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Glycobiology Advance Access published online on November 24, 2003
Glycobiology, doi:10.1093/glycob/cwh028
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Submitted on June 24, 2003
Revised on October 17, 2003
Accepted on November 11, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

Studies on gangliosides with affinity for Helicobacter pylori: binding to natural and chemically modified structures

Halina Miller-Podraza 1*, Petra Johansson 1, Jonas Ångström 1, Thomas Larsson 1, Marianne Longard 1, and Karl-Anders Karlsson 1

1 Institute of Medical Biochemistry, Göteborg University, P. O. Box 440, SE 405 30 Göteborg, Sweden

* To whom correspondence should be addressed. E-mail: Halina.Miller-Podraza{at}medkem.gu.se.

Abstract

Helicobacter pylori, like many other microbes has the ability to bind to carbohydrate epitopes and several sugar sequences have been reported as active for the bacterium including some neutral, sulfated and sialylated structures. In the present work we investigated structural requirements for the sialic acid-dependent binding using a number of natural and chemically modified gangliosides. We have chosen for derivatization studies two kinds of binding-active glycolipids, the simple ganglioside S-3PG (Neu5Ac{alpha}3Gal{beta}4GlcNAc{beta}3Gal{beta}4Glc{beta}1Cer, sialylparagloboside) and branched polyglycosylceramides (PGCs) of human origin. The modifications included oxidation of the sialic acid glycerol chain, reduction of the carboxyl group, amidation of the carboxyl group and lactonization.

Binding experiments confirmed a preference of H. pylori for 3-linked sialic acid and penultimate 4-linked galactose. As expected, neolacto gangliosides (with Gal{beta}4GlcNAc in the core structure) were active in our assays whereas gangliosides with lacto (Gal{beta}3GlcNAc) and ganglio (Gal{beta}3GalNAc) carbohydrate chains were not. Negative binding results were also obtained for disialylparagloboside (with terminal NeuAc{alpha}8NeuAc) and NeuAc{alpha}6-containing glycolipids.

Chemical studies revealed dependence of the binding on Neu5Ac and its glycerol and carboxyl side chains. Most of the derivatizations performed on these groups abolished the binding, however some of the amide forms turned out to be active and one of them (octadecylamide) was found to be an excellent binder. The combined data from molecular dynamics simulations indicate that the binding-active configuration of the terminal disaccharide of S-3PG is with the sialic acid in the anticlinal conformation, whereas in branched PGCs the same structural element most likely assumes the synclinal presentation.


Helicobacter pylori, sialic acid, binding epitope, derivatization
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