HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M700004-MCP200v1 6/9/1485    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Jang-Lee, J. Articles by Haslam, S. M. Search for Related Content PubMed PubMed Citation Articles by Jang-Lee, J. Articles by Haslam, S. M. Social Bookmarking                      What's this?

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 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.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				I. van Die and R. D Cummings Glycan gimmickry by parasitic helminths: A strategy for modulating the host immune response? Glycobiology, January 1, 2010; 20(1): 2 - 12. [Abstract] [Full Text] [PDF]

				A. J Hulsmeier, P. Deplazes, S. Naem, N. Nonaka, T. Hennet, and P. Kohler An Echinococcus multilocularis coproantigen is a surface glycoprotein with unique O-gycosylation Glycobiology, January 1, 2010; 20(1): 127 - 135. [Abstract] [Full Text] [PDF]

				J. T Aguilan, S. Sundaram, E. Nieves, and P. Stanley Mutational and functional analysis of Large in a novel CHO glycosylation mutant Glycobiology, September 1, 2009; 19(9): 971 - 986. [Abstract] [Full Text] [PDF]