Evidence map›Paper›PMID 37660104›Full record

ArticleNature communications2023

Coordinated peptidoglycan synthases and hydrolases stabilize the bacterial cell wall.

Huan Zhang, Srutha Venkatesan, Emily Ng, Beiyan Nan

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
8.8field-weighted citation impact, top 2% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Structural Insights into MltC fromJournal of microbiology and biotechnology · 2026
    Article
  4. Article
  5. Journal of bacteriology · 2025
    Article
  6. Milestones in the development ofJournal of bacteriology · 2025
    Review
  7. Tissue-like structures formed by a bacterium.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Article
  10. Bacterial peptidoglycan as a living polymer.Current opinion in chemical biology · 2025
    Review
  11. Review
  12. Article
  13. AlgU mediates hyperosmotic tolerance inApplied and environmental microbiology · 2024
    Article
  14. Article
  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Huan Zhang *Department of Biology, Texas A&M University, College Station, TX, 77843, USA.
Srutha Venkatesan *Department of Biology, Texas A&M University, College Station, TX, 77843, USA.
Emily NgDepartment of Biology, Texas A&M University, College Station, TX, 77843, USA.
Beiyan NanDepartment of Biology, Texas A&M University, College Station, TX, 77843, USA. bnan@tamu.edu.ORCID http://orcid.org/0000-0002-0326-9529
Texas A&M University · US

Funding

The Origin of Rod Shape in BacteriaR01GM129000 · NIGMS · TEXAS A&M UNIVERSITY · PI NAN, BEIYAN · 2018 to 2022
$1.6M
NIGMS NIH HHS R01 GM129000
6 · The paper itself

Abstract

Peptidoglycan (PG) defines cell shape and protects bacteria against osmotic stress. The growth and integrity of PG require coordinated actions between synthases that insert new PG strands and hydrolases that generate openings to allow the insertion. However, the mechanisms of their coordination remain elusive. Moenomycin that inhibits a family of PG synthases known as Class-A penicillin-binding proteins (aPBPs), collapses rod shape despite aPBPs being non-essential for rod-like morphology in the bacterium Myxococcus xanthus. Here, we demonstrate that inhibited PBP1a2, an aPBP, accelerates the degradation of cell poles by DacB, a hydrolytic PG peptidase. Moenomycin promotes the binding between DacB and PG and thus reduces the mobility of DacB through PBP1a2. Conversely, DacB also regulates the distribution and dynamics of aPBPs. Our findings clarify the action of moenomycin and suggest that disrupting the coordination between PG synthases and hydrolases could be more lethal than eliminating individual enzymes.

Indexed as

BambermycinsMyxococcus xanthusCell WallNitric Oxide SynthasePenicillin-Binding ProteinsPeptide HydrolasesPeptidoglycanBambermycinsNitric Oxide SynthasePenicillin-Binding ProteinsPeptide HydrolasesPeptidoglycan

Identifiers

PMID37660104
PMCPMC10475089
OpenAlexW4386398777

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.