Journal
BIOCHEMISTRY
Volume 48, Issue 49, Pages 11678-11691Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi901112q
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Funding
- Universidad de la Republica [250/2002, 404/2009]
- Ministry of Education of Uruguay [PDT 54/078]
- AMSUD-Pasteur travel grant
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The cestodes constitute important but understudied human and veterinary parasites. Their surfaces are rich in carbohydrates, on which very little structural information is available. The tissue-dwelling larva (hydatid cyst) of the cestode Echinococcus granulosus is outwardly protected by a massive layer of carbohydrate-rich extracellular matrix, termed the laminated layer. The monosaccharide composition of this layer suggests that its major carbohydrate components are exclusively mucin-type O-glycans. We have purified these glycans after their release from the crude laminated layer and obtained by MS and NMR the complete structure of 10 of the most abundant components. The structures, between two and six residues in length, encompass a limited number of biosynthetic motifs. The mucin cores I and 2 are either nondecorated or elongated by a chain of Galp beta 1-3 residues. This chain can be capped by a single Galp alpha 1-4 residue, such capping becoming more dominant with increasing chain size. In addition, the core 2 N-acetylglucosamine residue is in cases substituted with the disaccharide Galp alpha 1-4Galp beta 1-4, giving rise to the blood P-1-antigen motif. Larger, also related, glycans exist, reaching at least 18 residues in size. The glycans described are related but larger than those previously described from an Echinococcus multilocularis mucin [Hulsmeier, A. J., et al. (2002) J. Biol. Chem. 277, 5742-5748]. Our results reveal that the E. granulosus cyst exposes to the host only a few different major carbohydrate motifs. These motifs are composed essentially of galactose units and include the elongation by (Galp beta 1-3)(n) and the capping by Galp alpha 1-4, novel in animal mucin-type O-glycans.
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