Evidence map›Paper›PMID 39849213›Full record

ArticleJournal of neural transmission (Vienna, Austria : 1996)2025

Probing the properties of PTEN specific botulinum toxin type E mutants.

Giorgia Schiavone, Sandy Richter, Tina Henke, Ineke Koch, Linda Thies, Fiete Klöpper, Aram Megighian, Marco Pirazzini, Thomas Binz

Abstract read
In one paragraph

Article in Journal of neural transmission (Vienna, Austria : 1996), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

9 authors.

Giorgia SchiavoneDepartment of Biomedical Sciences, University of Padova, Padova, 35131, Italy.
Sandy RichterDepartment of Biomedical Sciences, University of Padova, Padova, 35131, Italy.
Tina HenkeInstitut für Zellbiochemie, OE 4310, Medizinische Hochschule Hannover, 30623, Hannover, Germany.
Ineke KochInstitut für Zellbiochemie, OE 4310, Medizinische Hochschule Hannover, 30623, Hannover, Germany.
Linda ThiesInstitut für Zellbiochemie, OE 4310, Medizinische Hochschule Hannover, 30623, Hannover, Germany.
Fiete KlöpperInstitut für Zellbiochemie, OE 4310, Medizinische Hochschule Hannover, 30623, Hannover, Germany.
Aram MegighianDepartment of Biomedical Sciences, University of Padova, Padova, 35131, Italy.
Marco PirazziniDepartment of Biomedical Sciences, University of Padova, Padova, 35131, Italy. marco.pirazzini@unipd.it.ORCID 0000-0003-4127-254X
Thomas BinzInstitut für Zellbiochemie, OE 4310, Medizinische Hochschule Hannover, 30623, Hannover, Germany. binz.thomas@mh-hannover.de.ORCID 0000-0001-9133-3617

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Botulinum neurotoxins (BoNT) are established biopharmaceuticals for neuromuscular and secretory conditions based on their ability to block neurotransmitter release from neurons by proteolyzing specific soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins. Recently, a mutant catalytic domain of serotype E (LC/E) exhibiting 16 mutations was reported to cleave the phosphatase and tensin homolog (PTEN). This molecule represents an attractive new target in neurons as several reports support PTEN knockdown as a strategy to stimulate axonal regeneration after injury. Though this LC/E mutant was shown to cleave PTEN in primary neurons through lentivirus-based expression, its expression and functionality as mutated full-length BoNT/E have not been studied. Hence, we assembled the 16 mutations stepwise in a bacterial expression plasmid for LC/E and purified several multiple mutants of LC/E. Biochemical characterization showed that the 16-fold mutant did not exhibit a detectable activity toward SNAP-25 up to 10 µM final concentration while it displayed an EC

Indexed as

Botulinum ToxinsPTEN PhosphohydrolaseAnimalsHumansMutationNeuronsRatsSynaptosomal-Associated Protein 25Botulinum Toxinsbotulinum toxin type EPTEN PhosphohydrolaseSynaptosomal-Associated Protein 25Botulinum neurotoxinNeurotoxin engineeringPTENSNAP-25Substrate specificityZinc protease

Identifiers

PMID39849213
PMCPMC12669263

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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.