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HELICOBACTER PYLORI BINDING TO NEW GLYCANS BASED ON N-ACETYLLACTOSAMINE.

Journal article
Authors Halina Miller-Podraza
Krista Weikkolainen
Thomas Larsson
Petra Johansson
Jari Helin
Jari Natunen
Karl-Anders Karlsson
Published in Glycobiology
Volume 19
Issue 4
Pages 399-407
ISSN 1460-2423
Publication year 2009
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 399-407
Language en
Links dx.doi.org/10.1093/glycob/cwn150
Subject categories Medical and Health Sciences

Abstract

Previously we reported binding of Helicobacter pylori to various non-acid and sialylated neolacto carbohydrate structures using a wide range of natural and chemically modified sequences. A novel non-sialylated neolacto-based binding epitope, GlcNAcbeta3Galbeta4GlcNAc, and analogous structures carrying terminal GalNAcbeta3, GalNAcalpha3 or Galalpha3 showed the binding activity (Miller-Podraza, H. et.al. 2005. J. Biol. Chem. 280, 19695-19703). The present work reports two other H. pylori-binding non-sialylated neolacto-based structures, GlcAbeta3Galbeta4GlcNAcbeta3-R and Glcbeta3Galbeta4GlcNAcbeta3-R, and two amide derivatives (N-methyl and N-ethyl) of GlcAbeta3Galbeta4GlcNAcbeta3-R which were bound by H. pylori. The latter structures turned out to be more effective as H. pylori binders than the parent saccharide. New reducing end variants of the neolacto epitope including species containing N-acetyllactosamine linked beta6 to GlcNAc or Gal with similarity to branched polylactosamines and mucins were prepared and tested. The results extend our previous findings on binding specificities of H. pylori and show that this pathogen is able to interact with an array of lactosamine/neolacto structures, which may be of importance for the in vivo interaction of the bacterium with human cells. The information gained in this work may also be of value for rational design of anti-H. pylori drugs.

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