The granulomatous pathology in human intestinal schistosomiasis is induced primarily by the egg antigens of schistosome, a parasitic trematode. Glycolipids and glycoproteins were extracted from the eggs of the two major species which infect human, Schistosoma mansoni and Schistosoma japonicum, for structural characterization based on highly sensitive mass spectrometric analysis coupled with chemical derivatization. Here, we demonstrate that a series of uniquely multifucosylated glycosphingolipids constitute the major egg glycolipids of S. mansoni but not of S. japonicum. The S. mansoni glycosphingolipids were found to be extended by varying numbers of an unusual repeating unit, -->4(Fuc1-->2Fuc1-->3)GlcNAc1-->, and terminating as +/-Fuc1-->2Fuc1-->3GalNAc1--> at the nonreducing terminus. The similarity of these fucosylated structures, particularly the nonreducing terminal sequence, to the previously identified multifucosylated O-linked oligosaccharides of the cercarial glycocalyx, suggests that they may constitute the cross-reacting epitopes between the egg antigens and cercariae of S. mansoni. On the other hand, the difucosylated GalNAc terminal epitope was not found on the glycosphingolipids of S. japonicum. Thus, it qualifies for a possible role as a species-specific recognition glycan.