Evidence map›Paper›PMID 32766244›Full record

ArticleFrontiers in cell and developmental biology2020

The Beauty of Asymmetric Membranes: Reconstitution of the Outer Membrane of Gram-Negative Bacteria.

Laura Paulowski, Annemarie Donoghue, Christian Nehls, Sabrina Groth, Max Koistinen, Sven O Hagge, Arne Böhling, Mathias Winterhalter, Thomas Gutsmann

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cell and developmental biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

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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

9 authors at 2 institutions in 1 country.

Laura PaulowskiDivision of Biophysics, Priority Research Area Infection, Research Center Borstel Leibniz Lung Center, Borstel, Germany.
Annemarie DonoghueDivision of Biophysics, Priority Research Area Infection, Research Center Borstel Leibniz Lung Center, Borstel, Germany.
Christian NehlsDivision of Biophysics, Priority Research Area Infection, Research Center Borstel Leibniz Lung Center, Borstel, Germany.
Sabrina GrothDivision of Biophysics, Priority Research Area Infection, Research Center Borstel Leibniz Lung Center, Borstel, Germany.
Max KoistinenDivision of Biophysics, Priority Research Area Infection, Research Center Borstel Leibniz Lung Center, Borstel, Germany.
Sven O HaggeDivision of Biophysics, Priority Research Area Infection, Research Center Borstel Leibniz Lung Center, Borstel, Germany.
Arne BöhlingDivision of Biophysics, Priority Research Area Infection, Research Center Borstel Leibniz Lung Center, Borstel, Germany.
Mathias WinterhalterDepartment of Life Sciences & Chemistry, Jacobs University Bremen, Bremen, Germany.
Thomas GutsmannDivision of Biophysics, Priority Research Area Infection, Research Center Borstel Leibniz Lung Center, Borstel, Germany.
Research Center Borstel - Leibniz Lung Center · DEConstructor University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The architecture of the lipid matrix of the outer membrane of Gram-negative bacteria is extremely asymmetric: Whereas the inner leaflet is composed of a phospholipid mixture, the outer leaflet is built up by glycolipids. For most Gram-negative species, these glycolipids are lipopolysaccharides (LPS), for a few species, however, glycosphingolipids. We demonstrate experimental approaches for the reconstitution of these asymmetric membranes as (i) solid supported membranes prepared by the Langmuir-Blodgett technique, (ii) planar lipid bilayers prepared by the Montal-Mueller technique, and (iii) giant unilamellar vesicles (GUVs) prepared by the phase transfer method. The asymmetric GUVs (aGUVs) composed of LPS on one leaflet are shown for the first time. They are characterized with respect to their phase behavior, flip-flop of lipids and their usability to investigate the interaction with membrane active peptides or proteins. For the antimicrobial peptide LL-32 and for the bacterial porin OmpF the specificity of the interaction with asymmetric membranes is shown. The three reconstitution systems are compared with respect to their usability to investigate domain formation and interactions with peptides and proteins.

Indexed as

asymmetrycouplinglipid flip-flopmembranesphase transfer

Identifiers

PMID32766244
PMCPMC7381204
OpenAlexW3043079597

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.