HEMAGGLUTINATION AND GLYCOLIPID-BINDING ACTIVITIES OF LACTOBACILLUS-REUTERI

The carbohydrate-binding activity of Lactobacillus reuteri was studied by haemagglutination (HA), HA inhibition and thin layer chromatograph y (TLC) overlay assays. Three of the six Lact. reuteri strains examine d showed HA activity. Two strains (JCM1081 and JCM1112(T)) agglutinate d neuraminidase-treated, but not untreated, erythrocytes, Strain JCM27 62 agglutinated both treated and untreated erythrocytes. The HA activi ty of JCM1081 was inhibited by galactose, lactose, methyl beta-galacto side and asialoglycophorin A. Among 12 glycosphingolipids, TLC overlap assay showed that JCM1081 strongly bound to asialo-GM1. These results indicated that JCM1081 bound to the beta-galactosyl residues of the n on-reducing terminal of sugar chains of glycoconjugates. The carbohydr ate-binding ability of JCM1081 may be responsible for the adhesion of this strain to the mucosal surface of the intestine.