Evidence map›Paper›PMID 24896129›Full record

ArticleBiophysical journal2014

E. coli outer membrane and interactions with OmpLA.

Emilia L Wu, Patrick J Fleming, Min Sun Yeom, Göran Widmalm, Jeffery B Klauda, Karen G Fleming, Wonpil Im

Abstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing 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

81 citing papers in PubMed.

  1. Article
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  4. Review
  5. Article
  6. Article
  7. Article
  8. Microwave-Activated Bacterial Biorobot for Multimodal Cancer Therapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Sequence-Sensitivity in Functional Synthetic Polymer Properties.Angewandte Chemie (International ed. in English) · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. An elevated OmpA expression during the production of a recombinant protein in Escherichia coli.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Article

21 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

7 authors.

Emilia L WuDepartment of Molecular Biosciences and Center for Bioinformatics, The University of Kansas, Lawrence, Kansas.
Patrick J FlemingT. C. Jenkins Department of Biophysics, John Hopkins University, Baltimore, Maryland.
Min Sun YeomKorean Institute of Science and Technology Information, Daejeon, Korea.
Göran WidmalmDepartment of Organic Chemistry and Stockholm Center for Biomembrane Research, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden.
Jeffery B KlaudaDepartment of Chemical and Biomolecular Engineering, The University of Maryland, College Park, Maryland.
Karen G FlemingT. C. Jenkins Department of Biophysics, John Hopkins University, Baltimore, Maryland. Electronic address: Karen.Fleming@jhu.edu.
Wonpil ImDepartment of Molecular Biosciences and Center for Bioinformatics, The University of Kansas, Lawrence, Kansas. Electronic address: wonpil@ku.edu.

Funding

Membrane Protein StabilityR01GM079440 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FLEMING, KAREN G. · 2009 to 2022
$4.1M
NIGMS NIH HHS GM0790440NIGMS NIH HHS R01 GM079440
6 · The paper itself

Abstract

The outer membrane of Gram-negative bacteria is a unique asymmetric lipid bilayer composed of phospholipids (PLs) in the inner leaflet and lipopolysaccharides (LPSs) in the outer leaflet. Its function as a selective barrier is crucial for the survival of bacteria in many distinct environments, and it also renders Gram-negative bacteria more resistant to antibiotics than their Gram-positive counterparts. Here, we report the structural properties of a model of the Escherichia coli outer membrane and its interaction with outer membrane phospholipase A (OmpLA) utilizing molecular dynamics simulations. Our results reveal that given the lipid composition used here, the hydrophobic thickness of the outer membrane is ∼3 Å thinner than the corresponding PL bilayer, mainly because of the thinner LPS leaflet. Further thinning in the vicinity of OmpLA is observed due to hydrophobic matching. The particular shape of the OmpLA barrel induces various interactions between LPS and PL leaflets, resulting in asymmetric thinning around the protein. The interaction between OmpLA extracellular loops and LPS (headgroups and core oligosaccharides) stabilizes the loop conformation with reduced dynamics, which leads to secondary structure variation and loop displacement compared to that in a DLPC bilayer. In addition, we demonstrate that the LPS/PL ratios in asymmetric bilayers can be reliably estimated by the per-lipid surface area of each lipid type, and there is no statistical difference in the overall membrane structure for the outer membranes with one more or less LPS in the outer leaflet, although individual lipid properties vary slightly.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceBacterial Outer Membrane ProteinsCell MembraneEscherichia coliLipid BilayersMembrane LipidsMolecular Sequence DataPhospholipases A1Protein BindingProtein Structure, TertiaryBacterial Outer Membrane ProteinsLipid BilayersMembrane Lipidsouter membrane phospholipase APhospholipases A1

Identifiers

PMID24896129
PMCPMC4052237

What OpenQuestion holds

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Registered trials

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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.