It is reported that "Probiotic Lactic Acid Bacteria (LAB)" has various physiological effects for a host. To demonstrate those various actions, an adhesion of probiotic LAB to human intestinal tract is very important. We recently discovered 'blood group recognizing LAB' and identified SlpA as lectin-like protein recognizing A type antigen. Pathogens such as
Helicobacter pylori are reported to recognized human blood group antigens. The blood group antigen sugar chain of mucin may play an essential role for bacterial colonization.
Lactobacillus plantarum LA 318 is a potential probiotic bacterium isolated from normal human intestinal tissue and shows high adhesion to human colonic mucin (HCM) mediated by the bacterial cell surface glyceraldehyde-3-phosphate dehydrogenase (GAPDH). After periodate oxidation of the HCM, the adhesion of LA 318 bacterial cells significantly decreased compared to the normal HCM. A BIACORE adhesion assay of the GAPDH to the blood group antigens was then performed. High adhesion was observed binding the A and B group antigens while adhesion to the H group antigen was lower. No interaction was observed between GAPDH and various monosaccharides. Further, the GAPDH adhesion to B-trisaccharide biotinyl polymer (BP)-probe [Galα1-3 (Fucα1-2) Gal-] was significantly higher as compared to B-disaccharide, Lewis D-trisaccharide, 3-fucosyl-N-acetylglucosamine and α-
N-acetylneuraminic acid BP-probes. The data suggests the trisaccharide structure is important in binding to the blood group antigens. The adhesion of GAPDH to HCM significantly decreased after incubation with NAD
+. This suggests the NAD binding domain on GAPDH may be related to the adhesion to the HCM. Thus, because strain LA 318 and some pathogens recognize the same receptor, strain LA 318 may competitively inhibit pathogenic infections, and therefore may be useful in the development of new anti-infectional foods.
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