期刊
RESEARCH IN MICROBIOLOGY
卷 159, 期 9-10, 页码 685-691出版社
ELSEVIER
DOI: 10.1016/j.resmic.2008.07.005
关键词
Adhesion; Probiotics; ABO blood group antigen; Glyceraldehyde-3-phosphate dehydrogenase; Lectin
类别
资金
- Japan Society for the Promotion of Science (JSPS) [19002318, 00118358]
- Scientific Research [16380179]
- Ryoshoku Kenkyukai (Odawara, Japan)
- NIG Cooperative Research Program [2007-B44]
Lactobacillus plantarum LA 318 is a potential probiotic strain isolated from normal human intestinal tissue that shows high adhesion to human colonic mucin mediated by the bacterial cell surface glyceraldehyde-3-phosphate dehydrogenase (GAPDH). We report the adhesion mechanism of the lactobacilli is in part due to GAPDH binding to human ABO-type blood group antigens expressed on human colonic mucin (HCM). After periodate oxidation of HCM, adhesion of L. plantarum LA 318 bacterial cells significantly decreased compared to normal HCM. A BIACORE binding assay of GAPDH to blood group antigens was then performed. High binding was observed to A and B group antigens, while binding to H group antigen was lower (P < 0.01). No interaction was observed between GAPDH and various monosaccharides. Furthermore, GAPDH binding to the B-trisaccharide biotinyl polymer (BP)-probe [Gal alpha 1-3 (Fuc alpha 1-2) Gal-] was significantly higher as compared to B-disaccharide, Lewis D-trisaccharide, 3-fucosyl-N-acetylglucosamine and alpha-N-acetylneuraminic acid BP-probes. The data suggests the trisaccharide structure is important in binding to the blood group antigens. The binding of GAPDH to HCM significantly decreased after incubation with NAD(+). This suggests that the NAD binding domain on GAPDH may be related to binding to HCM. (C) 2008 Elsevier Masson SAS. All rights reserved.
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