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Helicobacter pylori and complex gangliosides.

Roche, Niamh, 1969 (author)
Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry
Ångström, Jonas, 1950 (author)
Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry
Hurtig, Marina (author)
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Larsson, Thomas (author)
Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry
Borén, Thomas (author)
Umeå universitet,Institutionen för medicinsk kemi och biofysik
Teneberg, Susann, 1955 (author)
Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry
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 (creator_code:org_t)
2004
2004
English.
In: Infection and immunity. - 0019-9567. ; 72:3, s. 1519-29
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Keyword

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

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art (subject category)

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