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Journal of Biochemistry Advance Access originally published online on April 7, 2009
Journal of Biochemistry 2009 146(2):185-191; doi:10.1093/jb/mvp058
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© The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

Distribution of Receptor Glycolipids for Lactobacilli in Murine Digestive Tract and Production of Antibodies Cross-reactive with them by Immunization of Rabbits with Lactobacilli*

Masao Iwamori1,{dagger}, Takahiro Shibagaki1, Yoshiyuki Nakata1, Shigeki Adachi2 and Taisei Nomura2

1Department of Biochemistry, Faculty of Science and Technology, Kinki University, 3-4-1 Kowakae, Higashiosaka, Osaka 577-8502; and 2Animal Models of Human Diseases, National Institute of Biomedical Innovation, 7-6-8 Asagi-Saito, Ibaraki, Osaka 567-0085, Japan

{dagger}To whom correspondence should be addressed. Tel: +81 6 6721 2332, Fax: +81 6 6723 6721, E-mail: iwamori{at}life.kindai.ac.jp

Received February 12, 2009; Accepted March 23, 2009


   Abstract

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 µg/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. Gal{alpha}1–2Glc{alpha}1–3DG, 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 Lc4Cer, nLc4Cer and IV3Gal{alpha}-nLc4Cer, 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.

Key Words: asialo GM1, bacterial receptor, digestive tract, glycoglycerolipids, TLC-immunostaining

Abbreviations: CL, cardiolipin; CMH, ceramide monohexoside; CS, cholesterol sulphate; DG, diacyl glycerol; Hep, L-glycero-D-mannoheptose; FGA1, fucosyl asialo GM1; FGM1, fucosyl GM1; GA1, asialo GM1; PG, phosphatidyl glycerol; Sul, sulphatide


*The nomenclature for glycolipids and gangliosides is based on the recommendations of the IUPAC-IUB Commission on Biochemical Nomenclature [IUPAC-IUB Commission on Biochemical Nomenclature. (1977) The nomenclature of lipids. Eur. J. Biochem. 179, 11–21] and Svennerholm [Svennerholm, L. (1963) Chromatographic separation of human brain gangliosides. J. Neurochem. 10, 613–623], respectively.


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