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In the digestive tract of mice (HR-1 strain), glycolipids belonging to the ganglio-series were revealed to be expressed in region-specific manners, i.e. FGA1 and FGM1 in the stomach, GA1 in the small intestine, and FGA1 and sulphatides in the cecum. The amount of GA1 as a receptor glycolipid for Lactobacilli was especially higher in the small intestine than in the other regions, it comprising 1.6-2.8 microg/mg dry weight. On immunization of rabbits with Lactobacillus johnsonii and Lactobacillus intestinalis, both of which are murine intestinal bacteria, antibodies toward bacterial glycolipids, i.e. Galalpha1-2Glcalpha1-3DG, and tri- and tetrahexaosyl DGs, were effectively generated and, in addition, they were found to cross-react with GA1 and GalCer, but not with structurally related glycolipids such as Lc(4)Cer, nLc(4)Cer and IV(3)Galalpha-nLc(4)Cer, indicating that GA1 is a preferable antigen for anti-lactobacillus antisera and suggesting the presence of epitopes common to both Lactobacilli and the host. In fact, molecules reacting with anti-GA1 antibodies were detected among bacterial proteins on Western blotting, indicating a possible occurrence of the carbohydrate structure mimicking GA1 in bacterial proteins.


Masao Iwamori, Takahiro Shibagaki, Yoshiyuki Nakata, Shigeki Adachi, Taisei Nomura. Distribution of receptor glycolipids for Lactobacilli in murine digestive tract and production of antibodies cross-reactive with them by immunization of rabbits with Lactobacilli. Journal of biochemistry. 2009 Aug;146(2):185-91

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PMID: 19351707

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