Evidence map›Paper›PMID 37255442›Full record

ArticleMicrobiology spectrum2023

Characterization of Pseudomonas aeruginosa l,d-Transpeptidases and Evaluation of Their Role in Peptidoglycan Adaptation to Biofilm Growth.

Inès Hugonneau-Beaufet, Jean-Philippe Barnier, Stanislas Thiriet-Rupert, Sylvie Létoffé, Jean-Luc Mainardi, Jean-Marc Ghigo, Christophe Beloin, Michel Arthur

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

11 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. Outer Membrane-Peptidoglycan Anchoring inJournal of the American Chemical Society · 2026
    Article
  4. Article
  5. Article
  6. Biochemistry · 2025
    Article
  7. Article
  8. Article
  9. Bacterial peptidoglycan as a living polymer.Current opinion in chemical biology · 2025
    Review
  10. Review
  11. 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

8 authors at 2 institutions in 1 country.

Inès Hugonneau-BeaufetCentre de Recherche des Cordeliers, Sorbonne Université, INSERM, Université Paris Cité, Paris, France.
Jean-Philippe BarnierCentre de Recherche des Cordeliers, Sorbonne Université, INSERM, Université Paris Cité, Paris, France.
Stanislas Thiriet-RupertInstitut Pasteur, Université Paris Cité, UMR CNRS 6047, Genetics of Biofilms Laboratory, Paris, France.
Sylvie LétofféInstitut Pasteur, Université Paris Cité, UMR CNRS 6047, Genetics of Biofilms Laboratory, Paris, France.
Jean-Luc MainardiCentre de Recherche des Cordeliers, Sorbonne Université, INSERM, Université Paris Cité, Paris, France.
Jean-Marc GhigoInstitut Pasteur, Université Paris Cité, UMR CNRS 6047, Genetics of Biofilms Laboratory, Paris, France.
Christophe BeloinInstitut Pasteur, Université Paris Cité, UMR CNRS 6047, Genetics of Biofilms Laboratory, Paris, France.ORCID 0000-0002-0344-3443
Michel ArthurCentre de Recherche des Cordeliers, Sorbonne Université, INSERM, Université Paris Cité, Paris, France.ORCID 0000-0003-1007-636X
Centre National de la Recherche Scientifique · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptidoglycan is an essential component of the bacterial cell envelope that sustains the turgor pressure of the cytoplasm, determines cell shape, and acts as a scaffold for the anchoring of envelope polymers such as lipoproteins. The final cross-linking step of peptidoglycan polymerization is performed by classical d,d-transpeptidases belonging to the penicillin-binding protein (PBP) family and by l,d-transpeptidases (LDTs), which are dispensable for growth in most bacterial species and whose physiological functions remain elusive. In this study, we investigated the contribution of LDTs to cell envelope synthesis in Pseudomonas aeruginosa grown in planktonic and biofilm conditions. We first assigned a function to each of the three P. aeruginosa LDTs by gene inactivation in P. aeruginosa, heterospecific gene expression in Escherichia coli, and, for one of them, direct determination of its enzymatic activity. We found that the three P. aeruginosa LDTs catalyze peptidoglycan cross-linking (Ldt

Indexed as

Peptidyl TransferasesBacterial ProteinsEdetic AcidEscherichia coliPenicillin-Binding ProteinsPeptidoglycanPseudomonas aeruginosaBacterial ProteinsEdetic AcidPenicillin-Binding ProteinsPeptidoglycanPeptidyl Transferasesbiofilmsl,d-transpeptidaseslipoproteinspeptidoglycan

Identifiers

PMID37255442
PMCPMC10434034
OpenAlexW4378781126

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.