Evidence map›Paper›PMID 33219282›Full record

ArticleCommunications biology2020

New insights in the coordinated amidase and glucosaminidase activity of the major autolysin (Atl) in Staphylococcus aureus.

Mulugeta Nega, Paula Maria Tribelli, Katharina Hipp, Mark Stahl, Friedrich Götz

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
0.7field-weighted citation impact, top 18% 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

30 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. 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
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Beyond the double helix: the multifaceted landscape of extracellular DNA inFrontiers in cellular and infection microbiology · 2024
    Review
  15. Article
  16. A Clinically Selected Staphylococcus aureusAntimicrobial agents and chemotherapy · 2023
    Article
  17. Identification of FacZ as a division site placement factor inbioRxiv : the preprint server for biology · 2023
    Article
  18. Autolysin-mediated peptidoglycan hydrolysis is required for the surface display ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Review
  20. Review
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

5 authors at 3 institutions in 2 countries.

Mulugeta NegaMicrobial Genetics, Interfaculty Institute of Microbiology and Infection Medicine Tübingen (IMIT), University of Tübingen, Auf der Morgenstelle 28, D-72076, Tübingen, Germany.
Paula Maria TribelliMicrobial Genetics, Interfaculty Institute of Microbiology and Infection Medicine Tübingen (IMIT), University of Tübingen, Auf der Morgenstelle 28, D-72076, Tübingen, Germany.
Katharina HippMax Planck Institute for Developmental Biology, Max-Planck-Ring 5, D-72076, Tübingen, Germany.ORCID 0000-0002-1493-9698
Mark StahlZentrum für Molekularbiologie der Pflanzen (ZMBP), University of Tübingen, Auf der Morgenstelle 32, D-72076, Tübingen, Germany.
Friedrich GötzMicrobial Genetics, Interfaculty Institute of Microbiology and Infection Medicine Tübingen (IMIT), University of Tübingen, Auf der Morgenstelle 28, D-72076, Tübingen, Germany. friedrich.goetz@uni-tuebingen.de.ORCID 0000-0002-2042-0518
University of Tübingen · DEInstituto de Química y Fisicoquímica Biológicas · ARMax Planck Institute for Developmental Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

After bacterial cell division, the daughter cells are still covalently interlinked by the peptidoglycan network which is resolved by specific hydrolases (autolysins) to release the daughter cells. In staphylococci, the major autolysin (Atl) with its two domain enzymes, N-acetylmuramyl-L-alanine amidase (AmiA) and β-N-acetylglucosaminidase (GlcA), resolves the peptidoglycan to release the daughter cells. Internal deletions in each of the enzyme domains revealed defined morphological alterations such as cell cluster formation in ΔamiA, ΔglcA and Δatl, and asymmetric cell division in the ΔglcA. A most important finding was that GlcA activity requires the prior removal of the stem peptide by AmiA for its activity thus the naked glycan strand is its substrate. Furthermore, GlcA is not an endo-β-N-acetylglucosaminidase but an exo-enzyme that cuts the glycan backbone to disaccharides independent of its O-acetylation modification. Our results shed new light into the sequential peptidoglycan hydrolysis by AmiA and GlcA during cell division in staphylococci.

Indexed as

AmidohydrolasesBacterial ProteinsGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicHexosaminidasesMuramidaseMutationN-Acetylmuramoyl-L-alanine AmidaseStaphylococcus aureusamidaseAmidohydrolasesBacterial ProteinsHexosaminidasesMuramidaseN-Acetylmuramoyl-L-alanine Amidase

Identifiers

PMID33219282
PMCPMC7679415
OpenAlexW3104677386

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.