Glycobiology Advance Access originally published online on October 23, 2003
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Glycobiology vol 14 no 2 pp. 187-196, 2004
© Oxford University Press 2004; all rights reserved.
Carbohydrate recognition by enterohemorrhagic Escherichia coli: characterization of a novel glycosphingolipid from cat small intestine
2 Institute of Medical Biochemistry, Göteborg University, P.O. Box 440, SE 405 30 Göteborg, Sweden; and 3 Department of Medical Microbiology, Dermatology and Infection, Lund University, SE 223 62 Lund, Sweden
Received on September 2, 2003; revised on October 1, 2003; accepted on October 2, 2003
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 nonacid 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
3Galß4Glcß1Cer (isoglobotriaosylceramide) and Gal3Gal3Galß4Glcß1Cer. The latter glycosphingolipid has not been described before. The interaction was not based on terminal Gal3 because the bacteria did not recognize the structurally related glycosphingolipids Gal3Gal4Galß4Glcß1Cer and Gal3Galß4GlcNAcß3Galß4Glcß1Cer (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.
1 To whom correspondence should be addressed; e-mail: susann.teneberg{at}medkem.gu.se
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