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J. Biol. Chem., Vol. 277, Issue 22, 19709-19719, May 31, 2002

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Lactotetraosylceramide, a Novel Glycosphingolipid Receptor for Helicobacter pylori, Present in Human Gastric Epithelium^*

Susann Teneberg^§, Iréne Leonardsson, Hasse Karlsson, Per-Åke Jovall^¶, Jonas Ångström, Dan Danielsson, Ingmar Näslund^**, Åsa Ljungh, Torkel Wadström, and Karl-Anders Karlsson

From the  Institute of Medical Biochemistry, Göteborg University, P. O. Box 440, SE 405 30 Göteborg, Sweden,  Department of Clinical Microbiology and Immunology and ^** Department of General Surgery, Örebro Medical Centre Hospital, SE 701 85 Örebro, Sweden, and the  Department of Medical Microbiology, Dermatology, and Infection, University of Lund, SE 223 62 Lund, Sweden

The binding of Helicobacter pylori to glycosphingolipids was examined by binding of ³⁵S-labeled bacteria to glycosphingolipids on thin-layer chromatograms. In addition to previously reported binding specificities, a selective binding to a non-acid tetraglycosylceramide of human meconium was found. This H. pylori binding glycosphingolipid was isolated and, on the basis of mass spectrometry, proton NMR spectroscopy, and degradation studies, were identified as Gal3GlcNAc3Gal4Glc1Cer (lactotetraosylceramide). When using non-acid glycosphingolipid preparations from human gastric epithelial cells, an identical binding of H. pylori to the tetraglycosylceramide interval was obtained in one of seven samples. Evidence for the presence of lactotetraosylceramide in the binding-active interval was obtained by proton NMR spectroscopy of intact glycosphingolipids and by gas chromatography-electron ionization mass spectrometry of permethylated tetrasaccharides obtained by ceramide glycanase hydrolysis. The lactotetraosylceramide binding property was detected in 65 of 74 H. pylori isolates (88%). Binding of H. pylori to lactotetraosylceramide on thin-layer chromatograms was inhibited by preincubation with lactotetraose but not with lactose. Removal of the terminal galactose of lactotetraosylceramide by galactosidase hydrolysis abolished the binding as did hydrazinolysis of the acetamido group of the N-acetylglucosamine. Therefore, Gal3GlcNAc is an essential part of the binding epitope.

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