Glycobiology Advance Access published online on October 23, 2003
Glycobiology, doi:10.1093/glycob/cwh015
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© 2003 Oxford University Press
ORIGINAL ARTICLES
1 Institute of Medical Biochemistry, Göteborg University, P.O. Box 440, SE 405 30 Göteborg, Sweden A key virulence trait of pathogenic bacteria is the ability to bind to receptors on mucosal cells. Here the potential glycosphingolipid receptors of enterohemorrhagic Escherichia coli were examined by binding of 35S-labeled bacteria to glycosphingolipids on thin-layer chromatograms. Thereby, a selective interaction with two non-acid glycosphingolipids of cat small intestinal epithelium was found. The binding-active glycosphingolipids were isolated and, on the basis of mass spectrometry, proton NMR spectroscopy, and degradation studies, identified as Gal
Revised on October 1, 2003
Accepted on October 2, 2003
Carbohydrate recognition by enterohemorrhagic Escherichia coli. Characterization of a novel glycosphingolipid from cat small intestine
2 Department of Medical Microbiology, Dermatology and Infection, Lund University, SE 223 62 Lund, Sweden
3Gal
4Glc1Cer (isoglobotriaosylceramide) and Gal3Gal3Gal4Glc1Cer. The latter glycosphingolipid has not been described before. The interaction was not based on terminal Gal3 since the bacteria did not recognize the structurally related glycosphingolipids Gal3Gal4Gal4Glc1Cer and Gal3Gal4GlcNAc3Gal4Glc1Cer (B5 glycosphingolipid). However, further binding assays using reference glycosphingolipids showed that the enterohemorrhagic E. coli also bound to lactosylceramide with phytosphingosine and/or hydroxy fatty acids, suggesting that the minimal structural element recognized is a correctly presented lactosyl unit. Further binding of neolactotetraosylceramide, lactotetraosylceramide, the Lea-5 glycosphingolipid, as well as a weak binding to gangliotriaosylceramide and gangliotetraosylceramide, was found in analogy with binding patterns that previously have been described for other bacteria classified as "lactosylceramide-binding".
Carbohydrate binding, glycosphingolipids, enterohemorrhagic E. coli, microbial adhesion, mass spectrometry
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