The parasitic helminth Schistosoma mansoni is a major public health concern in many developing countries. Glycoconjugates, and in particular the carbohydrate component of these products, represent the main immunogenic challenge to the host and could therefore represent one of the crucial determinants for successful parasite establishment. Here, we report a comparative glycomic analysis of the N- and O-glycans derived from glycoproteins present in S. mansoni egg (ESP) and cercarial (0-3h RP) secretions by a combination of mass spectrometric techniques. Our results show that S. mansoni secrete glycoproteins with glycosylation patterns that are complex and stage-specific. Cercarial stage secretions were dominated by N-glycans that were core xylosylated whereas N-glycans from egg secretions were predominantly core difucosylated. O-glycan core structures from cercarial secretions primarily consisted of the core sequence Galß13(Galß16)GalNAc, whereas egg-secreted O-glycans carried the mucin-type core 1 (Galß13GalNAc) and 2 (Galß13(GlcNAcß16)GalNAc) structures. Additionally, we identified a novel O-glycan core in both secretions in which a Gal residue is linked to the protein. Terminal structures of N- and O-glycans contained high levels of fucose and include stage-specific structures. These glycan structures identified in S. mansoni secretions are potentially antigenic motifs and ligands for carbohydrate binding proteins of the host immune system.