Evidence map›Paper›PMID 14977958›Full record

ArticleInfection and immunity2004

Helicobacter pylori and complex gangliosides.

Niamh Roche, Jonas Angström, Marina Hurtig, Thomas Larsson, Thomas Borén, Susann Teneberg

Open access · greenAbstract readComparative Study
In one paragraph

Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
5.7field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Beyond the stomach: the association betweenFrontiers in cellular and infection microbiology · 2025
    Review
  3. Pathogens (Basel, Switzerland) · 2024
    Review
  4. Review
  5. Microorganisms · 2020
    Article
  6. Glycosphingolipids Recognized byMicroorganisms · 2020
    Article
  7. TheScientificWorldJournal · 2020
    Review
  8. Toxins · 2019
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Ganglioside biochemistry.ISRN biochemistry · 2012
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Pathogenesis of Helicobacter pylori infection.Clinical microbiology reviews · 2006
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Niamh RocheInstitute of Medical Biochemistry, Göteborg University, SE 405 30 Göteborg, Sweden.
Jonas Angström
Marina Hurtig
Thomas Larsson
Thomas Borén
Susann Teneberg
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Adhesins, BacterialAnimalsBacterial AdhesionBinding SitesCarbohydrate SequenceErythrocytesGangliosidesGenes, BacterialHelicobacter pyloriHumansIn Vitro TechniquesKineticsMolecular Sequence DataMolecular StructureMutationNuclear Magnetic Resonance, BiomolecularAdhesins, BacterialGangliosides

Identifiers

PMID14977958
PMCPMC356016
OpenAlexW2160803838

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.