ArticleJournal of neural transmission (Vienna, Austria : 1996)2025
Probing the properties of PTEN specific botulinum toxin type E mutants.
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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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
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