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Carbohydrate recognition by enterohemorrhagic Escherichia coli: characterization of a novel glycosphingolipid from cat small intestine

Teneberg, S; Angstrom, J and Ljungh, Åsa LU (2004) In Glycobiology 14(2). p.187-196
Abstract
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 S-35-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 Galalpha3Galbeta4Glcbeta1Cer (isoglobotriaosylceramide) and Galalpha3Galalpha3Galbeta4Glcbeta1Cer. The latter glycosphingolipid has not been described before. The interaction was not based on... (More)
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 S-35-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 Galalpha3Galbeta4Glcbeta1Cer (isoglobotriaosylceramide) and Galalpha3Galalpha3Galbeta4Glcbeta1Cer. The latter glycosphingolipid has not been described before. The interaction was not based on terminal Galalpha3 because the bacteria did not recognize the structurally related glycosphingolipids Galalpha3Galalpha4Galbeta4Glcbeta1Cer and Galalpha3Galbeta4GlcNAcbeta3Galbeta4Glcbeta1Cer (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 Le(a)-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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
enterohemorrhagic E. coli, carbohydrate binding, glycosphingolipids, mass spectrometry, microbial adhesion
in
Glycobiology
volume
14
issue
2
pages
187 - 196
publisher
Oxford University Press
external identifiers
  • wos:000188615400011
  • pmid:14576169
  • scopus:1442332005
ISSN
1460-2423
DOI
10.1093/glycob/cwh015
language
English
LU publication?
yes
id
567349a7-afb7-4594-b154-ecd8558faec3 (old id 288759)
date added to LUP
2007-11-03 09:12:09
date last changed
2017-08-27 05:18:38
@article{567349a7-afb7-4594-b154-ecd8558faec3,
  abstract     = {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 S-35-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 Galalpha3Galbeta4Glcbeta1Cer (isoglobotriaosylceramide) and Galalpha3Galalpha3Galbeta4Glcbeta1Cer. The latter glycosphingolipid has not been described before. The interaction was not based on terminal Galalpha3 because the bacteria did not recognize the structurally related glycosphingolipids Galalpha3Galalpha4Galbeta4Glcbeta1Cer and Galalpha3Galbeta4GlcNAcbeta3Galbeta4Glcbeta1Cer (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 Le(a)-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.},
  author       = {Teneberg, S and Angstrom, J and Ljungh, Åsa},
  issn         = {1460-2423},
  keyword      = {enterohemorrhagic E. coli,carbohydrate binding,glycosphingolipids,mass spectrometry,microbial adhesion},
  language     = {eng},
  number       = {2},
  pages        = {187--196},
  publisher    = {Oxford University Press},
  series       = {Glycobiology},
  title        = {Carbohydrate recognition by enterohemorrhagic Escherichia coli: characterization of a novel glycosphingolipid from cat small intestine},
  url          = {http://dx.doi.org/10.1093/glycob/cwh015},
  volume       = {14},
  year         = {2004},
}