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Updated: Apr 23, 2026

A High-throughput-compatible FRET-based Platform for Identification and Characterization of Botulinum Neurotoxin Light Chain Modulators
Published on: December 27, 2013
Redox regulation of botulinum neurotoxin toxicity: therapeutic implications
1Section of Neurobiology, University of California San Diego, La Jolla, CA 92093, USA.
Abstract:
Botulinum neurotoxin causes botulism, and the only effective antidote is the antitoxin. Botulinum neurotoxins are disulfide linked di-chain proteins encompassing a light chain Zn2+-protease that is translocated by a heavy chain channel from the synaptic vesicle lumen into the neuronal cytosol where it acts. Protease release from the channel is required for toxicity. The Thioredoxin Reductase-Thioredoxin system cleaves the interchain disulfide, and its inhibition prevents neurotoxicity, and may provide novel strategies for chemoprophylaxis and therapy.
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