Evidence map›Paper›PMID 30873139›Full record

ReviewFrontiers in microbiology2019

Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.

Aurore Vermassen, Sabine Leroy, Régine Talon, Christian Provot, Magdalena Popowska, Mickaël Desvaux

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 201 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
201citing papers in PubMed, 1 pooled it
51.8field-weighted citation impact, top 1% 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

201 citing papers in PubMed, 1 synthesis or guideline pooled it, 351 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Draft genome sequence ofMicrobiology resource announcements · 2026
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  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. How Bioactive Glass S53P4 Kills Bacteria.Journal of functional biomaterials · 2026
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. The innate immune protein calprotectin ablates the bactericidal activity of β-lactam antibiotics.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  16. Secretome Profiling ofAntibiotics (Basel, Switzerland) · 2026
    Article
  17. Article
  18. Article
  19. Article
  20. Proteomic Analysis of the Differential Response ofAntibiotics (Basel, Switzerland) · 2025
    Article

141 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Aurore VermassenUniversité Clermont Auvergne, INRA, MEDiS, Clermont-Ferrand, France.
Sabine LeroyUniversité Clermont Auvergne, INRA, MEDiS, Clermont-Ferrand, France.
Régine TalonUniversité Clermont Auvergne, INRA, MEDiS, Clermont-Ferrand, France.
Christian ProvotBioFilm Control SAS, Saint-Beauzire, France.
Magdalena PopowskaDepartment of Applied Microbiology, Faculty of Biology, Institute of Microbiology, University of Warsaw, Warsaw, Poland.
Mickaël DesvauxUniversité Clermont Auvergne, INRA, MEDiS, Clermont-Ferrand, France.
Université Clermont Auvergne · FRInstitut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement · FRUniversity of Warsaw · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cell wall (CW) of bacteria is an intricate arrangement of macromolecules, at least constituted of peptidoglycan (PG) but also of (lipo)teichoic acids, various polysaccharides, polyglutamate and/or proteins. During bacterial growth and division, there is a constant balance between CW degradation and biosynthesis. The CW is remodeled by bacterial hydrolases, whose activities are carefully regulated to maintain cell integrity or lead to bacterial death. Each cell wall hydrolase (CWH) has a specific role regarding the PG: (i) cell wall amidase (CWA) cleaves the amide bond between N-acetylmuramic acid and L-alanine residue at the N-terminal of the stem peptide, (ii) cell wall glycosidase (CWG) catalyses the hydrolysis of the glycosidic linkages, whereas (iii) cell wall peptidase (CWP) cleaves amide bonds between amino acids within the PG chain. After an exhaustive overview of all known conserved catalytic domains responsible for CWA, CWG, and CWP activities, this review stresses that the CWHs frequently display a modular architecture combining multiple and/or different catalytic domains, including some lytic transglycosylases as well as CW binding domains. From there, direct physiological and collateral roles of CWHs in bacterial cells are further discussed.

Indexed as

bacterial cell wallbacterial division and growthcell lysiscell wall binding domainscell wall remodelingpeptidoglycan (PG) hydrolasesprotein modules

Identifiers

PMID30873139
PMCPMC6403190
OpenAlexW2920691960

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.