<i>Lactobacillus rhamnosus</i>GG SpaC pilin subunit binds to the carbohydrate moieties of intestinal glycoconjugates

  • Keita Nishiyama
    Department of Animal Science, School of Veterinary Medicine; Kitasato University; Towada
  • Shintaro Ueno
    Department of Animal Science, School of Veterinary Medicine; Kitasato University; Towada
  • Makoto Sugiyama
    Faculty of Veterinary Medicine, School of Veterinary Medicine; Kitasato University; Towada, Aomori Japan
  • Yuji Yamamoto
    Department of Animal Science, School of Veterinary Medicine; Kitasato University; Towada
  • Takao Mukai
    Department of Animal Science, School of Veterinary Medicine; Kitasato University; Towada

書誌事項

タイトル別名
  • SPAC BINDS TO INTESTINAL GLYCOCONJUGATES
公開日
2015-10-05
資源種別
journal article
権利情報
  • http://doi.wiley.com/10.1002/tdm_license_1.1
DOI
  • 10.1111/asj.12491
公開者
Wiley

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説明

Lactobacillus rhamnosus GG (LGG) is a well-established probiotic strain. The beneficial properties of this strain are partially dependent on its prolonged residence in the gastrointestinal tract, and are likely influenced by its adhesion to the intestinal mucosa. The pilin SpaC subunit, located within the Spa pili structure, is the most well studied LGG adhesion factor. However, the binding epitopes of SpaC remain largely unknown. The aim of this study was to evaluate the binding properties of SpaC to the carbohydrate moieties of intestinal glycoconjugates using a recombinant SpaC protein. In a competitive enzyme-linked immunosorbent assay, SpaC binding was markedly reduced by addition of purified mucin and the mucin oligosaccharide fraction. Histochemical staining revealed that the binding of SpaC was drastically reduced by periodic acid treatment. Moreover, in the surface plasmon resonance-based Biacore assay, SpaC bound strongly to the carbohydrate moieties containing β-galactoside at the non-reducing terminus of glycolipids. We here provide the first demonstration that SpaC binds to the oligosaccharide chains of mucins, and that the carbohydrate moieties containing β-galactoside at the non-reducing termini of glycoconjugates play a crucial role in this binding. Our results demonstrate the importance of carbohydrates of SpaC for mucus interactions.

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