Structural characterization of the N-glycans from Echinococcus granulosus hydatid cyst membrane and protoscoleces.

Infection by the tapeworm Echinococcus granulosus in the intermediate host results in the development of a hydatid cyst which contains the protoscoleces within a fluid-filled cavity enclosed by the bilayered cyst membrane. N-glycans were enzymatically released from crude extracts of homogenates of hydatid cyst membranes and protoscoleces and their structures were defined by high sensitivity fast atom bombardment mass spectrometry in conjunction with sequential exoglycosidase digestions. The major N-glycans from the cyst membrane were found to be non-charged structures having complex-type antennae and core fucosylation. The antennae are either truncated at the first N-acetylglucosamine or are extended with beta-galactose to form N-acetyllactosamine (lacNAc). A significant proportion of the lacNAc backbones are capped by alpha-galactose. The resulting Gal alpha-Gal beta-terminal structures may account for the earlier observation that antibodies against the blood group P1 epitope recognise components of hydatid cyst extracts. The complex-type N-glycans identified in the protoscoleces extracts were the same as the neutral structures found in the cyst membrane but a small proportion of high mannose structures and truncated di- and trimannosyl core structures were also identified. Sialylated N-glycans were identified as minor constituents of the cyst membrane preparation but were not observed in protoscoleces extracts. Whether the sialylated glycans are host derived or endogenously synthesized by the parasite remains to be established. This is the first reported structural analysis of N-glycans from cestodes and provides new insights into protein glycosylation in helminths.