Characterization of a core alpha1-->3-fucosyltransferase from the snail Lymnaea stagnalis that is involved in the synthesis of complex-type N-glycans

FEBS Lett. 1999 Nov 19;461(3):311-4. doi: 10.1016/s0014-5793(99)01489-1.


We have identified a core alpha1-->3-fucosyltransferase activity in the albumin and prostate glands of the snail Lymnaea stagnalis. Incubation of albumin gland extracts with GDP-[(14)C]Fuc and asialo/agalacto-glycopeptides from human fibrinogen resulted in a labeled product in 50% yield. Analysis of the product by 400 MHz (1)H-NMR spectroscopy showed the presence of a Fuc residue alpha1-->3-linked to the Asn-linked GlcNAc. Therefore, the enzyme can be identified as a GDP-Fuc:GlcNAc (Asn-linked) alpha1-->3-fucosyltransferase. The enzyme acts efficiently on asialo/agalacto-glycopeptides from both human fibrinogen and core alpha1-->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 alpha1-->3-fucosylated complex-type glycans in L. stagnalis. Core alpha1-->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 alpha1-->3-fucosylation in L. stagnalis may be clinically relevant.

MeSH terms

  • Animals
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Fibrinogen / metabolism
  • Food Hypersensitivity / etiology
  • Fucosyltransferases / isolation & purification*
  • Fucosyltransferases / metabolism
  • Glycopeptides / metabolism
  • Glycoproteins / chemistry
  • Glycoproteins / immunology
  • Humans
  • Immunoglobulin G / metabolism
  • Lymnaea / enzymology*
  • Lymnaea / immunology
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Polysaccharides / biosynthesis*
  • Polysaccharides / chemistry
  • Polysaccharides / immunology


  • Glycopeptides
  • Glycoproteins
  • Immunoglobulin G
  • Polysaccharides
  • Fibrinogen
  • Fucosyltransferases
  • galactoside 3-fucosyltransferase