Evidence map›Paper›PMID 20384697›Full record

ArticleMolecular microbiology2010

Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides.

Carmen M Herrera, Jessica V Hankins, M Stephen Trent

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

99 citing papers in PubMed, 162 citations in OpenAlex.

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  16. Lipopolysaccharides: Regulated Biosynthesis and Structural Diversity.International journal of molecular sciences · 2023
    Article
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39 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Carmen M HerreraSection of Molecular Genetics and Microbiology, The University of Texas at Austin, Austin, TX 78712, USA.
Jessica V Hankins
M Stephen Trent
Laboratory of Molecular Genetics · PLAugusta University · US

Funding

MODIFICATION OF HELICOBACTER PYLORI LIPOPOLYSACCHARIDESR01AI064184 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI TRENT, MICHAEL STEPHEN · 2006 to 2015
$3.4M
The Outer Surface of Vibrio CholeraeR01AI076322 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI TRENT, MICHAEL STEPHEN · 2008 to 2017
$3.2M
The Outer Surface of Vibrio choleraeR56AI076322 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI TRENT, MICHAEL STEPHEN · 2013 to 2013
$384k
NIAID NIH HHS AI064184NIAID NIH HHS AI76322NIAID NIH HHS R01 AI064184NIAID NIH HHS R01 AI076322NIAID NIH HHS R56 AI076322
6 · The paper itself

Abstract

During its transport to the bacterial surface, the phosphate groups of the lipid A anchor of Escherichia coli and Salmonella lipopolysaccharide are modified by membrane enzymes including ArnT, EptA and LpxT. ArnT and EptA catalyse the periplasmic addition of the positively charged substituents 4-amino-4-deoxy-L-arabinose and phosphoethanolamine respectively. These modifications are controlled by the PmrA transcriptional regulator and confer resistance to cationic antimicrobial peptides, including polymyxin. LpxT, however, catalyses the phosphorylation of lipid A at the 1-position forming 1-diphosphate lipid A increasing the negative charge of the bacterial surface. Here, we report that PmrA is involved in the regulation of LpxT. Interestingly, this regulation does not occur at the level of transcription, but rather following the assembly of LpxT into the inner membrane. PmrA-dependent inhibition of LpxT is required for phosphoethanolamine decoration of lipid A, which is shown here to be critical for E. coli to resist the bactericidal activity of polymyxin. Furthermore, although Salmonella lipid A is more prevalently modified with l-4-aminoarabinose, we demonstrate that loss of Salmonella lpxT greatly increases EptA modification. The current work is an example of the complexities associated with the structural remodelling of Gram-negative lipopolysaccharides promoting bacterial survival.

Indexed as

Gene Expression Regulation, BacterialAnti-Bacterial AgentsBacterial ProteinsDrug Resistance, BacterialEscherichia coliEscherichia coli ProteinsGene DeletionLipid AMolecular StructurePhosphorylationPhosphotransferasesPhosphotransferases (Phosphate Group Acceptor)PolymyxinsSalmonella typhimuriumAnti-Bacterial AgentsBacterial ProteinsEscherichia coli ProteinsLipid ALpxT protein, E coliPhosphotransferasesPhosphotransferases (Phosphate Group Acceptor)pmrA protein, BacteriaPolymyxins

Identifiers

PMID20384697
PMCPMC2904496
OpenAlexW2158665665

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.