Helicobacter pylori binding to new glycans based on N-acetyllactosamine

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Abstract
Previously we reported binding of Helicobacter pylori to various nonacid and sialylated neolacto carbohydrate structures using a wide range of natural and chemically modified sequences. A novel nonsialylated neolacto-based binding epitope, GlcNAcβ3Galβ4GlcNAc, and analogous structures carrying terminal GalNAcβ3, GalNAcα3, or Galα3 showed the binding activity (Miller-Podraza H, Lanne B, Ångström J, Teneberg S, Abul-Milh M, Jovall P-Å, Karlsson H, Karlsson K-A. 2005. Novel binding epitope for Helicobacter pylori found in neolacto carbohydrate chains. J Biol Chem. 280:19695–19703). The present work reports two other H. pylori-binding nonsialylated neolacto-based structures, GlcAβ3Galβ4GlcNAcβ3-R and Glcβ3Galβ4GlcNAcβ3-R, and two amide derivatives (N-methyl and N-ethyl) of GlcAβ3Galβ4GlcNAcβ3-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 β6 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 N-acetyllactosamine/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.