An increasing number of plant glycoproteins have been shown to possess a characteristic N-glycan component containing a beta-(1----2)-linked D-xylose unit on the core beta-D-mannose unit, and an alpha-(1----3)-linked L-fucose unit on the asparagine-linked 2-acetamido-2-deoxy-D-glucose unit. Wistaria floribunda seeds have two distinct lectins; the erythroagglutinin, WFA, and the lymphocyte mitogen, WFM. Earlier studies indicated that both lectins belong to such a class of glycoproteins. We now report the complete structural analysis of Pronase glycopeptides derived from WFA. On the basis of chemical treatment of the glycopeptides, carbohydrate composition and methylation analysis of fluorescein-labeled glycopeptides, and their susceptibility to specific exoglycosidases, the structure of the WFA glycan was found to be, alpha-D-Manp-(1----6)-[beta-D-Xylp-(1----2)]- [alpha-D-Manp(1----3)]-beta-D-Manp-(1----4)-beta-D-GlcpNAc-[ alpha-L- Fucp-(1----3)]-beta-D-Glcp-NAc-(1----N). Quantitative studies on the interaction of the original fluorescein-labeled glycopeptide and its specific degradation products with a rabbit anti-glycan antibody, developed against WFM, showed that the (1----3)-linked alpha-L-fucose unit is essential for interaction. Loss of the terminal alpha-D-mannosyl groups resulted in decreased, though detectable binding.
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