Evidence map›Paper›PMID 35073258›Full record

ArticleeLife2022

Lytic transglycosylases mitigate periplasmic crowding by degrading soluble cell wall turnover products.

Anna Isabell Weaver, Laura Alvarez, Kelly M Rosch, Asraa Ahmed, Garrett Sean Wang, Michael S van Nieuwenhze, Felipe Cava, Tobias Dörr

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
75.1field-weighted citation impact, top 1% 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

32 citing papers in PubMed, 351 citations in OpenAlex.

  1. Review
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  10. Perturbation ofmBio · 2025
    Article
  11. Bacterial peptidoglycan as a living polymer.Current opinion in chemical biology · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024
    Article
  18. Article
  19. Article
  20. 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

8 authors at 3 institutions in 2 countries.

Anna Isabell WeaverWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.ORCID 0000-0002-0556-0336
Laura AlvarezThe Laboratory for Molecular Infection Medicine Sweden (MIMS), Department of Molecular Biology, Umeå University, Umeå, Sweden.ORCID 0000-0003-2429-7542
Kelly M RoschWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.ORCID 0000-0002-6416-1730
Asraa AhmedWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.
Garrett Sean WangWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.
Michael S van NieuwenhzeDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Sweden.
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, United States.ORCID 0000-0003-3283-9161
Cornell University · USUmeå University · SEIndiana University Bloomington · US

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 peptidoglycan cell wall is a predominant structure of bacteria, determining cell shape and supporting survival in diverse conditions. Peptidoglycan is dynamic and requires regulated synthesis of new material, remodeling, and turnover - or autolysis - of old material. Despite exploitation of peptidoglycan synthesis as an antibiotic target, we lack a fundamental understanding of how peptidoglycan synthesis and autolysis intersect to maintain the cell wall. Here, we uncover a critical physiological role for a widely misunderstood class of autolytic enzymes, lytic transglycosylases (LTGs). We demonstrate that LTG activity is essential to survival by contributing to periplasmic processes upstream and independent of peptidoglycan recycling. Defects accumulate in

Indexed as

Bacterial ProteinsCell WallEndopeptidasesPeptidoglycanPeriplasmVibrio choleraeBacterial ProteinsEndopeptidasesPeptidoglycanpeptidoglycan endopeptidaseinfectious diseaselytic transglycosylasemicrobiologypeptidoglycanperiplasmVibrio cholerae

Identifiers

PMID35073258
PMCPMC8820737
OpenAlexW4220823647

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.