Evidence map›Paper›PMID 10325361›Full record

ArticleJournal of clinical microbiology1999

Differentiation of Helicobacter pylori isolates based on lectin binding of cell extracts in an agglutination assay.

S O Hynes, S Hirmo, T Wadström, A P Moran

Open access · bronzeAbstract read
In one paragraph

Article in Journal of clinical microbiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 36 citations in OpenAlex.

  1. Applications of mannose-binding lectins and mannan glycoconjugates in nanomedicine.Journal of nanoparticle research : an interdisciplinary forum for nanoscale science and technology · 2022
    Review
  2. Article
  3. Detection of galectin-3 interaction with commensal bacteria.Applied and environmental microbiology · 2013
    Article
  4. Article
  5. Article
  6. Article
  7. Lectin staining patterns in human gastric mucosae with and without exposure to Helicobacter pylori.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2008
    Article
  8. Article
  9. Lectin typing of Campylobacter concisus.Journal of clinical microbiology · 2002
    Article
  10. 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

4 authors at 2 institutions in 2 countries.

S O HynesDepartment of Microbiology, National University of Ireland, Galway, Ireland.
S Hirmo
T Wadström
A P Moran
Lund University · SEOllscoil na Gaillimhe – University of Galway · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant and animal lectins with various carbohydrate specificities were used to type 35 Irish clinical isolates of Helicobacter pylori and the type strain NCTC 11637 in a microtiter plate assay. Initially, a panel of eight lectins with the indicated primary specificities were used: Anguilla anguilla (AAA), Lotus tetragonolobus (Lotus A), and Ulex europaeus I (UEA I), specific for alpha-L-fucose; Solanum tuberosum (STA) and Triticum vulgaris (WGA), specific for beta-N-acetylglucosamine; Glycine max (SBA), specific for beta-N-acetylgalactosamine; Erythrina cristagali (ECA), specific for beta-galactose and beta-N-acetylgalactosamine; and Lens culinaris (LCA), specific for alpha-mannose and alpha-glucose. Three of the lectins (SBA, STA, and LCA) were not useful in aiding in strain discrimination. An optimized panel of five lectins (AAA, ECA, Lotus A, UEA I, and WGA) grouped all 36 strains tested into eight lectin reaction patterns. For optimal typing, pretreatment by washing bacteria with a low-pH buffer to allow protein release, followed by proteolytic degradation to eliminate autoagglutination, was used. Lectin types of treated samples were stable and reproducible. No strain proved to be untypeable by this system. Electrophoretic and immunoblotting analyses of lipopolysaccharides (LPSs) indicated that the lectins interact primarily, but not solely, with the O side chain of H. pylori LPS.

Indexed as

LectinsAgglutination TestsAnguillaAnimalsBiomassHelicobacter InfectionsHelicobacter pyloriHumansIrelandPlant LectinsPlantsSensitivity and SpecificityLectinsPlant Lectins

Identifiers

PMID10325361
PMCPMC85005
OpenAlexW2169379731

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.