Cell surface glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Lactobacillus plantarum LA 318 recognizes human A and B blood group antigens

Hideki Kinoshita, Nozomi Wakahara, Masamichi Watanabe, Tomomi Kawasaki, Hiroki Matsuo, Yasushi Kawai, Haruki Kitazawa, Sinobu Ohnuma, Koh Miura, Akira Horii, Tadao Saito

研究成果: Article査読

57 被引用数 (Scopus)

抄録

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 [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 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.

本文言語English
ページ(範囲)685-691
ページ数7
ジャーナルResearch in Microbiology
159
9-10
DOI
出版ステータスPublished - 2008 11

ASJC Scopus subject areas

  • 微生物学
  • 分子生物学

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