Abstract
Soybean (Glycine max) is a key source of plant-based protein, yet its nutritional value is impacted by antinutritional factors, including lectins. Whereas soybean lectin is known to bind N-acetyl-d-galactosamine (GalNAc), its lipid interactions remain unexplored. Using a novel purification method, we isolated lectin from soybean meals and characterized its interactions with GalNAc and the glycosphingolipid sulfatide. Isothermal titration calorimetry revealed micromolar affinity for GalNAc, whereas most GalNAc derivatives displayed weak or no binding. Lectin exhibited high-affinity binding to sulfatide in a membrane curvature-dependent manner. Binding of lectin to sulfatide promoted cross-linking of sulfatide-containing vesicles. Whereas sulfatide interaction was independent of GalNAc binding, suggesting distinct binding sites, vesicle cross-linking was inhibited by the sugar. Molecular dynamics simulations identified a consensus sulfatide-binding site in lectin. These findings highlight the dual ligand-binding properties of soybean lectin and may provide strategies to mitigate its antinutritional effects and improve soybean meal processing.