Evidence map›Paper›PMID 36757204›Full record

ReviewJournal of bacteriology2023

Masters of Misdirection: Peptidoglycan Glycosidases in Bacterial Growth.

Anna Weaver, Atsushi Taguchi, Tobias Dörr

Open access · greenAbstract readReview
In one paragraph

Review in Journal of bacteriology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
12.3field-weighted citation impact, top 2% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. mBio · 2026
    Article
  3. Article
  4. bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Bacterial peptidoglycan as a living polymer.Current opinion in chemical biology · 2025
    Review
  12. Review
  13. Review
  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

3 authors at 3 institutions in 2 countries.

Anna WeaverDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, Massachusetts, USA.ORCID 0000-0002-0556-0336
Atsushi TaguchiSANKEN (The Institute of Scientific and Industrial Research), Osaka University, Ibaraki, Osaka, Japan.ORCID 0000-0003-4962-0393
Tobias DörrWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York, USA.ORCID 0000-0003-3283-9161
Cornell University · USHarvard University · USThe University of Osaka · JP

Funding

Release of Extracellular DNA during Biofilm Formation in Staphylococcus aureusR01AI139011 · NIAID · HARVARD UNIVERSITY · PI KAHNE, DANIEL, LOSICK, RICHARD MARC · 2018 to 2022
$3.2M
The mechanism of autolysin regulation in Vibrio choleraeR01GM130971 · NIGMS · CORNELL UNIVERSITY · PI DOERR, TOBIAS · 2019 to 2025
$2.0M
NIAID NIH HHS R01 AI139011NIGMS NIH HHS R01 GM130971
6 · The paper itself

Abstract

The dynamic composition of the peptidoglycan cell wall has been the subject of intense research for decades, yet how bacteria coordinate the synthesis of new peptidoglycan with the turnover and remodeling of existing peptidoglycan remains elusive. Diversity and redundancy within peptidoglycan synthases and peptidoglycan autolysins, enzymes that degrade peptidoglycan, have often made it challenging to assign physiological roles to individual enzymes and determine how those activities are regulated. For these reasons, peptidoglycan glycosidases, which cleave within the glycan strands of peptidoglycan, have proven veritable masters of misdirection over the years. Unlike many of the broadly conserved peptidoglycan synthetic complexes, diverse bacteria can employ unrelated glycosidases to achieve the same physiological outcome. Additionally, although the mechanisms of action for many individual enzymes have been characterized, apparent conserved homologs in other organisms can exhibit an entirely different biochemistry. This flexibility has been recently demonstrated in the context of three functions critical to vegetative growth: (i) release of newly synthesized peptidoglycan strands from their membrane anchors, (ii) processing of peptidoglycan turned over during cell wall expansion, and (iii) removal of peptidoglycan fragments that interfere with daughter cell separation during cell division. Finally, the regulation of glycosidase activity during these cell processes may be a cumulation of many factors, including protein-protein interactions, intrinsic substrate preferences, substrate availability, and subcellular localization. Understanding the true scope of peptidoglycan glycosidase activity will require the exploration of enzymes from diverse organisms with equally diverse growth and division strategies.

Indexed as

Glycoside HydrolasesPeptidoglycanBacteriaBacterial ProteinsCell DivisionCell WallBacterial ProteinsGlycoside HydrolasesPeptidoglycanglucosaminidaseglycosidaselytic transglycosylasemuramidasepeptidoglycanpeptidoglycan hydrolases

Identifiers

PMID36757204
PMCPMC10029718
OpenAlexW4319656520

What OpenQuestion holds

Textmetadata
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.