Abstract

The ability of Schistosoma mansoni schistosomula to synthesize glycolipids and to acquire radioactively labeled glycoproteins or glycolipids from human erythrocytes or hamster fibroblasts in culture was studied in an attempt to establish the origin of host-like antigens on the schistosome surface. Schistosomula synthesized a lipid which cochromatographed with bovine cerebroside (ceramide monohexoside: CMH) but failed to elaborate larger glycolipids. When schistosomula were cultured with 14C-labeled NIL 2 hamster fibroblasts, the worms did not acquire the glycolipids, ceramide dihexoside (CDH), ceramide trihexoside (CTH), or globoside. Schistosomula cultured with 3H-labeled human erythrocytes acquired small amounts of radioactively labeled low molecular weight material, possibly lipid in nature, but they did not acquire high molecular weight glycoproteins. These results support the view that blood group antigens in the glycoprotein form are unlikely to be acquired by the worm from its host and that glycolipid blood group antigens, which are believed to be present on the surface of the worm, are not synthesized by the parasite.

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