TY - JOUR
T1 - Inhibition of binding of Helicobacter pylori to the glycolipid receptors by probiotic Lactobacillus reuteri
AU - Mukai, Takao
AU - Asasaka, Tomoko
AU - Sato, Eri
AU - Mori, Kenichi
AU - Matsumoto, Mitsuyo
AU - Ohori, Hitoshi
N1 - Funding Information:
This study was partially supported by a Grant-in-Aid for Scientific Research (09876037 and 11760186) from the Ministry of Education, Science, and Culture of Japan, and by a Kitasato University Research Grant for Young Researchers (H10-12).
PY - 2002/1/14
Y1 - 2002/1/14
N2 - 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.
AB - 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.
KW - Glycolipid receptor
KW - Helicobacter pylori
KW - Inhibition
KW - Lactobacillus reuteri
KW - Probiotic
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U2 - 10.1016/S0928-8244(01)00284-X
DO - 10.1016/S0928-8244(01)00284-X
M3 - Article
C2 - 11821231
AN - SCOPUS:0037074529
VL - 32
SP - 105
EP - 110
JO - Pathogens and Disease
JF - Pathogens and Disease
SN - 2049-632X
IS - 2
ER -