Evidence map›Paper›PMID 34006648›Full record

ArticlemBio2021

Ser/Thr Kinase-Dependent Phosphorylation of the Peptidoglycan Hydrolase CwlA Controls Its Export and Modulates Cell Division in Clostridioides difficile.

Transito Garcia-Garcia, Sandrine Poncet, Elodie Cuenot, Thibaut Douché, Quentin Giai Gianetto, Johann Peltier, Pascal Courtin, Marie-Pierre Chapot-Chartier, Mariette Matondo, Bruno Dupuy and 2 more

Abstract read
In one paragraph

Article in mBio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Unique growth and morphology properties of Clade 5bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Review
  7. Review
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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

12 authors.

Transito Garcia-GarciaLaboratoire Pathogénese des Bactéries Anaérobies, Institut Pasteur, UMR CNRS 2001, Université de Paris, Paris, France.
Sandrine PoncetUniversité Paris-Saclay, INRAE, AgroParisTech, Micalis Institute, Jouy-en-Josas, France.
Elodie CuenotLaboratoire Pathogénese des Bactéries Anaérobies, Institut Pasteur, UMR CNRS 2001, Université de Paris, Paris, France.
Thibaut DouchéPlateforme Protéomique, Unité de Technologie et Service Spectrométrie de Masse pour la Biologie, CNRS USR 2000, Institut Pasteur, Paris, France.
Quentin Giai GianettoPlateforme Protéomique, Unité de Technologie et Service Spectrométrie de Masse pour la Biologie, CNRS USR 2000, Institut Pasteur, Paris, France.
Johann PeltierLaboratoire Pathogénese des Bactéries Anaérobies, Institut Pasteur, UMR CNRS 2001, Université de Paris, Paris, France.ORCID 0000-0003-3207-9465
Pascal CourtinUniversité Paris-Saclay, INRAE, AgroParisTech, Micalis Institute, Jouy-en-Josas, France.
Marie-Pierre Chapot-ChartierUniversité Paris-Saclay, INRAE, AgroParisTech, Micalis Institute, Jouy-en-Josas, France.ORCID 0000-0002-4947-0519
Mariette MatondoPlateforme Protéomique, Unité de Technologie et Service Spectrométrie de Masse pour la Biologie, CNRS USR 2000, Institut Pasteur, Paris, France.
Bruno DupuyLaboratoire Pathogénese des Bactéries Anaérobies, Institut Pasteur, UMR CNRS 2001, Université de Paris, Paris, France.
Thomas CandelaUniversité Paris-Saclay, INRAE, AgroParisTech, Micalis Institute, Jouy-en-Josas, France.
Isabelle Martin-VerstraeteLaboratoire Pathogénese des Bactéries Anaérobies, Institut Pasteur, UMR CNRS 2001, Université de Paris, Paris, France isabelle.martin-verstraete@pasteur.fr.ORCID 0000-0002-8376-7690

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell growth and division require a balance between synthesis and hydrolysis of the peptidoglycan (PG). Inhibition of PG synthesis or uncontrolled PG hydrolysis can be lethal for the cells, making it imperative to control peptidoglycan hydrolase (PGH) activity. The synthesis or activity of several key enzymes along the PG biosynthetic pathway is controlled by the Hanks-type serine/threonine kinases (STKs). In Gram-positive bacteria, inactivation of genes encoding STKs is associated with a range of phenotypes, including cell division defects and changes in cell wall metabolism, but only a few kinase substrates and associated mechanisms have been identified. We previously demonstrated that STK-PrkC plays an important role in cell division, cell wall metabolism, and resistance to antimicrobial compounds in the human enteropathogen

Indexed as

Signal TransductionBacterial ProteinsCell DivisionClostridioides difficileN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanPhosphorylationProtein Serine-Threonine KinasesBacterial ProteinsN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanProtein Serine-Threonine Kinasesanaerobescell divisioncell wallcell wall hydrolasesClostridium difficilecontrol of exportationenvelope homeostasisHanks kinasekinasespeptidoglycanphosphorylationprotein phosphorylation

Identifiers

PMID34006648
PMCPMC8262956

What OpenQuestion holds

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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.