Identification and localization of a schistosome-associated fucosyllactose determinant expressed by Fasciola hepatica.

A Biomphalaria alexandrina-derived lectin (BaSII), of proven specificity to a Schistosoma mansoni-associated fucosyllactose [(Fuc alpha1-2) Gal beta1-4 Glc] determinant, was employed to investigate the putative antigenic cross-reactivity between Schistosoma mansoni and Fasciola hepatica in terms of this structurally-defined oligosaccharide sequence. BaSII affinity column chromatography of extracts of adult worms metabolically radiolabelled with 35S-methionine and analysis by two-dimensional gels established the expression of the fucosyllactose determinant in multiple copies among heterogeneous, acidic glycoproteins synthesized by adult Fasciola hepatica. Direct fluorescence microscopy revealed that determinant-bearing glycoproteins were localized to the external glycocalyx and perikarya of the tegument as well as the epithelial lining of the intestinal caeca and vitelline ducts and glands. Determinant expression was also evident in embryonated cells of eggs and miracidia as well as the intermediate cellular wall of encysted metacercariae, suggesting its conservation during the course of development of the parasite. Based on the structural relatedness of the cross-reactive fucosyllactose determinant to the antigenic mammalian blood group H trisaccharide, our observations may have implications in serodiagnosis and immunoprophylaxis of schistosomiasis/fascioliasis.