Inhibition of binding of Helicobacter pylori to the glycolipid receptors by probiotic Lactobacillus reuteri

Takao Mukai, Tomoko Asasaka, Eri Sato, Kenichi Mori, Mitsuyo Matsumoto, Hitoshi Ohori

Research output: Contribution to journalArticlepeer-review

230 Citations (Scopus)


We examined the competition of binding of Lactobacillus reuteri and Helicobacter pylori to gangliotetraosylceramide (asialo-GM1) and sulfatide which are putative glycolipid receptor molecules of H. pylori, and identified a possible sulfatide-binding protein of the L. reuteri strain. Among nine L. reuteri strains, two (JCM1081 and TM105) were shown to bind to asialo-GM1 and sulfatide, and to inhibit binding of H. pylori to both glycolipids by a thin layer chromatogram-overlay assay using biotin-labeled bacterial cells. The extract from the bacterial cells of strain TM105 with several detergents, including octyl β-D-glucopyranoside, retained binding to both glycolipids and also inhibited H. pylori binding, suggesting that a binding inhibitor(s) is associated with the bacterial cell surface. When the cell extract was applied to the agarose gel immobilized galactose 3-sulfate corresponding to the structure of sugar moieties of sulfatide, an approximately 47-kDa protein was found to bind to the gel. This observation strongly suggested that inhibition by selected L. reuteri strains help to prevent infection in an early stage of colonization in H. pylori and proposed that L. reuteri strains sharing glycolipid specificity with H. pylori have a potential as probiotics.

Original languageEnglish
Pages (from-to)105-110
Number of pages6
JournalFEMS Immunology and Medical Microbiology
Issue number2
Publication statusPublished - 2002 Jan 14
Externally publishedYes


  • Glycolipid receptor
  • Helicobacter pylori
  • Inhibition
  • Lactobacillus reuteri
  • Probiotic

ASJC Scopus subject areas

  • Immunology and Allergy
  • Microbiology
  • Immunology
  • Microbiology (medical)
  • Infectious Diseases


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