Evidence map›Paper›PMID 34361086›Full record

ArticleInternational journal of molecular sciences2021

Mechanism of Ganglioside Receptor Recognition by Botulinum Neurotoxin Serotype E.

Geoffrey Masuyer, Jonathan R Davies, Pål Stenmark

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 25% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Advances in Clostridial and Related Neurotoxins.International journal of molecular sciences · 2022
    Article
  5. Article
  6. Article
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 1 institution in 2 countries.

Geoffrey MasuyerDepartment of Biochemistry and Biophysics, Stockholm University, 10691 Stockholm, Sweden.ORCID 0000-0002-9527-2310
Jonathan R DaviesDepartment of Biochemistry and Biophysics, Stockholm University, 10691 Stockholm, Sweden.ORCID 0000-0002-4986-8594
Pål StenmarkDepartment of Biochemistry and Biophysics, Stockholm University, 10691 Stockholm, Sweden.ORCID 0000-0003-4777-3417
Stockholm University · SE

Funding

Cancerfonden 20 1287 PjFVetenskapsrådet 2018-03406
6 · The paper itself

Abstract

The botulinum neurotoxins are potent molecules that are not only responsible for the lethal paralytic disease botulism, but have also been harnessed for therapeutic uses in the treatment of an increasing number of chronic neurological and neuromuscular disorders, in addition to cosmetic applications. The toxins act at the cholinergic nerve terminals thanks to an efficient and specific mechanism of cell recognition which is based on a dual receptor system that involves gangliosides and protein receptors. Binding to surface-anchored gangliosides is the first essential step in this process. Here, we determined the X-ray crystal structure of the binding domain of BoNT/E, a toxin of clinical interest, in complex with its GD1a oligosaccharide receptor. Beyond confirmation of the conserved ganglioside binding site, we identified key interacting residues that are unique to BoNT/E and a significant rearrangement of loop 1228-1237 upon carbohydrate binding. These observations were also supported by thermodynamic measurements of the binding reaction and assessment of ganglioside selectivity by immobilised-receptor binding assays. These results provide a structural basis to understand the specificity of BoNT/E for complex gangliosides.

Indexed as

Amino Acid SequenceBinding SitesBotulinum ToxinsCrystallography, X-RayGangliosidesHumansProtein BindingProtein ConformationReceptors, Cell SurfaceSequence Homology, Amino AcidBotulinum Toxinsbotulinum toxin type Eganglioside receptorGangliosidesReceptors, Cell SurfaceBoNT/Ebotulinum neurotoxinClostridium botulinumgangliosidesglycan bindingreceptor binding

Identifiers

PMID34361086
PMCPMC8346984
OpenAlexW3188964811

What OpenQuestion holds

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LicenceCC BY
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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.