Evidence map›Paper›PMID 12700254›Full record

ArticleJournal of bacteriology2003

Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a multifibrillar and adhesive structure.

Eric Durand, Alain Bernadac, Geneviève Ball, Andrée Lazdunski, James N Sturgis, Alain Filloux

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
4.7field-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

70 citing papers in PubMed, 158 citations in OpenAlex.

  1. Article
  2. Article
  3. Structural and functional insights into Pseudomonas aeruginosa's secretion systems 1-6: regulation, role in microbial keratitis and drug targets.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026
    Review
  4. Frontiers in microbiology · 2026
    Article
  5. Frontiers in microbiology · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Comparative Genomic Analysis of the Human PathogenFrontiers in cellular and infection microbiology · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. NOD-like receptor(s) and host immune responses with Pseudomonas aeruginosa infection.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2018
    Review
  17. Article
  18. Article
  19. Article
  20. Review

10 more citing papers are in PubMed but not listed here.

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.

Eric DurandLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Unité Propre de Recherche 9027, Institut de Biologie Structurale et Microbiologie/Centre National de la Recherche Scientifique, 13402 Marseille Cedex 20, France.
Alain Bernadac
Geneviève Ball
Andrée Lazdunski
James N Sturgis
Alain Filloux
Institut de Biologie Structurale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The type II secretion pathway of Pseudomonas aeruginosa is involved in the extracellular release of various toxins and hydrolytic enzymes such as exotoxin A and elastase. This pathway requires the function of a macromolecular complex called the Xcp secreton. The Xcp secreton shares many features with the machinery involved in type IV pilus assembly. More specifically, it involves the function of five pilin-like proteins, the XcpT-X pseudopilins. We show that, upon overexpression, the XcpT pseudopilin can be assembled in a pilus, which we call a type II pseudopilus. Image analysis and filtering of electron micrographs indicated that these appendages are composed of individual fibrils assembled together in a bundle structure. Our observations thus revealed that XcpT has properties similar to those of type IV pilin subunits. Interestingly, the assembly of the type II pseudopilus is not exclusively dependent on the Xcp machinery but can be supported by other similar machineries, such as the Pil (type IV pilus) and Hxc (type II secretion) systems of P. aeruginosa. In addition, heterologous pseudopilins can be assembled by P. aeruginosa into a type II pseudopilus. Finally, we showed that assembly of the type II pseudopilus confers increased bacterial adhesive capabilities. These observations confirmed the ability of pseudopilins to form a pilus structure and raise questions with respect to their function in terms of secretion and adhesion, two crucial biological processes in the course of bacterial infections.

Indexed as

Adhesins, BacterialBacterial AdhesionBacterial ProteinsFimbriae, BacterialFimbriae ProteinsMembrane Transport ProteinsMicroscopy, ElectronPseudomonas aeruginosaSpectroscopy, Fourier Transform InfraredAdhesins, BacterialBacterial ProteinsFimbriae ProteinsMembrane Transport ProteinsXcpT protein, Pseudomonas aeruginosa

Identifiers

PMID12700254
PMCPMC154417
OpenAlexW2087631877

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.