Originally published In Press as doi:10.1074/mcp.M700004-MCP200 on June 4, 2007.
Molecular & Cellular Proteomics 6:1485-1499, 2007.
© 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
Research
Glycomics Analysis of Schistosoma mansoni Egg and Cercarial Secretions*,S
Jihye Jang-Lee ,
Rachel S. Curwen ,
Peter D. Ashton ,
Bérangère Tissot ,
William Mathieson ,
Maria Panico ,
Anne Dell ,¶,
R. Alan Wilson and
Stuart M. Haslam ,||
From the Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, United Kingdom and Department of Biology, University of York, York YO10 5YW, United Kingdom
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 Galß1 3(Galß1 6)GalNAc, whereas egg-secreted O-glycans carried the mucin-type core 1 (Galß1 3GalNAc) and 2 (Galß1 3(GlcNAcß1 6)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.
|| To whom correspondence should be addressed. Tel.: 44-207-594-5222; Fax: 44-207-225-0458; E-mail: s.haslam{at}imperial.ac.uk

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Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.
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