Evidence map›Paper›PMID 9038297›Full record

ArticleInfection and immunity1997

Identification of the N-acetylneuraminyllactose-specific laminin-binding protein of Helicobacter pylori.

K H Valkonen, T Wadström, A P Moran

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
7.1field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Modeling and optimization of culture media for recombinantFrontiers in bioengineering and biotechnology · 2024
    Article
  3. Article
  4. Review
  5. Strategies used byWorld journal of gastroenterology · 2017
    Review
  6. Anti-World journal of gastrointestinal pathophysiology · 2016
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Avian pathogenic Escherichia coli bind fibronectin and laminin.Veterinary research communications · 2009
    Article
  14. Laminin isoforms in development and disease.Journal of molecular medicine (Berlin, Germany) · 2007
    Review
  15. Article
  16. Pathogenesis of Helicobacter pylori infection.Clinical microbiology reviews · 2006
    Review
  17. Article
  18. Article
  19. Review
  20. Article
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

3 authors at 1 institution in 1 country.

K H ValkonenDepartment of Microbiology, University College, Galway, Ireland.
T Wadström
A P Moran
Ollscoil na Gaillimhe – University of Galway · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interaction of the gastroduodenal pathogen Helicobacter pylori with the glycoprotein laminin was investigated. Binding of 125I-radiolabelled laminin in a liquid-phase assay by both hemagglutinating and poorly hemagglutinating strains was rapid, saturable, specific, partially reversible, of high affinity, and insensitive to pH. Inhibition of laminin binding by fetuin, but not asialofetuin, and reduced bacterial binding to periodate- or sialidase-treated laminin indicated that glycosylation, particularly sialylation, was important for laminin binding by H. pylori. Inhibition experiments with monosaccharides, disaccharides, and trisaccharides showed that the strains bound to a region spanning a trisaccharide. In particular, inhibition and displacement studies showed that binding to the trisaccharide N-acetylneuraminyl-alpha(2-3)-lactose [NeuAc(2-3)Lac] was preferential to that to the NeuAc(2-6)Lac isomer. Complete inhibition of laminin binding by both hemagglutinating and poorly hemagglutinating strains was achieved only when isolated lipopolysaccharide (LPS) was used as an inhibitor in combination with heat or protease treatment of H. pylori cells, thereby confirming the involvement of both LPS and a protein adhesin in laminin binding. Further inhibition experiments indicated that the protein receptor, rather than LPS, on H. pylori bound NeuAc(2-3)Lac. By using a Western blotting procedure, a 25-kDa outer membrane protein was identified as mediating laminin binding by both hemagglutinating and poorly hemagglutinating H. pylori strains. The specificity of binding was confirmed by complete inhibition of laminin binding by the 25-kDa protein with NeuAc(2-3)Lac. The data collectively suggest that a 25-kDa outer membrane protein acts in a lectin-like manner with LPS to mediate attachment of H. pylori to laminin.

Indexed as

Adhesins, BacterialBlotting, WesternCarrier ProteinsGlycosylationHelicobacter pyloriHemagglutinationLactoseLamininReceptors, LamininSialic AcidsAdhesins, BacterialCarrier ProteinsLactoseLamininN-acetylneuraminoyllactoseReceptors, LamininSialic Acids

Identifiers

PMID9038297
PMCPMC175069
OpenAlexW2065837963

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.