T. Mukai et K. Arihara, PRESENCE OF INTESTINAL LECTIN-BINDING GLYCOPROTEINS ON THE CELL-SURFACE OF LACTOBACILLUS-ACIDOPHILUS, Bioscience, biotechnology, and biochemistry, 58(10), 1994, pp. 1851-1854
The presence of intestinal lectin-binding glycoproteins on the cell su
rface of Lactobacillus acidophilus group lactic acid bacteria was exam
ined. The cell-surface components were extracted with 2M guanidine hyd
rochloride, and electrophoresed by SDS-PAGE followed by electroblottin
g. Several glycoproteins were detected on the blots of the extracts fr
om 7 of the 11 strains tested. The distribution of glycoproteins seeme
d to be specific for strains rather than for species. beta-Galactoside
-specific lectin was extracted from chicken intestine, and then was la
beled with horseradish peroxidase. The binding of the lectin to glycop
roteins 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 J
CM1132(T), but not from other strains. The binding was inhibited in th
e presence of lactose, indicating that the binding was specific. Presu
mably, the interaction between bacterial cell glycoproteins and intest
inal lectins participates in the specific adherent of the bacterium to
intestinal epithelial surfaces.