Evidence map›Paper›PMID 11500392›Full record

ArticleInfection and immunity2001

Recognition of Lewis x derivatives present on mucins by flagellar components of Pseudomonas aeruginosa.

A Scharfman, S K Arora, P Delmotte, E Van Brussel, J Mazurier, R Ramphal, P Roussel

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.0field-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

35 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Insights onMicroorganisms · 2024
    Article
  3. Article
  4. Assessment of the Glycan-Binding Profile ofbioRxiv : the preprint server for biology · 2023
    Article
  5. Article
  6. Article
  7. Molecular Mechanisms Involved in Pseudomonas aeruginosa Bacteremia.Advances in experimental medicine and biology · 2022
    Review
  8. Flagella, Chemotaxis and Surface Sensing.Advances in experimental medicine and biology · 2022
    Article
  9. Article
  10. Review
  11. Mucins trigger dispersal ofNPJ biofilms and microbiomes · 2018
    Article
  12. 3-Sulfogalactosyl-dependent adhesion ofThe Journal of biological chemistry · 2017
    Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  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

7 authors at 4 institutions in 2 countries.

A ScharfmanUnité INSERM No. 377 and Université de Lille 2, 59045 Lille Cedex, France.
S K Arora
P Delmotte
E Van Brussel
J Mazurier
R Ramphal
P Roussel
Université de Lille · FRUniversity of Florida · USCentre National de la Recherche Scientifique · FRInserm · FR

Funding

BRONCHOPULMONARY INFECTION--THE ROLE OF MUCINR01HL033622 · NHLBI · UNIVERSITY OF FLORIDA · PI RAMPHAL, REUBEN · 1985 to 1999
–
NHLBI NIH HHS HL-33622
6 · The paper itself

Abstract

Pseudomonas aeruginosa binds to human respiratory mucins by mechanisms involving flagellar component-receptor interactions. The adhesion of P. aeruginosa strain PAK is mediated by the flagellar cap protein, FliD, without the involvement of flagellin. Two distinct types of FliD proteins have been identified in P. aeruginosa: A type, found in strain PAK, and B type, found in strain PAO1. In the present work, studies performed with the P. aeruginosa B-type strain PAO1 indicate that both the FliD protein and the flagellin of this strain are involved in the binding to respiratory mucins. Using polyacrylamide-based fluorescent glycoconjugates in a flow cytometry assay, it was previously demonstrated that P. aeruginosa recognizes Le(x) (or Lewis x) derivatives found at the periphery of human respiratory mucins. The aim of the present work was therefore to determine whether these carbohydrate epitopes (or glycotopes) are receptors for FliD proteins and flagellin. The results obtained by both flow cytometry and a microplate adhesion assay indicate that the FliD protein of strain PAO1 is involved in the binding of glycoconjugates bearing Le(x) or sialyl-Le(x) determinants, while the binding of flagellin is restricted to the glycoconjugate bearing Le(x) glycotope. In contrast, the type A cap protein of P. aeruginosa strain PAK is not involved in the binding to glycoconjugates bearing Le(x), sialyl-Le(x), or sulfosialyl-Le(x) glycotopes. This study demonstrates a clear association between a specific Pseudomonas adhesin and a specific mucin glycotope and demonstrates that fine specificities exist in mucin recognition by P. aeruginosa.

Indexed as

Bacterial AdhesionBacterial ProteinsFlagellinFlow CytometryGlycoconjugatesHumansLewis X AntigenMucinsMutationOligosaccharidesPseudomonas aeruginosaRespiratory MucosaSialyl Lewis X Antigen6'-sulfated sialyl Lewis xBacterial ProteinsFlaD protein, BacteriaFlagellinGlycoconjugatesLewis X AntigenMucinsOligosaccharidesSialyl Lewis X Antigen

Identifiers

PMID11500392
PMCPMC98632
OpenAlexW2169610737

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.