PRESENCE OF INTESTINAL LECTIN-BINDING GLYCOPROTEINS ON THE CELL-SURFACE OF LACTOBACILLUS-ACIDOPHILUS

The presence of intestinal lectin-binding glycoproteins on the cell surface of Lactobacillus acidophilus group lactic acid bacteria was examined. The cell-surface components were extracted with 2M guanidine hydrochloride, and electrophoresed by SDS-PAGE followed by electroblotting. Several glycoproteins were detected on the blots of the extracts from 7 of the 11 strains tested. The distribution of glycoproteins seemed to be specific for strains rather than for species. beta-Galactoside-specific lectin was extracted from chicken intestine, and then was labeled with horseradish peroxidase. The binding of the lectin to glycoproteins detected was assayed by a ligand blotting procedure using the labeled lectin. The lectin-binding glycoproteins estimated to be 60.2 and 43.0 kDa, respectively, were detected from strain L. acidophilus JCM1132(T), but not from other strains. The binding was inhibited in the presence of lactose, indicating that the binding was specific. Presumably, the interaction between bacterial cell glycoproteins and intestinal lectins participates in the specific adherent of the bacterium to intestinal epithelial surfaces.