Effects of purification on the bioavailability of botulinum neurotoxin type A

Luisa W. Cheng, Bruce Onisko, Eric A. Johnson, J. Rachel Reader, Stephen M Griffey, Ann E. Larson, William H. Tepp, Larry H. Stanker, David L. Brandon, J. Mark Carter

Research output: Contribution to journalArticlepeer-review

43 Scopus citations


Botulinum neurotoxins (BoNTs) are among the most potent biological toxins for humans. They are primarily produced by the gram-positive, anaerobic spore-forming bacterium, Clostridium botulinum. In bacterial cultures, secreted BoNTs are associated with non-toxic accessory proteins forming large complexes. Neurotoxin-associated proteins have been shown to play an important role in the oral toxicity of BoNTs by protecting them from degradation and digestion by gastric acid and enzymes. Most toxicity studies using BoNTs have been performed using highly purified toxin. In this study, the toxicities of purified and crude BoNT/A toxin preparations were compared. Protein components secreted into culture supernatants along with BoNT/A were identified by mass spectrometry and the contribution of extra proteins found in the soluble crude toxin extracts to the toxicity of BoNTs was determined in mouse models of oral and parenteral botulinum intoxication. Analysis of crude toxin composition permitted assessment of the impact of accessory proteins on the oral bioavailability of BoNT/A toxin in food matrices.

Original languageEnglish (US)
Pages (from-to)123-129
Number of pages7
Issue number2-3
StatePublished - Jul 30 2008


  • Bioavailability
  • Botulinum neurotoxin type A (BoNT/A)
  • Clostridium botulinum
  • Food matrices

ASJC Scopus subject areas

  • Toxicology


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