Evidence map›Paper›PMID 16788194›Full record

ArticleJournal of bacteriology2006

FppA, a novel Pseudomonas aeruginosa prepilin peptidase involved in assembly of type IVb pili.

Sophie de Bentzmann, Marianne Aurouze, Geneviève Ball, Alain Filloux

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

58 citing papers in PubMed, 96 citations in OpenAlex.

  1. Review
  2. Article
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  11. Plants (Basel, Switzerland) · 2024
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  16. Article
  17. Antimicrobial resistance, virulence factors, and genotypes of Pseudomonas aeruginosa clinical isolates from Gorgan, northern Iran.International microbiology : the official journal of the Spanish Society for Microbiology · 2022
    Article
  18. Histamine: A Bacterial Signal Molecule.International journal of molecular sciences · 2021
    Review
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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 1 country.

Sophie de BentzmannLaboratoire d'Ingénierie des Systèmes Macromoléculaires, CNRS-IBSM-UPR9027, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
Marianne Aurouze
Geneviève Ball
Alain Filloux
Centre National de la Recherche Scientifique · FRLaboratoire d'Ingénierie des Systèmes Macromoléculaires

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several subclasses of type IV pili have been described according to the characteristics of the structural prepilin subunit. Whereas molecular mechanisms of type IVa pilus assembly have been well documented for Pseudomonas aeruginosa and involve the PilD prepilin peptidase, no type IVb pili have been described in this microorganism. One subclass of type IVb prepilins has been identified as the Flp prepilin subfamily. Long and bundled Flp pili involved in tight adherence have been identified in Actinobacillus actinomycetemcomitans, for which assembly was due to a dedicated machinery encoded by the tad-rcp locus. A similar flp-tad-rcp locus containing flp, tad, and rcp gene homologues was identified in the P. aeruginosa genome. The function of these genes has been investigated, which revealed their involvement in the formation of extracellular Flp appendages. We also identified a gene (designated by open reading frame PA4295) outside the flp-tad-rcp locus, that we named fppA, encoding a novel prepilin peptidase. This is the second enzyme of this kind found in P. aeruginosa; however, it appears to be truncated and is similar to the C-terminal domain of the previously characterized PilD peptidase. In this study, we show that FppA is responsible for the maturation of the Flp prepilin and belongs to the aspartic acid protease family. We also demonstrate that FppA is required for the assembly of cell surface appendages that we called Flp pili. Finally, we observed an Flp-dependent bacterial aggregation process on the epithelial cell surface and an increased biofilm phenotype linked to Flp pilus assembly.

Indexed as

Amino Acid SequenceAspartic Acid EndopeptidasesBacterial ProteinsBiofilmsEndopeptidasesFimbriae, BacterialFimbriae ProteinsMolecular Sequence DataOpen Reading FramesPseudomonas aeruginosaSequence AlignmentAspartic Acid EndopeptidasesBacterial ProteinsEndopeptidasesFimbriae ProteinsFlp protein, bacteriaprepilin peptidase protein, Bacteria

Identifiers

PMID16788194
PMCPMC1483019
OpenAlexW2150011050

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.