Structural characterization of glycosphingolipids from the eggs of Schistosoma mansoni and Schistosoma japonicum

birthday. The granulomatous pathology in human intestinal schisto-somiasis is induced primarily by the egg antigens of schis-tosome, a parasitic trematode. Glycolipids and glycopro-teins 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 chemi-cal derivatization. Here, we demonstrate that a series of uniquely multifucosylated glycosphingolipids constitute the major egg glycolipids of S.mansoni but not of Sjaponicum. The S.mansoni glycosphingolipids were found to be ex-tended by varying numbers of an unusual repeating unit,-»4(Fucl—»2Fucl—»3)GlcNAcl—», and terminating as ±Fucl—>2Fucl-»3GalNAcl—> at the nonreducing termi-nus. The similarity of these fucosylated structures, particu-larly 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.mansonL On the other hand, the difuco-sylated GalNAc terminal epitope was not found on the gly-cosphingolipids of S.japonicum. Thus, it qualifies for a pos-sible role as a species-specific recognition glycan. Key words: egg antigens/glycolipid/mass spectrometry/ Schistosoma mansoni/Schistosoma japonicu