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  • Title: Carbohydrate binding specificity of the basic lectin from winged bean (Psophocarpus tetragonolobus).
    Author: Matsuda T, Kabat EA, Surolia A.
    Journal: Mol Immunol; 1989 Feb; 26(2):189-95. PubMed ID: 2918860.
    Abstract:
    The carbohydrate binding specificity of the basic lectin from winged bean (Psophocarpus tetragonolobus) was investigated by quantitative precipitin analysis using blood group A, B, H, Le and I substances and by precipitation inhibition with various mono- and oligosaccharides. The lectin precipitated best with A1 substances and moderately with B and A2 substances, but not with H or Le substances. Inhibition assays of lectin-blood group A1 precipitation demonstration that A substance-derived oligosaccharides having the common structure: D-GalNAc alpha(1----3)D-Gal-(beta 1----3/4) to a D-Glc, were the best inhibitors and about 8 and 4 times more active than D-GalNAc and D-GalNAc alpha(1----3)D-Gal, respectively. A difucosyl A-specific oligosaccharide (A-penta), a monofucosyl (A-tetra) and a non-fucosyl containing (A5II) oligosaccharide, D-GalNAc alpha(1----3)D-Gal beta(1----3)D-GlcNAc, had almost the same reactivity, suggesting that the fucose linked to the sub-terminal D-Gal or to the third sugar. D-GlcNAc, from the non-reducing end made no contribution to the carbohydrate binding. Although a terminal non-reducing D-GalNAc or D-Gal residue was indispensible for binding, the lectin bound not only to these terminal non-reducing galactopyranosyl residues, but also showed increased binding to oligosaccharides in which it was bonded to a sub-terminal D-Gal joined to a D-GlcNAc residue, as in blood group A or B substances. This defines the site, thus far, as complementary to a disaccharide plus the beta linkage to the third sugar (D-Glc or D-GlcNAc) from the non-reducing end. The role of the beta(1----3) or beta(1----4) linkage of the sub-terminal non-reducing D-Gal to the D-GlcNAc requires further study.
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