Search: WFRF:(Teneberg Susann 1955)
> (2000-2004) >
Helicobacter pylori...
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)
-
show more...
-
- 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
-
show less...
-
(creator_code:org_t)
- 2004
- 2004
- English.
-
In: Infection and immunity. - 0019-9567. ; 72:3, s. 1519-29
- Related links:
-
http://www.ncbi.nlm....
-
show more...
-
https://gup.ub.gu.se...
-
https://doi.org/10.1...
-
https://urn.kb.se/re...
-
show less...
Abstract
Subject headings
Close
- 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
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database