract

The distribution of exposed and hidden lectin-binding glycoconjugates in adult Schistosoma mansoni worms was studied. Fluorochrome-conjugated lectins were allowed to react both with intact worms and with frozen sections of worms. The results show a selective reactivity of lectins with tegumental surface structures, the intestine, eggs and basement membranes. Strong binding of wheat germ agglutinin (WGA) was seen to the exposed surface of intact worms. Peanut agglutinin (PNA), Ricinus communis agglutinin (RCA) and concanavalin A (Con A) gave a weaker reaction. There was a preferential affinity of PNA and RCA to the spikes covering the tubercles of male worms whereas Con A gave a more uniform staining pattern. Internal structures exposed in frozen sections of worms gave distinct staining reactions. Binding sites for Con A were widely distributed throughout the worm. PNA produced a more selective binding and was the only lectin staining basement membranes as distinct structures. There was a strong selective staining of the gut with soybean agglutinin (SBA) and RCA. Eggs seen in large quantitites inside female parasites reacted strongly with SBA and PNA and less intensely with RCA and WGA. The observed selectivity of lectin binding may reflect physiological function. The results may be important as a basis for using lectin affinity-chromatography for purification and characterization of worm constituents.

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