Helicobacter pylori and complex gangliosides

Infect Immun. 2004 Mar;72(3):1519-29. doi: 10.1128/IAI.72.3.1519-1529.2004.


Recognition of sialic acid-containing glycoconjugates by the human gastric pathogen Helicobacter pylori has been repeatedly demonstrated. To investigate the structural requirements for H. pylori binding to complex gangliosides, a large number of gangliosides were isolated and characterized by mass spectrometry and proton nuclear magnetic resonance. Ganglioside binding of sialic acid-recognizing H. pylori strains (strains J99 and CCUG 17874) and knockout mutant strains with the sialic acid binding adhesin SabA or the NeuAcalpha3Galbeta4GlcNAcbeta3Galbeta4GlcNAcbeta-binding neutrophil-activating protein HPNAP deleted was investigated using the thin-layer chromatogram binding assay. The wild-type bacteria bound to N-acetyllactosamine-based gangliosides with terminal alpha3-linked NeuAc, while gangliosides with terminal NeuGcalpha3, NeuAcalpha6, or NeuAcalpha8NeuAcalpha3 were not recognized. The factors affecting binding affinity were identified as (i) the length of the N-acetyllactosamine carbohydrate chain, (ii) the branches of the carbohydrate chain, and (iii) fucose substitution of the N-acetyllactosamine core chain. While the J99/NAP(-) mutant strain displayed a ganglioside binding pattern identical to that of the parent J99 wild-type strain, no ganglioside binding was obtained with the J99/SabA(-) mutant strain, demonstrating that the SabA adhesin is the sole factor responsible for the binding of H. pylori bacterial cells to gangliosides.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial / genetics
  • Adhesins, Bacterial / physiology
  • Animals
  • Bacterial Adhesion / physiology*
  • Binding Sites
  • Carbohydrate Sequence
  • Erythrocytes / chemistry
  • Gangliosides / chemistry*
  • Gangliosides / physiology*
  • Genes, Bacterial
  • Helicobacter pylori / genetics
  • Helicobacter pylori / pathogenicity*
  • Helicobacter pylori / physiology
  • Humans
  • In Vitro Techniques
  • Kinetics
  • Molecular Sequence Data
  • Molecular Structure
  • Mutation
  • Nuclear Magnetic Resonance, Biomolecular
  • Spectrometry, Mass, Electrospray Ionization
  • Spectrometry, Mass, Fast Atom Bombardment


  • Adhesins, Bacterial
  • Gangliosides