Bacillus thuringiensis cry toxins bound specifically to various proteins via domain 3, which had a galactose-binding domain-like fold

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  • KITAMI Madoka
    Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology
  • KADOTANI Tomoyuki
    Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology
  • NAKANISHI Kazuko
    Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology
  • ATSUMI Shogo
    Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology
  • HIGURASHI Satoshi
    Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology
  • ISHIZAKA Takahisa
    Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology
  • WATANABE Ayako
    Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology
  • SATO Ryoichi
    Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology

書誌事項

タイトル別名
  • <I>Bacillus thuringiensis</I> Cry Toxins Bound Specifically to Various Proteins <I>via</I> Domain III, Which Had a Galactose-Binding Domain-Like Fold
  • Bacillus thuringiensis Cry toxins bound specifically to various proteins via domain III, which had a galactose-binding domain-like fold

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抄録

Cry toxins have been reported to bind not only to receptors on insect cells but also to several unrelated proteins. In this study, we investigated the binding properties of Bacillus thuringiensis Cry toxins, focusing on domain III, a Cry toxin region with a structure that of the galactose-binding domain-like. Cry1Aa, Cry1Ac, and Cry8Ca specifically bound to several proteins unrelated to insect midgut cells. Cry1Aa binding to Cry toxin-binding proteins was inhibited by a monoclonal antibody, 2C2, indicating that Cry1Aa binds to these Cry toxin-binding proteins through domain III. Cry1Aa binding to Bombyx mori aminopeptidase N and other Cry toxin-binding proteins was inhibited by carbonic anhydrase, a Cry toxin-binding protein. The binding regions of carbonic anhydrase and Bombyx mori aminopeptidase N were narrowed to regions of less than 20 amino acids that did not have any similarity, suggesting that Cry toxin domain III has a binding pocket for multiple proteins.

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