Evidence map›Paper›PMID 36830704›Full record

ArticleBiomolecules2023

Enzymatic Glyco-Modification of Synthetic Membrane Systems.

Dylan Jabeguero, Lina Siukstaite, Chunyue Wang, Anna Mitrovic, Serge Pérez, Olga Makshakova, Ralf P Richter, Winfried Römer, Christelle Breton

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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 4 institutions in 4 countries.

Dylan JabegueroCentre de Recherches sur les Macromolécules Végétales (CERMAV), CNRS, University Grenoble Alpes, 38041 Grenoble, France.ORCID 0000-0002-0198-1715
Lina SiukstaiteFaculty of Biology, Signalling Research Centres BIOSS and CIBSS, Freiburg Institute of Advanced Studies (FRIAS), Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.ORCID 0000-0002-0899-1916
Chunyue WangSchool of Biomedical Sciences, Faculty of Biological Sciences, School of Physics and Astronomy, Faculty of Engineering and Physical Sciences, Astbury Centre for Structural Molecular Biology, Bragg Centre for Materials Research, University of Leeds, Leeds LS2 9JT, UK.
Anna MitrovicFaculty of Biology, Signalling Research Centres BIOSS and CIBSS, Freiburg Institute of Advanced Studies (FRIAS), Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.ORCID 0000-0003-3261-8473
Serge PérezCentre de Recherches sur les Macromolécules Végétales (CERMAV), CNRS, University Grenoble Alpes, 38041 Grenoble, France.ORCID 0000-0003-3464-5352
Olga MakshakovaFRC Kazan Scientific Center of RAS, Kazan Institute of Biochemistry and Biophysics, 420111 Kazan, Russia.
Ralf P RichterSchool of Biomedical Sciences, Faculty of Biological Sciences, School of Physics and Astronomy, Faculty of Engineering and Physical Sciences, Astbury Centre for Structural Molecular Biology, Bragg Centre for Materials Research, University of Leeds, Leeds LS2 9JT, UK.ORCID 0000-0003-3071-2837
Winfried RömerFaculty of Biology, Signalling Research Centres BIOSS and CIBSS, Freiburg Institute of Advanced Studies (FRIAS), Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.ORCID 0000-0002-2847-246X
Christelle BretonCentre de Recherches sur les Macromolécules Végétales (CERMAV), CNRS, University Grenoble Alpes, 38041 Grenoble, France.ORCID 0000-0003-3697-0677
Centre National de la Recherche Scientifique · FRUniversity of Freiburg · DEUniversity of Leeds · GBRussian Academy of Sciences · RU

Funding

Deutsche Forschungsgemeinschaft EXC 2189European Cooperation in Science and Technology CA18103European Union 814029University Grenoble Alpes ANR-15-IDEX-02
6 · The paper itself

Abstract

The present report assesses the capability of a soluble glycosyltransferase to modify glycolipids organized in two synthetic membrane systems that are attractive models to mimic cell membranes: giant unilamellar vesicles (GUVs) and supported lipid bilayers (SLBs). The objective was to synthesize the Gb3 antigen (Galα1,4Galβ1,4Glcβ-Cer), a cancer biomarker, at the surface of these membrane models. A soluble form of LgtC that adds a galactose residue from UDP-Gal to lactose-containing acceptors was selected. Although less efficient than with lactose, the ability of LgtC to utilize lactosyl-ceramide as an acceptor was demonstrated on GUVs and SLBs. The reaction was monitored using the B-subunit of Shiga toxin as Gb3-binding lectin. Quartz crystal microbalance with dissipation analysis showed that transient binding of LgtC at the membrane surface was sufficient for a productive conversion of LacCer to Gb3. Molecular dynamics simulations provided structural elements to help rationalize experimental data.

Indexed as

GlycolipidsLactoseCell MembraneLipid BilayersUnilamellar LiposomesGlycolipidsLactoseLipid BilayersUnilamellar Liposomesgiant unilamellar vesiclesglobotriaosylceramideLgtCmolecular dynamicssupported lipid bilayer

Identifiers

PMID36830704
PMCPMC9952996
OpenAlexW4319971634

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.