Crystal Structure of Hemagglutinin from Type B <i>Clostridium Botulinum</i>

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  • AMATSU Sho
    International Research Center for Infectious Diseases, Research Institute for Microbial Disease, Osaka University
  • SUGAWARA Yo
    International Research Center for Infectious Diseases, Research Institute for Microbial Disease, Osaka University
  • FUJINAGA Yukako
    International Research Center for Infectious Diseases, Research Institute for Microbial Disease, Osaka University
  • KITADOKORO Kengo
    Graduate School of Science and Technology, Department of Biomolecular Engineering, Kyoto Institute of Technology

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Other Title
  • ボツリヌス菌由来ヘマグルチニンの立体構造
  • ボツリヌスキン ユライ ヘマグルチニン ノ リッタイ コウゾウ

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Abstract

Botulinum neurotoxins (BoNTs), which are produced by Clostridium botulinum, are the most potent toxins, and cause the highly lethal food poisoning. BoNTs are produced as the assemblies with non-toxic components. Hemagglutinin (HA), one of the non-toxic components, has three biological activities: one is protecting BoNT from degradation in gastrointestinal tract, another is binding activity to carbohydrates and the other is disrupting of the epithelial barrier by direct binding to E-cadherin, which are critical for oral toxicity of BoNT. Here, we review the study on the crystal structure of type B whole HA. This structure reveals whole HA to be a huge triskelion-shaped molecule composed of 12 subcomponents, and biochemical data show that these functions of HA are employed at distinct sites.

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