Evidence map›Paper›PMID 24341982›Full record

ArticleJournal of the American Chemical Society2014

Lipoprotein activators stimulate Escherichia coli penicillin-binding proteins by different mechanisms.

Tania J Lupoli, Matthew D Lebar, Monica Markovski, Thomas Bernhardt, Daniel Kahne, Suzanne Walker

Abstract 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 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Tazobactam selects for multidrug resistance.npj antimicrobials and resistance · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. The LpoA activator is required to stimulate the peptidoglycan polymerase activity of its cognate cell wall synthase PBP1a.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Review
  17. Article
  18. Article
  19. Regulation of peptidoglycan synthesis and remodelling.Nature reviews. Microbiology · 2020
    Review
  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

6 authors.

Tania J LupoliDepartment of Microbiology and Immunobiology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Matthew D Lebar
Monica Markovski
Thomas Bernhardt
Daniel Kahne
Suzanne Walker

Funding

Treatments for Nipah Virus InfectionU54AI057159 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI KASPER, DENNIS L. · 2003 to 2013
$113.7M
Studies Toward Hybrid Glycopeptide AntibioticsR01GM066174 · NIGMS · PRINCETON UNIVERSITY · PI KAHNE, DANIEL · 2002 to 2018
$8.9M
Peptidoglycan Biogenesis in Escherichia ColiR01AI083365 · NIAID · HARVARD MEDICAL SCHOOL · PI Thomas G Bernhardt · 2010 to 2026
$8.3M
Mechanism and Inhibition of Enzymes that Assemble Bacterial Cell WallR01GM076710 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALKER, SUZANNE · 2007 to 2019
$5.9M
Mechanistic studies on peptidoglycan tailoring that mediate biofilm stabilityF32GM103056 · NIGMS · HARVARD UNIVERSITY · PI LEBAR, MATTHEW DENNIS · 2012 to 2013
$101k
NIAID NIH HHS AI057159NIAID NIH HHS AI083365NIAID NIH HHS R01 AI083365NIAID NIH HHS U54 AI057159NIGMS NIH HHS F32 GM103056NIGMS NIH HHS GM066174NIGMS NIH HHS GM103056NIGMS NIH HHS GM76710NIGMS NIH HHS R01 GM066174NIGMS NIH HHS R01 GM076710
6 · The paper itself

Abstract

In Escherichia coli , the bifunctional penicillin-binding proteins (PBPs), PBP1A and PBP1B, play critical roles in the final stage of peptidoglycan (PG) biosynthesis. These synthetic enzymes each possess a PG glycosyltransferase (PGT) domain and a transpeptidase (TP) domain. Recent genetic experiments have shown that PBP1A and PBP1B each require an outer membrane lipoprotein, LpoA and LpoB, respectively, to function properly in vivo. Here, we use complementary assays to show that LpoA and LpoB each increase the PGT and TP activities of their cognate PBPs, albeit by different mechanisms. LpoA directly increases the rate of the PBP1A TP reaction, which also results in enhanced PGT activity; in contrast, LpoB directly affects PGT domain activity, resulting in enhanced TP activity. These studies demonstrate bidirectional coupling of PGT and TP domain function. Additionally, the transpeptidation assay described here can be applied to study other activators or inhibitors of the TP domain of PBPs, which are validated drug targets.

Indexed as

Bacterial Outer Membrane ProteinsCoenzymesEscherichia coliLipoproteinsModels, BiologicalMolecular StructurePenicillin-Binding ProteinsBacterial Outer Membrane ProteinsCoenzymesLipoproteinsPenicillin-Binding Proteins

Identifiers

PMID24341982
PMCPMC3961711

What OpenQuestion holds

Textmetadata
LicenceTDM
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.