Evidence map›Paper›PMID 30037998›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Liquid crystalline bacterial outer membranes are critical for antibiotic susceptibility.

Nicolò Paracini, Luke A Clifton, Maximilian W A Skoda, Jeremy H Lakey

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

45 citing papers in PubMed, 98 citations in OpenAlex.

  1. The mycomembrane proteins PorH and ProtX are inserted at polar growth zones and linked to the cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Thermal Shifts Dominate Single-Gene Responses to Transcription-Targeting Antibiotics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Article
  4. Twin-compartment solid-liquid cells for neutron reflectometry.Journal of applied crystallography · 2026
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  10. Immobile lipopolysaccharides and outer membrane proteins differentially segregate in growingProceedings of the National Academy of Sciences of the United States of America · 2025
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  12. Elucidating Antibiotic Permeation through theJournal of chemical information and modeling · 2024
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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

4 authors at 2 institutions in 1 country.

Nicolò ParaciniInstitute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom.
Luke A CliftonISIS Pulsed Neutron and Muon Source, Science and Technology Facilities Council (STFC), Rutherford Appleton Laboratory, Didcot, Oxfordshire OX11 OQX, United Kingdom.
Maximilian W A SkodaISIS Pulsed Neutron and Muon Source, Science and Technology Facilities Council (STFC), Rutherford Appleton Laboratory, Didcot, Oxfordshire OX11 OQX, United Kingdom.
Jeremy H LakeyInstitute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom; jeremy.lakey@ncl.ac.uk.ORCID 0000-0003-4646-9085
Newcastle University · GBRutherford Appleton Laboratory · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The outer membrane (OM) of Gram-negative bacteria is a robust, impermeable, asymmetric bilayer of outer lipopolysaccharides (LPSs) and inner phospholipids containing selective pore proteins which confer on it the properties of a molecular sieve. This structure severely limits the variety of antibiotic molecules effective against Gram-negative pathogens and, as antibiotic resistance has increased, so has the need to solve the OM permeability problem. Polymyxin B (PmB) represents those rare antibiotics which act directly on the OM and which offer a distinct starting point for new antibiotic development. Here we investigate PmB's interactions with in vitro OM models and show how the physical state of the lipid matrix of the OM is a critical factor in regulating the interaction with the antimicrobial peptide. Using neutron reflectometry and infrared spectroscopy, we reveal the structural and chemical changes induced by PmB on OM models of increasing complexity. In particular, only a tightly packed model reproduced the temperature-controlled disruption of the asymmetric lipid bilayer by PmB observed in vivo. By measuring the order of outer-leaflet LPS and inner-leaflet phospholipids, we show that PmB insertion is dependent on the phase transition of LPS from the gel to the liquid crystalline state. The demonstration of a lipid phase transition in the physiological temperature range also supports the hypothesis that bacteria grown at different temperatures adapt their LPS structures to maintain a homeoviscous OM.

Indexed as

Drug Resistance, BacterialAnti-Bacterial AgentsCell MembraneCell Membrane PermeabilityGram-Negative BacteriaLipid BilayersLipopolysaccharidesLiquid CrystalsModels, ChemicalPhase TransitionPhospholipidsPolymyxin BSpectrum AnalysisTemperatureAnti-Bacterial AgentsLipid BilayersLipopolysaccharidesPhospholipidsPolymyxin Blipopolysaccharideneutron reflectometryouter membranephase transitionpolymyxin

Identifiers

PMID30037998
PMCPMC6094139
OpenAlexW2883390882

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.