YesU from Bacillus subtilis preferentially binds fucosylated glycans.

The interaction of carbohydrate-binding proteins (CBPs) with their corresponding glycan ligands is challenging to study both experimentally and computationally. This is in part due to their low binding affinity, high flexibility, and the lack of a linear sequence in carbohydrates, as exists in nucleic acids and proteins. We recently described a function-prediction technique called SPOT-Struc that identifies CBPs by global structural alignment and binding-affinity prediction. Here we experimentally determined the carbohydrate specificity and binding affinity of YesU (RCSB PDB ID: 1oq1), an uncharacterized protein from Bacillus subtilis that SPOT-Struc predicted would bind high mannose-type glycans. Glycan array analyses however revealed glycan binding patterns similar to those exhibited by fucose (Fuc)-binding lectins, with SPR analysis revealing high affinity binding to Lewis^x and lacto-N-fucopentaose III. Structure based alignment of YesU revealed high similarity to the legume lectins UEA-I and GS-IV, and docking of Lewis^x into YesU revealed a complex structure model with predicted binding affinity of -4.3 kcal/mol. Moreover the adherence of B. subtilis to intestinal cells was significantly inhibited by Le^x and Le^y but by not non-fucosylated glycans, suggesting the interaction of YesU to fucosylated glycans may be involved in the adhesion of B. subtilis to the gastrointestinal tract of mammals.

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