| Literature DB >> 15170102 |
Hideaki Uchida1, Kenji Fujitani, Yasushi Kawai, Haruki Kitazawa, Akira Horii, Kenichi Shiiba, Kazuya Saito, Tadao Saito.
Abstract
A new binding assay to investigate the mechanism of adhesion of lactic acid bacteria to the human intestine was established by the surface plasmon resonance technique using a biosensor BIACORE1000. Cells of 26 strains of the Lactobacillus acidophilus group as analytes were eluted onto a sensor chip on which were immobilized biotinylated A-trisaccharide polymer probes having human A-type antigen [(GalNAcalpha1-3(Fucalpha1-2)Gal)-] or human colonic mucin of blood type A (HCM-A) as ligands. In the first screening, high adhesive affinity to the A-trisaccharide BP-probe was observed in L. acidophilus OLL2769, L. crispatus JCM8778, LA205 and LA206. In the second screening, which used HCM-A, only L. acidophilus OLL2769 and L. crispatus JCM8778 were selected as adhesive strains with specific binding ability to human A-antigen. The results indicated that some strains of the L. acidophilus group could recognize and bind the sugar chain of A-antigen structure on HCM.Entities:
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Year: 2004 PMID: 15170102 DOI: 10.1271/bbb.68.1004
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043