Evidence map›Paper›PMID 24082078›Full record

ArticleInfection and immunity2013

The Pseudomonas aeruginosa periplasmic protease CtpA can affect systems that impact its ability to mount both acute and chronic infections.

Jin Seo, Andrew J Darwin

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

27 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  4. Control of theJournal of bacteriology · 2025
    Article
  5. Tail-specific protease is an essentialInfection and immunity · 2024
    Article
  6. Journal of bacteriology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Review
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  12. Article
  13. Cell Envelope Stress Response in Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022
    Article
  14. Article
  15. Article
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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

2 authors at 1 institution in 1 country.

Jin SeoDepartment of Microbiology, New York University School of Medicine, New York, New York, USA.
Andrew J Darwin
New York University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteases play important roles in the virulence of Pseudomonas aeruginosa. Some are exported to act on host targets and facilitate tissue destruction and bacterial dissemination. Others work within the bacterial cell to process virulence factors and regulate virulence gene expression. Relatively little is known about the role of one class of bacterial serine proteases known as the carboxyl-terminal processing proteases (CTPs). The P. aeruginosa genome encodes two CTPs annotated as PA3257/Prc and PA5134/CtpA in strain PAO1. Prc degrades mutant forms of the anti-sigma factor MucA to promote mucoidy in some cystic fibrosis lung isolates. However, nothing is known about the role or importance of CtpA. We have now found that endogenous CtpA is a soluble periplasmic protein and that a ctpA null mutant has specific phenotypes consistent with an altered cell envelope. Although a ctpA null mutation has no major effect on bacterial growth in the laboratory, CtpA is essential for the normal function of the type 3 secretion system (T3SS), for cytotoxicity toward host cells, and for virulence in a mouse model of acute pneumonia. Conversely, increasing the amount of CtpA above its endogenous level induces an uncharacterized extracytoplasmic function sigma factor regulon, an event that has been reported to attenuate P. aeruginosa in a rat model of chronic lung infection. Therefore, a normal level of CtpA activity is critical for T3SS function and acute virulence, whereas too much activity can trigger an apparent stress response that is detrimental to chronic virulence.

Indexed as

Algal ProteinsAnimalsBacterial ProteinsBacterial Secretion SystemsCarboxypeptidasesCHO CellsCricetulusEndopeptidasesFemaleGene Expression Regulation, BacterialMiceMice, Inbred BALB CPneumoniaProprotein ConvertasesPseudomonas aeruginosaPseudomonas InfectionsAlgal ProteinsBacterial ProteinsBacterial Secretion SystemsCarboxypeptidasesC-terminal processing peptidaseEndopeptidasesphotosystem II, D1 polypeptide carboxy-terminal processing proteaseProprotein ConvertasesSigma Factor

Identifiers

PMID24082078
PMCPMC3837984
OpenAlexW2157756878

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.