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Lactotetraosylceramide, a novel glycosphingolipid receptor for Helicobacter pylori, present in human gastric epithelium

Teneberg, Susann; Leonardsson, Iréne; Karlsson, Hasse; Jovall, Per-Åke; Ångström, Jonas; Danielsson, Dan; Näslund, Ingmar; Ljungh, Åsa LU ; Wadström, Torkel LU and Karlsson, Karl-Anders (2002) In Journal of Biological Chemistry 277(22). p.19709-19719
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
277
issue
22
pages
19709 - 19719
publisher
ASBMB
external identifiers
  • wos:000175894800063
  • scopus:0037205524
ISSN
1083-351X
DOI
10.1074/jbc.M201113200
language
English
LU publication?
yes
id
ec77c4c4-7f9a-4e84-b92a-85e827620df2 (old id 132332)
date added to LUP
2007-07-10 14:27:22
date last changed
2017-06-25 03:28:21
@article{ec77c4c4-7f9a-4e84-b92a-85e827620df2,
  abstract     = {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.},
  author       = {Teneberg, Susann and Leonardsson, Iréne and Karlsson, Hasse and Jovall, Per-Åke and Ångström, Jonas and Danielsson, Dan and Näslund, Ingmar and Ljungh, Åsa and Wadström, Torkel and Karlsson, Karl-Anders},
  issn         = {1083-351X},
  language     = {eng},
  number       = {22},
  pages        = {19709--19719},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Lactotetraosylceramide, a novel glycosphingolipid receptor for Helicobacter pylori, present in human gastric epithelium},
  url          = {http://dx.doi.org/10.1074/jbc.M201113200},
  volume       = {277},
  year         = {2002},
}