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Haemagglutination and glycolipid‐binding activities of Lactobacillus reuteri
Author(s) -
Mukai T.,
Kaneko S.,
Ohori H.
Publication year - 1998
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1472-765x.1998.00418.x
Subject(s) - hemagglutination , glycoconjugate , galactose , lactobacillus reuteri , lactose , glycolipid , neuraminidase , microbiology and biotechnology , biochemistry , strain (injury) , carbohydrate , agglutination (biology) , chemistry , biology , lactobacillus , antibody , fermentation , enzyme , anatomy , immunology
The carbohydrate-binding activity of Lactobacillus reuteri was studied by haemagglutination (HA), HA inhibition and thin layer chromatography (TLC) overlay assays. Three of the six Lact. reuteri strains examined showed HA activity. Two strains (JCM1081 and JCM1112T) agglutinated neuraminidase-treated, but not untreated, erythrocytes. Strain JCM2762 agglutinated both treated and untreated erythrocytes. The HA activity of JCM 1081 was inhibited by galactose, lactose, methyl beta-galactoside and asialoglycophorin A. Among 12 glycosphingolipids, TLC overlay assay showed that JCM1081 strongly bound to asialo-GM1. These results indicated that JCM1081 bound to the beta-galactosyl residues of the non-reducing terminal of sugar chains of glycoconjugates. The carbohydrate-binding ability of JCM1081 may be responsible for the adhesion of this strain to the mucosal surface of the intestine.