Diversity of O‐linked glycosylation patterns between species

Amphibia egg jelly coats are formed by components secreted along the oviduct. These secretion products overlay the oocytes as they pass along the different oviducal portions. Mucin type glycoproteins are the major constituents of the egg jelly coats. In this study, the O‐linked carbohydrate chains of the jelly coats surrounding the eggs of Rana ridibunda were released by alkaline borohydride treatment. Fractionation of the mixture of O‐linked oligosaccharide‐alditols was achieved by a combination of chromatographic techniques including gel‐permeation chromatography, ion‐exchange chromatography and high‐performance liquid chromatography using an amino‐bonded silica column. The primary structures of these O‐glycans were determined by one‐dimensional and two‐dimensional 1 H‐NMR spectroscopy and matrix‐assisted laser‐desorption‐ionization‐time‐of flight mass spectrometry. 25 oligosaccharide structures, possessing a core consisting of Gal(β1–3)GalNAc‐ol with or without branching through a GlcNAc residue linked (β1–6) to the GalNAc residue (core type 2 or core type 1, respectively) are described. The most representative antennae are: HSO 3 (6)[Fuc(α1‐3)]GlcNAc; Gal(β1‐2)Gal; Gal(β1‐2)Gal(α1‐3)[Fuc(α1‐2)]Gal; GlcA(β1‐3)‐Gal(β1‐3)[Fuc(α1‐2)]Gal; GalNAc(α1‐4)Gal(β1‐4)Gal; Gal(β1‐3)GalNAc(α1‐4)Gal(β1‐4)Gal and GlcA(β1‐3)Gal(β1‐3)GalNAc. These results confirm the species‐specific O‐glycosylation of Amphibia oviducal mucins. The significance of this observation should be linked to a symbiotic role of carbohydrates involved in host–parasite interactions.