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Glycobiology Advance Access originally published online on September 13, 2006
Glycobiology 2007 17(1):82-103; doi:10.1093/glycob/cwl048
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Structural characterization of N-glycans from the freshwater snail Biomphalaria glabrata cross-reacting with Schistosoma mansoni glycoconjugates

Tobias Lehr2, Hildegard Geyer2, Kai Maaß2, Michael J. Doenhoff3 and Rudolf Geyer1,2

2 Institute of Biochemistry, Faculty of Medicine, University of Giessen, Friedrichstrasse 24, D-35392 Giessen, Germany
3 School of Biological Sciences, University of Wales, Bangor, Gwynedd LL57 2UW, Wales, UK


1 To whom correspondence should be addressed; Tel: +49-641-99-47400; Fax: +49-641-99-47409; e-mail: rudolf.geyer{at}biochemie.med.uni-giessen.de

Received on July 19, 2006; revised on September 1, 2006; accepted on September 6, 2006

The human parasitic trematode Schistosoma mansoni has a complex life cycle that includes the freshwater snail Biomphalaria glabrata as intermediate host. Within each stage, the parasite synthesizes a wide array of glycoconjugates, exhibiting, in part, unique carbohydrate structures. In addition, the parasite expresses definitive host-like sugar epitopes, such as Lewis X determinants, supporting the concept of carbohydrate-mediated molecular mimicry as an invasion and survival strategy. In the present study, we investigated whether common carbohydrate determinants occur also at the level of the intermediate host. To this end, a structural characterization of hemolymph glycoprotein-N-glycans of B. glabrata was performed. N-glycans were released from tryptic glycopeptides and labeled with 2-aminopyridine. Sugar chains serologically cross-reacting with S. mansoni glycoconjugates were isolated by immunoaffinity chromatography using a polyclonal antiserum directed against schistosomal egg antigens and fractionated by Aleuria aurantia lectin affinity chromatography and high-performance liquid chromatography. Obtained glycans were analyzed by different mass spectrometric techniques as well as by monosaccharide constituent and linkage analysis. The results revealed a highly heterogeneous oligosaccharide pattern. Cross-reacting species represented about 5% of the total glycans and exhibited a terminal Fuc({alpha}1-3)GalNAc unit, a (1-2)-linked xylosyl residue, or both types of structural motifs. In conclusion, our study demonstrates the presence of common carbohydrate epitopes also at the level of S. mansoni and its intermediate host.

Key words: Biomphalaria glabrata / mass spectrometry / mollusc glycoproteins / N-glycans / Schistosoma


None declared.


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