Repeats of LacdiNAc and fucosylated LacdiNAc on N‐glycans of the human parasite Schistosoma mansoni

N‐Glycans from glycoproteins of the worm stage of the human parasite Schistosoma mansoni were enzymatically released, fluorescently labelled and analysed using various mass spectrometric and chromatographic methods. A family of 28 mainly core‐α1–6‐fucosylated, diantennary N‐glycans of composition Hex3−4HexNAc6−12Fuc1−6 was found to carry dimers of N,N′‐diacetyllactosediamine [LacdiNAc or LDN; GalNAc(β1–4)GlcNAc(β1‐] with or without fucose α1–3‐linked to the N‐acetylglucosamine residues in the antennae {GalNAc(β1–4)[±Fuc(α1–3)]GlcNAc(β1–3)GalNAc(β1–4)[±Fuc(α1–3)]GlcNAc(β1‐}. To date, oligomeric LDN and oligomeric fucosylated LDN (LDNF) have been found only on N‐glycans from mammalian cells engineered to express Caenorhabditis elegansβ4‐GalNAc transferase and human α3‐fucosyltransferase IX [Z. S. Kawar et al. (2005) J Biol Chem280, 12810–12819]. It now appears that LDN(F) repeats can also occur in a natural system such as the schistosome parasite. Like monomeric LDN and LDNF, the dimeric LDN(F) moieties found here are expected to be targets of humoral and cellular immune responses during schistosome infection.