Interaction of Botulinum Toxin with the Epithelial BarrierReport as inadecuate

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Journal of Biomedicine and BiotechnologyVolume 2010 2010, Article ID 974943, 9 pages

Review ArticleLaboratory for Infection Cell Biology, International Research Center for Infectious Diseases, Research Institute for Microbial Diseases, Osaka University, Yamada-oka 3-1, Suita, Osaka 565-0871, Japan

Received 10 August 2009; Accepted 24 December 2009

Academic Editor: Karl Chai

Copyright © 2010 Yukako Fujinaga. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Botulinum neurotoxin BoNT is a protein toxin ~150 kDa, which possesses a metalloprotease activity. Food-borne botulism is manifested when BoNT is absorbed from the digestive tract to the blood stream and enters the peripheral nerves, where the toxin cleaves core proteins of the neuroexocytosis apparatus and elicits the inhibition of neurotransmitter release. The initial obstacle to orally ingested BoNT entering the body is the epithelial barrier of the digestive tract. Recent cell biology and molecular biology studies are beginning to elucidate the mechanism by which this large protein toxin crosses the epithelial barrier. In this review, we provide an overview of the structural features of botulinum toxins BoNT and BoNT complex and the interaction of these toxins with the epithelial barrier.

Author: Yukako Fujinaga



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