Evidence map›Paper›PMID 34382698›Full record

ArticleThe EMBO journal2021

Role of endopeptidases in peptidoglycan synthesis mediated by alternative cross-linking enzymes in Escherichia coli.

Henri Voedts, Delphine Dorchêne, Adam Lodge, Waldemar Vollmer, Michel Arthur, Jean-Emmanuel Hugonnet

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Peptidoglycan LD-Transpeptidases.Antibiotics (Basel, Switzerland) · 2025
    Review
  3. Article
  4. International journal of systematic and evolutionary microbiology · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Basal level of ppGpp coordinatesMicrobial cell (Graz, Austria) · 2023
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. 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

6 authors at 2 institutions in 2 countries.

Henri VoedtsCentre de Recherche des Cordeliers, Sorbonne Université, Inserm, Université de Paris, Paris, France.
Delphine DorchêneCentre de Recherche des Cordeliers, Sorbonne Université, Inserm, Université de Paris, Paris, France.
Adam LodgeCentre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.
Waldemar VollmerCentre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle Upon Tyne, UK.ORCID 0000-0003-0408-8567
Michel ArthurCentre de Recherche des Cordeliers, Sorbonne Université, Inserm, Université de Paris, Paris, France.
Jean-Emmanuel HugonnetCentre de Recherche des Cordeliers, Sorbonne Université, Inserm, Université de Paris, Paris, France.ORCID 0000-0003-4150-0944
Inserm · FRNewcastle University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria resist to the turgor pressure of the cytoplasm through a net-like macromolecule, the peptidoglycan, made of glycan strands connected via peptides cross-linked by penicillin-binding proteins (PBPs). We recently reported the emergence of β-lactam resistance resulting from a bypass of PBPs by the YcbB L,D-transpeptidase (LdtD), which form chemically distinct 3→3 cross-links compared to 4→3 formed by PBPs. Here we show that peptidoglycan expansion requires controlled hydrolysis of cross-links and identify among eight endopeptidase paralogues the minimum enzyme complements essential for bacterial growth with 4→3 (MepM) and 3→3 (MepM and MepK) cross-links. Purified Mep endopeptidases unexpectedly displayed a 4→3 and 3→3 dual specificity implying recognition of a common motif in the two cross-link types. Uncoupling of the polymerization of glycan chains from the 4→3 cross-linking reaction was found to facilitate the bypass of PBPs by YcbB. These results illustrate the plasticity of the peptidoglycan polymerization machinery in response to the selective pressure of β-lactams.

Indexed as

Anti-Bacterial Agentsbeta-Lactam ResistanceCatalysisEndopeptidasesEnzyme ActivationEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicHydrolysisMass SpectrometryMembrane ProteinsMutationPeptidoglycanPeptidyl TransferasesAnti-Bacterial AgentsBlr protein, E coliEndopeptidasesEscherichia coli ProteinsMembrane ProteinsPeptidoglycanPeptidyl TransferasesYcbB protein, E coliendopeptidaseEscherichia coliL,D-transpeptidasepeptidoglycanβ-lactam

Identifiers

PMID34382698
PMCPMC8488565
OpenAlexW3189217299

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.