Characterization of a core α1→3-fucosyltransferase from the snail Lymnaea stagnalis that is involved in the synthesis of complex-type N -glycans

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Abstract
We have identified a core α1→3-fucosyltransferase activity in the albumin and prostate glands of the snail Lymnaea stagnalis. Incubation of albumin gland extracts with GDP-[14C]Fuc and asialo/agalacto-glycopeptides from human fibrinogen resulted in a labeled product in 50% yield. Analysis of the product by 400 MHz 1H-NMR spectroscopy showed the presence of a Fuc residue α1→3-linked to the Asn-linked GlcNAc. Therefore, the enzyme can be identified as a GDP-Fuc:GlcNAc (Asn-linked) α1→3-fucosyltransferase. The enzyme acts efficiently on asialo/agalacto-glycopeptides from both human fibrinogen and core α1→6-fucosylated human IgG, whereas bisected asialo/agalacto-glycopeptide could not serve as an acceptor. We propose that the enzyme functions in the synthesis of core α1→3-fucosylated complex-type glycans in L. stagnalis. Core α1→3-fucosylation of the asparagine-linked GlcNAc of plant- and insect-derived glycoproteins is often associated with the allergenicity of such glycoproteins. Since allergic reactions have been reported after consumption of snails, the demonstration of core α1→3-fucosylation in L. stagnalis may be clinically relevant.

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