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植物乳杆菌LA 318的细胞表面甘油醛-3-磷酸脱氢酶(GAPDH)可识别人类A和B血型抗原。

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

作者信息

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

机构信息

Laboratory of Animal Products Chemistry, Graduate School of Agricultural Science, Tohoku University, Tsutsumidori-Amamiyamachi 1-1,Aoba-ku, Sendai, Miyagi 981-8555, Japan.

出版信息

Res Microbiol. 2008 Nov-Dec;159(9-10):685-91. doi: 10.1016/j.resmic.2008.07.005. Epub 2008 Aug 26.

DOI:10.1016/j.resmic.2008.07.005
PMID:18790050
Abstract

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 [Galalpha1-3 (Fucalpha1-2) 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.

摘要

植物乳杆菌LA 318是从正常人肠道组织中分离出的一种潜在益生菌菌株,它通过细菌细胞表面的甘油醛-3-磷酸脱氢酶(GAPDH)对人结肠粘蛋白表现出高度粘附性。我们报告了乳酸杆菌的粘附机制部分归因于GAPDH与人结肠粘蛋白(HCM)上表达的人ABO血型抗原的结合。在对HCM进行高碘酸盐氧化后,与正常HCM相比,植物乳杆菌LA 318细菌细胞的粘附显著降低。然后进行了GAPDH与血型抗原的BIACORE结合测定。观察到与A和B组抗原的结合力高,而与H组抗原的结合力较低(P<0.01)。未观察到GAPDH与各种单糖之间的相互作用。此外,与B-二糖、Lewis D-三糖、3-岩藻糖基-N-乙酰葡糖胺和α-N-乙酰神经氨酸BP-探针相比,GAPDH与B-三糖生物素聚合物(BP)-探针[Galα1-3(Fucα1-2)Gal-]的结合显著更高。数据表明三糖结构在与血型抗原的结合中很重要。与NAD +孵育后,GAPDH与HCM的结合显著降低。这表明GAPDH上的NAD结合结构域可能与与HCM的结合有关。

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