Evidence map›Paper›PMID 33824203›Full record

ArticlemBio2021

Class A Penicillin-Binding Protein-Mediated Cell Wall Synthesis Promotes Structural Integrity during Peptidoglycan Endopeptidase Insufficiency in Vibrio cholerae.

Shannon G Murphy, Andrew N Murtha, Ziyi Zhao, Laura Alvarez, Peter Diebold, Jung-Ho Shin, Michael S VanNieuwenhze, Felipe Cava, Tobias Dörr

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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Non-O1/Non-O139Microorganisms · 2024
    Review
  8. Structural Insights into the Penicillin-Binding Protein 4 (DacB) fromInternational journal of molecular sciences · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

9 authors.

Shannon G MurphyWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York, USA.ORCID 0000-0003-4544-1400
Andrew N MurthaWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York, USA.
Ziyi ZhaoWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York, USA.
Laura AlvarezThe Laboratory for Molecular Infection Medicine Sweden (MIMS), Department of Molecular Biology, Umeå University, Umeå, Sweden.
Peter DieboldDepartment of Microbiology, Cornell University, Ithaca, New York, USA.
Jung-Ho ShinWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York, USA.
Michael S VanNieuwenhzeDepartment of Molecular and Cellular Biochemistry and Department of Biology, Indiana University, Bloomington, Indiana, USA.
Felipe CavaThe Laboratory for Molecular Infection Medicine Sweden (MIMS), Department of Molecular Biology, Umeå University, Umeå, Sweden.ORCID 0000-0001-5995-718X
Tobias DörrWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York, USA tdoerr@cornell.edu.ORCID 0000-0003-3283-9161

Funding

Dynamics of bacterial peptidoglycan synthesisR01GM113172 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI BRUN, YVES V, VANNIEUWENHZE, MICHAEL S · 2015 to 2018
$3.5M
Supplement to Chemical Biology Studies of the Dynamics and Inhibition of Peptidoglycan BiosynthesisR35GM136365 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI VANNIEUWENHZE, MICHAEL S · 2020 to 2024
$2.0M
The mechanism of autolysin regulation in Vibrio choleraeR01GM130971 · NIGMS · CORNELL UNIVERSITY · PI DOERR, TOBIAS · 2019 to 2025
$2.0M
NIGMS NIH HHS R01 GM113172NIGMS NIH HHS R01 GM130971NIGMS NIH HHS R35 GM136365
6 · The paper itself

Abstract

The bacterial cell wall is composed primarily of peptidoglycan (PG), a poly-aminosugar that is essential to sustain cell shape, growth, and structural integrity. PG is synthesized by class A/B penicillin-binding proteins (a/bPBPs) and shape, elongation, division, and sporulation (SEDS) proteins like RodA (as part of the Rod system cell elongation machinery) and degraded by "autolytic" enzymes to accommodate growth processes. It is thought that autolysins (particularly endopeptidases [EPs]) are required for PG synthesis and incorporation by creating gaps that are patched and paved by PG synthases, but the exact relationship between autolysins and PG synthesis remains incompletely understood. Here, we have probed the consequences of EP depletion for PG synthesis in the diarrheal pathogen

Indexed as

Bacterial ProteinsCell WallEndopeptidasesPenicillin-Binding ProteinsPeptidoglycanVibrio choleraeBacterial ProteinsEndopeptidasesPenicillin-Binding ProteinsPeptidoglycanpeptidoglycan endopeptidaseautolysincell wallendopeptidaseLysMM23mreBpenicillin-binding proteinpenicillin-binding proteinspeptidoglycan

Identifiers

PMID33824203
PMCPMC8092314

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.