The exposed carbohydrates of schistosomula of Schistosoma mansoni and their modification during maturation in vivo.
Lectins labeled with 125I or conjugated with fluorescein were employed to study the carbohydrates on the surface of different stages of schistosomula of Schistosoma mansoni. Newly transformed schistosomula were shown to bind concanavalin A; the 60 000 and 120 000 dalton agglutinins from Ricinus communis; the fucose-binding protein from Lotus tetragonolobus; wheat germ agglutinin and peanut agglutinin. Soybean agglutinin, Ulex europaeus agglutinin and Dolichos biflorus agglutinin, on the other hand, failed to bind to the schistosomulum surface. The binding of peanut and soybean agglutinin was unaffected by pretreatment of the parasites with neuraminidase. Binding of concanavalin A, the 120 000 dalton agglutinin from Ricinus communis, wheat germ agglutinin and peanut agglutinin to the surface of 5-day schistosomula, recovered from the lungs of mice, was also demonstrated. In each case, however, the level of binding was approximately 70% less than that observed with newly transformed schistosomula and the binding of the fucose-binding protein from L. tetragonolobus practically disappeared. In contrast with newly transformed schistosomula, lung stage schistosomula, pretreated with neuraminidase, displayed a significant increase in the binding of peanut and soybean agglutinin. The results indicate that a significant alteration in the surface carbohydrates of S. mansoni occurs during in vivo maturation of the parasite. This change may contribute to the organism's ability to survive in the vertebrate host.
D000818:Animals; D050260:Carbohydrate Metabolism; D003208:Concanavalin A / Q000494:pharmacology; D037102:Lectins; D008168:Lung / Q000469:parasitology; D051379:Mice; D008808:Mice, Inbred CBA; D009439:Neuraminidase / Q000494:pharmacology; D012550:Schistosoma mansoni / Q000254:growth & development / Q000378:metabolism*; D013194:Staining and Labeling
D037102:Lectins; D003208:Concanavalin A; D009439:Neuraminidase