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Updated: Sep 27, 2026

A High-throughput-compatible FRET-based Platform for Identification and Characterization of Botulinum Neurotoxin Light Chain Modulators
Published on: December 27, 2013
Characterization of Clostridium butyricum neurotoxin associated with food-borne botulism
Kentaro Tsukamoto1, Masafumi Mukamoto, Tomoko Kohda
1Department of Veterinary Science, Graduate School of Agriculture and Biological Sciences, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan.
Abstract:
The neurotoxin of Clostridium butyricum strain LCL155 (BuNT/LCL155) associated with type E food-borne botulism showed antigenic and biological properties different from those of C. botulinum type E (BoNT/E) andC. butyricum strain BL5262 (BuNT/BL5262). The specific toxicity of BuNT/LCL155 was found to be about 10% those of BoNT/E and BuNT/BL5262. Immunological analysis with monoclonal antibodies against BoNT/E showed that the heavy chain of BuNT/LCL155 differs partially from those of BoNT/E and BuNT/BL5262. Binding experiments with rat brain synaptic membrane revealed that BuNT/LCL155 possesses a binding activity lower than either BoNT/E or BuNT/BL5262. There was no difference in the catalytic activity of the three neurotoxins, which had been determined with a recombinant of the intracellular target protein SNAP-25. These data suggest that the BuNT/LCL155 shares the receptor-recognition site structurally different from BoNT/E and BuNT/BL5262, perhaps causing a decreased specific toxicity.
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