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Novel binding epitope for Helicobacter pylori found in neolacto carbohydrate chains: structure and cross-binding properties.

Journal article
Authors Halina Miller-Podraza
Boel Lanne
Jonas Ångström
Susann Teneberg
Maan Abul Milh
Per-Åke Jovall
Hasse Karlsson
Karl-Anders Karlsson
Published in The Journal of biological chemistry
Volume 280
Issue 20
Pages 19695-703
ISSN 0021-9258
Publication year 2005
Published at Institute of Medical Biochemistry
Pages 19695-703
Language en
Links dx.doi.org/10.1074/jbc.M412688200
Keywords Animals, Antigens, Bacterial, chemistry, metabolism, Binding Sites, Carbohydrate Conformation, Carbohydrate Sequence, Epitopes, chemistry, metabolism, Glycoconjugates, chemistry, immunology, metabolism, Glycolipids, chemistry, immunology, metabolism, Helicobacter pylori, immunology, metabolism, pathogenicity, Humans, Models, Molecular, Molecular Sequence Data, Molecular Structure, Oligosaccharides, chemistry, immunology, metabolism, Rabbits, Thymus Gland, metabolism, microbiology
Subject categories Medical and Health Sciences

Abstract

Helicobacter pylori is a bacterium that colonizes the stomach of a majority of the global human population causing common gastric diseases like ulcers and cancer. It has an unusually complex pattern of binding to various host glycoconjugates including interaction with sialylated, sulfated, and fucosylated sequences. The present study describes an additional binding epitope comprising the neolacto internal sequence of GlcNAcbeta3-Galbeta4GlcNAcbeta. The binding was detected on TLC plates as an interaction with a seven-sugar ganglioside of rabbit thymus. The glycolipid was purified and characterized as Neu5Gcalpha3Galbeta4GlcNAcbeta3Galbeta4GlcNAcbeta3-Galbeta4Glcbeta1Cer with less than 10% of the fraction carrying a repeated lacto (type-1) core chain, Galbeta3Glc-NAcbeta3Galbeta3GlcNAcbeta. After stepwise chemical and enzymatic degradation and structural analysis of products the strongest binder was found to be the pentaglycosylceramide GlcNAcbeta3Galbeta4GlcNAcbeta3Galbeta4Glcbeta1-Cer, whereas the hexa- and tetraglycosylceramides were less active, and the trihexosylceramide was inactive. Further studies revealed that the terminal GlcNAcbeta of the pentaglycosylceramide may be exchanged for either GalNAcbeta3, GalNAcalpha3, or Galalpha3 without loss of the activity. Calculated minimum energy conformers of these four isoreceptors show a substantial topographical similarity suggesting that this binding is a result of a molecular mimicry. Although the glycoconjugate composition of human gastric epithelial cells is not known in detail it is proposed that repeating N-acetyllactosamine units of glycoconjugates may serve as bacterial attachment sites in the stomach.

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