Glycomics analysis of Schistosoma mansoni egg and cercarial secretions

Jihye Jang-Lee, Rachel S. Curwen, Peter D. Ashton, Bérangère Tissot, William Mathieson, Maria Panico, Anne Dell, R. Alan Wilson, Stuart M. Haslam*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

101 Citations (Scopus)


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 glycomics analysis of the N- and O-glycans derived from glycoproteins present in S. mansoni egg (egg-secreted protein) and cercarial (0-3-h released protein) 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 Galβ1 →3(Galβ1 →6)GaINAc, whereas egg-secreted O-glycans carried the mucin-type core 1 (Gal→1 →3GalNAc) and 2 (Galβ1 →3(GlcNAcβ1 →6)GaINAc) 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.

Original languageEnglish
Pages (from-to)1485-1499
Number of pages15
JournalMolecular and Cellular Proteomics
Issue number9
Publication statusPublished - Sept 2007
Externally publishedYes


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