Evidence map›Paper›PMID 37418323›Full record

ArticleCell reports2023

Molecular basis of the final step of cell division in Streptococcus pneumoniae.

Siseth Martínez-Caballero, Céline Freton, Rafael Molina, Sergio G Bartual, Virginie Gueguen-Chaignon, Chryslène Mercy, Federico Gago, Kiran V Mahasenan, Inés G Muñoz, Mijoon Lee and 4 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
4.5field-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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. [Advances in the Regulation of Protein Phosphorylation in Streptococcal Cell Wall Synthesis].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2026
    Review
  5. Review
  6. Article
  7. Clinical microbiology reviews · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Article
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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

14 authors at 5 institutions in 3 countries.

Siseth Martínez-CaballeroDepartment of Crystallography and Structural Biology, Instituto de Química-Física "Rocasolano," Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Céline FretonMolecular Microbiology and Structural Biochemistry, UMR 5086, Université de Lyon, CNRS, Lyon, France.
Rafael MolinaDepartment of Crystallography and Structural Biology, Instituto de Química-Física "Rocasolano," Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Sergio G BartualDepartment of Crystallography and Structural Biology, Instituto de Química-Física "Rocasolano," Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Virginie Gueguen-ChaignonSFR Biosciences, Université de Lyon, CNRS UAR3444, ENS de Lyon, INSERM US8, Lyon, France.
Chryslène MercyMolecular Microbiology and Structural Biochemistry, UMR 5086, Université de Lyon, CNRS, Lyon, France.
Federico GagoDepartment of Biomedical Sciences & Instituto de Química Médica-CSIC Associated Unit, School of Medicine and Health Sciences, University of Alcalá, 28805 Alcalá de Henares, Spain.
Kiran V MahasenanDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
Inés G MuñozStructural Biology Program, Spanish National Cancer Research Center (CNIO), 28029 Madrid, Spain.
Mijoon LeeDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
Dusan HesekDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
Shahriar MobasheryDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
Juan A HermosoDepartment of Crystallography and Structural Biology, Instituto de Química-Física "Rocasolano," Consejo Superior de Investigaciones Científicas, Madrid, Spain. Electronic address: xjuan@iqfr.csic.es.
Christophe GrangeasseMolecular Microbiology and Structural Biochemistry, UMR 5086, Université de Lyon, CNRS, Lyon, France. Electronic address: christophe.grangeasse@ibcp.fr.
Consejo Superior de Investigaciones Científicas · ESUniversité Claude Bernard Lyon 1 · FRUniversity of Notre Dame · USSpanish National Cancer Research Centre · ESUniversidad de Alcalá · ES

Funding

Murine Model of Human Hepatitis AR01AI131685 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LEMON, STANLEY M., WHITMIRE, JASON KYLE · 2017 to 2021
$1.9M
Cell-Wall Recycling and Nexus to Antibiotic ResistanceR35GM131685 · NIGMS · UNIVERSITY OF NOTRE DAME · PI MOBASHERY, SHAHRIAR · 2019 to 2023
$1.9M
NIAID NIH HHS R01 AI131685NIGMS NIH HHS R35 GM131685
6 · The paper itself

Abstract

Bacterial cell-wall hydrolases must be tightly regulated during bacterial cell division to prevent aberrant cell lysis and to allow final separation of viable daughter cells. In a multidisciplinary work, we disclose the molecular dialogue between the cell-wall hydrolase LytB, wall teichoic acids, and the eukaryotic-like protein kinase StkP in Streptococcus pneumoniae. After characterizing the peptidoglycan recognition mode by the catalytic domain of LytB, we further demonstrate that LytB possesses a modular organization allowing the specific binding to wall teichoic acids and to the protein kinase StkP. Structural and cellular studies notably reveal that the temporal and spatial localization of LytB is governed by the interaction between specific modules of LytB and the final PASTA domain of StkP. Our data collectively provide a comprehensive understanding of how LytB performs final separation of daughter cells and highlights the regulatory role of eukaryotic-like kinases on lytic machineries in the last step of cell division in streptococci.

Indexed as

Protein Serine-Threonine KinasesStreptococcus pneumoniaeBacterial ProteinsCell DivisionCell WallHydrolasesProtein KinasesTeichoic AcidsBacterial ProteinsHydrolasesProtein KinasesProtein Serine-Threonine KinasesTeichoic Acidsbacterial divisioncell wallCP: MicrobiologycrystallographyLytBmolecular dynamicspeptidoglycanSAXSStkPStreptococcus pneumoniaeteichoic acid

Identifiers

PMID37418323
PMCPMC10434722
OpenAlexW4383313768

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.