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Published on: June 28, 2024
Mammalian galectins bind galactoseβ1-4fucose disaccharide, a unique structural component of protostomial N-type
Tomoharu Takeuchi1, Mayumi Tamura, Kazusa Nishiyama
1Laboratory of Molecular Immunology, Faculty of Pharmaceutical Sciences, Josai University, 1-1 Keyakidai, Sakado, Saitama 350-0295, Japan. t-take@josai.ac.jp
Abstract:
Galactoseβ1-4Fucose (Galβ1-4Fuc) is a unique disaccharide exclusively found in N-glycans of protostomia, and is recognized by some galectins of Caenorhabditis elegans and Coprinopsis cinerea. In the present study, we investigated whether mammalian galectins also bind such a disaccharide. We examined sugar-binding ability of human galectin-1 (hGal-1) and found that hGal-1 preferentially binds Galβ1-4Fuc compared to Galβ1-4GlcNAc, which is its endogenous recognition unit. We also tested other human and mouse galectins, i.e., hGal-3, and -9 and mGal-1, 2, 3, 4, 8, and 9. All of them also showed substantial affinity to Galβ1-4Fuc disaccharide. Further, we assessed the inhibitory effect of Galβ1-4Fuc, Galβ1-4Glc, and Gal on the interaction between hGal-1 and its model ligand glycan, and found that Galβ1-4Fuc is the most effective. Although the biological significance of galectin-Galβ1-4Fuc interaction is obscure, it might be possible that Galβ1-4Fuc disaccharide is recognized as a non-self-glycan antigen. Furthermore, Galβ1-4Fuc could be a promising seed compound for the synthesis of novel galectin inhibitors.
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