title: O-Glycosylation of snails.
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 and unmethylated galactose and mannose residues and/or fucose are present. The typical snail O-glycan structures are different to those so far described. Similar to snail N-glycan structures they display methylated hexose residues.
authors.affiliation: Department of Chemistry, Glycobiology, University of Natural Resources and Life Sciences Vienna, 1190, Vienna, Austria.
authors.forename: Herwig
authors.initials: H
authors.lastname: Stepan
authors.forename: Martin
authors.initials: M
authors.lastname: Pabst
authors.forename: Friedrich
authors.initials: F
authors.lastname: Altmann
authors.forename: Hildegard
authors.initials: H
authors.lastname: Geyer
authors.forename: Rudolf
authors.initials: R
authors.lastname: Geyer
authors.forename: Erika
authors.initials: E
authors.lastname: Staudacher
mesh_terms: D000818:Animals; D008401:Gas Chromatography-Mass Spectrometry; D006031:Glycosylation; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D012908:Snails / Q000378:metabolism*; D014312:Trisaccharides / Q000737:chemistry / Q000378:metabolism
chemical_list: D011134:Polysaccharides; D011506:Proteins; D014312:Trisaccharides