Evidence map›Paper›PMID 37692163›Full record

ArticleFrontiers in cellular and infection microbiology2023

Amidation of glutamate residues in mycobacterial peptidoglycan is essential for cell wall cross-linking.

Moagi T Shaku, Karl L Ocius, Alexis J Apostolos, Marcos M Pires, Michael S VanNieuwenhze, Neeraj Dhar, Bavesh D Kana

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cellular and infection microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

13 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Activity Profiling of Mycobacterial L,D-Transpeptidases.bioRxiv : the preprint server for biology · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. 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

7 authors at 5 institutions in 3 countries.

Moagi T ShakuDSI/NRF Centre of Excellence for Biomedical Tuberculosis (TB) Research, Faculty of Health Sciences, University of the Witwatersrand, National Health Laboratory Service, Johannesburg, South Africa.
Karl L OciusDepartment of Chemistry, University of Virginia, Charlottesville, VA, United States.
Alexis J ApostolosDepartment of Chemistry, University of Virginia, Charlottesville, VA, United States.
Marcos M PiresDepartment of Chemistry, University of Virginia, Charlottesville, VA, United States.
Michael S VanNieuwenhzeDepartment of Chemistry, Indiana University Bloomington, Bloomington, IN, United States.
Neeraj DharGlobal Health Institute, Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.
Bavesh D KanaDSI/NRF Centre of Excellence for Biomedical Tuberculosis (TB) Research, Faculty of Health Sciences, University of the Witwatersrand, National Health Laboratory Service, Johannesburg, South Africa.
University of Virginia · USÉcole Polytechnique Fédérale de Lausanne · CHIndiana University Bloomington · USNational Health Laboratory Service · ZAUniversity of the Witwatersrand · ZA

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Introduction: Mycobacteria assemble a complex cell wall with cross-linked peptidoglycan (PG) which plays an essential role in maintenance of cell wall integrity and tolerance to osmotic pressure. We previously demonstrated that various hydrolytic enzymes are required to remodel PG during essential processes such as cell elongation and septal hydrolysis. Here, we explore the chemistry associated with PG cross-linking, specifically the requirement for amidation of the D-glutamate residue found in PG precursors. Methods: Synthetic fluorescent probes were used to assess PG remodelling dynamics in live bacteria. Fluorescence microscopy was used to assess protein localization in live bacteria and CRISPR-interference was used to construct targeted gene knockdown strains. Time-lapse microscopy was used to assess bacterial growth. Western blotting was used to assess protein phosphorylation. Results and discussion: In

Indexed as

AmidesCell WallGlutamic AcidMycobacterium smegmatisPeptidoglycanBacterial ProteinsCarbon-Nitrogen Ligases with Glutamine as Amide-N-DonorAmidesBacterial ProteinsCarbon-Nitrogen Ligases with Glutamine as Amide-N-DonorGlutamic AcidPeptidoglycanMurT-GatD complexpeptidoglycan amidationpeptidoglycan biosynthesispeptidoglycan cross-linkingpeptidoglycan remodelling

Identifiers

PMID37692163
PMCPMC10484409
OpenAlexW4386122247

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.