O-Glycosylation of snails.

Glycoconjugate Journal
Herwig StepanErika Staudacher

Abstract

The glycosylation abilities of snails deserve attention, because snail species serve as intermediate hosts in the developmental cycles of some human and cattle parasites. In analogy to many other host-pathogen relations, the glycosylation of snail proteins may likewise contribute to these host-parasite interactions. Here we present an overview on the O-glycan structures of 8 different snails (land and water snails, with or without shell): Arion lusitanicus, Achatina fulica, Biomphalaria glabrata, Cepaea hortensis, Clea helena, Helix pomatia, Limax maximus and Planorbarius corneus. The O-glycans were released from the purified snail proteins by β-elimination. Further analysis was carried out by liquid chromatography coupled to electrospray ionization mass spectrometry and - for the main structures - by gas chromatography/mass spectrometry. Snail O-glycans are built from the four monosaccharide constituents: N-acetylgalactosamine, galactose, mannose and fucose. An additional modification is a methylation of the hexoses. The common trisaccharide core structure was determined in Arion lusitanicus to be N-acetylgalactosamine linked to the protein elongated by two 4-O-methylated galactose residues. Further elongations by methylated a...Continue Reading

References

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Apr 20, 2010·Carbohydrate Research·Herwig StepanErika Staudacher
May 4, 2011·Carbohydrate Research·Estelle GarenauxYann Guerardel

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Citations

Jun 13, 2015·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Erika Staudacher
Sep 30, 2015·International Journal of Biological Macromolecules·Agnieszka J PietrzykTomasz Niedziela
Sep 10, 2021·Glycobiology·Sabarinath Peruvemba SubramanianRamaswamy Subramanian

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Methods Mentioned

BETA
glycosylation

Software Mentioned

GlycoWorkbench

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