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

FEBS Letters

van den Eijnden, Dirk H¹  van Die, Irma¹  Schiphorst, Wietske E.C.M¹  van Tetering, Angelique¹ 

[1] Department of Medical Chemistry, Vrije Universiteit, Van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands

关键词: Fucose;    Complex-type N-glycan;    Allergy;    Glycosyltransferase;   

DOI  :  10.1016/S0014-5793(99)01489-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown