Evidence map›Paper›PMID 25036369›Full record

ArticleJournal of the American Chemical Society2014

Reconstitution of peptidoglycan cross-linking leads to improved fluorescent probes of cell wall synthesis.

Matthew D Lebar, Janine M May, Alexander J Meeske, Sara A Leiman, Tania J Lupoli, Hirokazu Tsukamoto, Richard Losick, David Z Rudner, Suzanne Walker, Daniel Kahne

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
8.9field-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

55 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Review
  3. Molecular biology of the cell · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Inhibition ofMicrobiology (Reading, England) · 2022
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Assembly of Peptidoglycan Fragments-A Synthetic Challenge.Pharmaceuticals (Basel, Switzerland) · 2020
    Review
  18. Article
  19. Article
  20. Chemical tools to characterize peptidoglycan synthases.Current opinion in chemical biology · 2019
    Review
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

10 authors at 1 institution in 1 country.

Matthew D LebarDepartment of Chemistry and Chemical Biology, Harvard University , Cambridge, Massachusetts 02138, United States.
Janine M May
Alexander J Meeske
Sara A Leiman
Tania J Lupoli
Hirokazu Tsukamoto
Richard Losick
David Z Rudner
Suzanne Walker
Daniel Kahne
Harvard University · US

Funding

Targeting bacterial cell wall biogenesis for the development of novel antimicrobU19AI109764 · NIAID · HARVARD MEDICAL SCHOOL · PI KASPER, DENNIS L. · 2014 to 2018
$25.2M
Training in Molecular, Cellular, and Chemical BiologyT32GM007598 · NIGMS · HARVARD UNIVERSITY · PI DULAC, CATHERINE · 1985 to 2019
$16.2M
Role of RNA Polymerase in Bacterial DifferentionR01GM018568 · NIGMS · HARVARD UNIVERSITY · PI LOSICK, RICHARD MARC · 1985 to 2018
$11.5M
Studies Toward Hybrid Glycopeptide AntibioticsR01GM066174 · NIGMS · PRINCETON UNIVERSITY · PI KAHNE, DANIEL · 2002 to 2018
$8.9M
Mechanism and Inhibition of Enzymes that Assemble Bacterial Cell WallR01GM076710 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALKER, SUZANNE · 2007 to 2019
$5.9M
Membrane Remodeling and Protein Trafficking in BacteriaR01GM073831 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI RUDNER, DAVID Z · 2005 to 2014
$3.4M
Mechanistic studies on peptidoglycan tailoring that mediate biofilm stabilityF32GM103056 · NIGMS · HARVARD UNIVERSITY · PI LEBAR, MATTHEW DENNIS · 2012 to 2013
$101k
NIAID NIH HHS U19 AI109764NIGMS NIH HHS F32 GM103056NIGMS NIH HHS R01 GM018568NIGMS NIH HHS R01 GM066174NIGMS NIH HHS R01 GM073831NIGMS NIH HHS R01 GM076710NIGMS NIH HHS R01 GM18568NIGMS NIH HHS T32 GM007598
6 · The paper itself

Abstract

The peptidoglycan precursor, Lipid II, produced in the model Gram-positive bacterium Bacillus subtilis differs from Lipid II found in Gram-negative bacteria such as Escherichia coli by a single amidation on the peptide side chain. How this difference affects the cross-linking activity of penicillin-binding proteins (PBPs) that assemble peptidoglycan in cells has not been investigated because B. subtilis Lipid II was not previously available. Here we report the synthesis of B. subtilis Lipid II and its use by purified B. subtilis PBP1 and E. coli PBP1A. While enzymes from both organisms assembled B. subtilis Lipid II into glycan strands, only the B. subtilis enzyme cross-linked the strands. Furthermore, B. subtilis PBP1 catalyzed the exchange of both D-amino acids and D-amino carboxamides into nascent peptidoglycan, but the E. coli enzyme only exchanged D-amino acids. We exploited these observations to design a fluorescent D-amino carboxamide probe to label B. subtilis PG in vivo and found that this probe labels the cell wall dramatically better than existing reagents.

Indexed as

Bacillus subtilisCell WallEscherichia coliFluorescent DyesPenicillin-Binding ProteinsPeptidoglycanPeptidyl TransferasesUridine Diphosphate N-Acetylmuramic AcidFluorescent Dyesmuramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenolPenicillin-Binding ProteinsPeptidoglycanPeptidyl TransferasesUridine Diphosphate N-Acetylmuramic Acid

Identifiers

PMID25036369
PMCPMC4132960
OpenAlexW2016296695

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.