Evidence map›Paper›PMID 37070977›Full record

ArticleJournal of bacteriology2023

Impact of the cAMP-cAMP Receptor Protein Regulatory Complex on Lipopolysaccharide Modifications and Polymyxin B Resistance in Escherichia coli.

Alexandria B Purcell, Brent W Simpson, M Stephen Trent

Open access · greenAbstract read
In one paragraph

Article 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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 32% 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

12 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Sugar Import SuppressesbioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. ISmBio · 2024
    Article
  9. Article
  10. Article
  11. The cAMP Receptor Protein (CRP) ofAnimals : an open access journal from MDPI · 2024
    Article
  12. 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 1 institution in 1 country.

Alexandria B PurcellDepartment of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia, USA.
Brent W SimpsonDepartment of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia, USA.
M Stephen TrentDepartment of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia, USA.ORCID 0000-0001-6134-1800
University of Georgia · US

Funding

The Cell Envelope of the Multi-Drug Resistant Pathogen Acinetobacter baumanniiR01AI150098 · NIAID · UNIVERSITY OF GEORGIA · PI Michael Stephen Trent · 2020 to 2026
$3.9M
Synthesis and transport of outer membrane components across the Gram-negative cell envelopeR01AI176776 · NIAID · UNIVERSITY OF GEORGIA · PI Michael Stephen Trent · 2023 to 2026
$2.5M
Molecular mechanisms required for the maintenance of the gram-negative outer membraneR01AI138576 · NIAID · UNIVERSITY OF GEORGIA · PI TRENT, MICHAEL STEPHEN · 2018 to 2022
$2.0M
Function and maintenance of molecules at the surface of Acinetobacter baumanniiF32GM137554 · NIGMS · UNIVERSITY OF GEORGIA · PI SIMPSON, BRENT · 2020 to 2021
$131k
NIAID NIH HHS R01 AI138576NIAID NIH HHS R01 AI150098NIAID NIH HHS R01 AI176776NIGMS NIH HHS F32 GM137554
6 · The paper itself

Abstract

Gram-negative bacteria have a unique cell surface that can be modified to maintain bacterial fitness in diverse environments. A well-defined example is the modification of the lipid A component of lipopolysaccharide (LPS), which promotes resistance to polymyxin antibiotics and antimicrobial peptides. In many organisms, such modifications include the addition of the amine-containing constituents 4-amino-4-deoxy-l-arabinose (l-Ara4N) and phosphoethanolamine (pEtN). Addition of pEtN is catalyzed by EptA, which uses phosphatidylethanolamine (PE) as its substrate donor, resulting in production of diacylglycerol (DAG). DAG is then quickly recycled into glycerophospholipid (GPL) synthesis by the DAG kinase A (DgkA) to produce phosphatidic acid, the major GPL precursor. Previously, we hypothesized that loss of DgkA recycling would be detrimental to the cell when LPS is heavily modified. Instead, we found that DAG accumulation inhibits EptA activity, preventing further degradation of PE, the predominant GPL of the cell. However, DAG inhibition of pEtN addition results in complete loss of polymyxin resistance. Here, we selected for suppressors to find a mechanism of resistance independent of DAG recycling or pEtN modification. Disrupting the gene encoding the adenylate cyclase,

Indexed as

LipopolysaccharidesPolymyxin BAnti-Bacterial AgentsCyclic AMP Receptor ProteinDrug Resistance, BacterialEscherichia coliLipid APolymyxinsAnti-Bacterial AgentsCyclic AMP Receptor ProteinLipid ALipopolysaccharidesPolymyxin BPolymyxinsaminoarabinosecAMP receptor proteincyclic AMPlipid Alipopolysaccharideouter membranephosphoethanolamine

Identifiers

PMID37070977
PMCPMC10210979
OpenAlexW4366234694

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.