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Literature summary for 1.2.1.12 extracted from

  • Kinoshita, H.; Wakahara, N.; Watanabe, M.; Kawasaki, T.; Matsuo, H.; Kawai, Y.; Kitazawa, H.; Ohnuma, S.; Miura, K.; Horii, A.; Saito, T.
    Cell surface glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Lactobacillus plantarum LA 318 recognizes human A and B blood group antigens (2008), Res. Microbiol., 159, 685-691.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Lactiplantibacillus plantarum
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Lactiplantibacillus plantarum LA 318
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General Information

General Information Comment Organism
physiological function 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. After periodate oxidation of colonic mucin, adhesion of Lactobacillus plantarum LA 318 bacterial cells significantly decreases compared to normal human colonic mucin. High binding is observed to A and B group antigens, while binding to H group antigen is lower. No interaction is observed between GAPDH and various monosaccharides. GAPDH binding to the B-trisaccharide biotinyl polymer probe [Gala1-3 (Fuca1-2) Gal-] is significantly higher as compared to B-disaccharide, Lewis D-trisaccharide, 3-fucosyl-N-acetylglucosamine and a-N-acetylneuraminic acid biotinyl polymer-probes Lactiplantibacillus plantarum