Evidence map›Paper›PMID 25690098›Full record

ArticleInfection and immunity2015

Pharmacological activation of Rap1 antagonizes the endothelial barrier disruption induced by exotoxins ExoS and ExoT of Pseudomonas aeruginosa.

Stéphanie Bouillot, Ina Attrée, Philippe Huber

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Rap1 in endothelial biology.Current opinion in hematology · 2017
    Review
  7. Frontiers in cellular and infection microbiology · 2017
    Review
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

3 authors at 3 institutions in 1 country.

Stéphanie BouillotUniversité Grenoble Alpes, Grenoble, France, CNRS, ERL5261, Grenoble, France, CEA, iRTSV-BCI, Grenoble, France, and INSERM, U1036, Grenoble, France.
Ina AttréeUniversité Grenoble Alpes, Grenoble, France, CNRS, ERL5261, Grenoble, France, CEA, iRTSV-BCI, Grenoble, France, and INSERM, U1036, Grenoble, France.
Philippe HuberUniversité Grenoble Alpes, Grenoble, France, CNRS, ERL5261, Grenoble, France, CEA, iRTSV-BCI, Grenoble, France, and INSERM, U1036, Grenoble, France phuber@cea.fr.
CEA Grenoble · FRInserm · FRUniversité Grenoble Alpes · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most clinical strains of Pseudomonas aeruginosa, a leading agent of nosocomial infections, are multiresistant to antibiotherapy. Because of the paucity of new available antibiotics, the investigation of strategies aimed at limiting the action of its major virulence factors has gained much interest. The type 3 secretion system of P. aeruginosa and its effectors are known to be major determinants of toxicity and are required for bacterial dissemination in the host. Bacterial transmigration across the vascular wall is considered to be an important step in the infectious process. Using human endothelial primary cells, we demonstrate that forskolin (FSK), a drug inducing cyclic AMP (cAMP) elevation in eukaryotic cells, strikingly reduced the cell retraction provoked by two type 3 toxins, ExoS and ExoT, found in the majority of clinical strains. Conversely, cytotoxicity of a strain carrying the type 3 effector ExoU was unaffected by FSK. In addition, FSK altered the capacity of two ExoS/ExoT strains to transmigrate across cell monolayers. In agreement with these findings, other drugs and a cytokine inducing the increase of cAMP intracellular levels have also protected cells from retraction. cAMP is an activator of both protein kinase A and EPAC, a GTPase exchange factor of Rap1. Using activators or inhibitors of either pathway, we show that the beneficial effect of FSK is exerted by the activation of the EPAC/Rap1 axis, suggesting that its protective effect is mediated by reinforcing cell-cell and cell-substrate adhesion.

Indexed as

ADP Ribose TransferasesBacterial ToxinsCells, CulturedColforsinEndothelial CellsEnzyme ActivatorsGTPase-Activating ProteinsHumansPseudomonas aeruginosaShelterin ComplexTelomere-Binding ProteinsADP Ribose TransferasesBacterial ToxinsColforsinEnzyme Activatorsexoenzyme SExoT protein, Pseudomonas aeruginosaGTPase-Activating ProteinsShelterin ComplexTelomere-Binding ProteinsTERF2IP protein, human

Identifiers

PMID25690098
PMCPMC4399046
OpenAlexW2129851905

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.