Blocking binding of Bacillus thuringiensis Cry1Aa to Bombyx mori cadherin receptor results in only a minor reduction of toxicity

<p>Abstract</p> <p>Background</p> <p><it>Bacillus thuringiensis </it>Cry1Aa insecticidal protein is the most active known <it>B. thuringiensis </it>toxin against the forest insect pest <it>Lymantria dispar </it>(gypsy moth), unfortunately it is also highly toxic against the non-target insect <it>Bombyx mori </it>(silk worm).</p> <p>Results</p> <p>Surface exposed hydrophobic residues over domains II and III were targeted for site-directed mutagenesis. Substitution of a phenylalanine residue (F328) by alanine reduced binding to the <it>Bombyx mori </it>cadherin by 23-fold, reduced biological activity against <it>B. mori </it>by 4-fold, while retaining activity against <it>Lymantria dispar</it>.</p> <p>Conclusion</p> <p>The results identify a novel receptor-binding epitope and demonstrate that virtual elimination of binding to cadherin BR-175 does not completely remove toxicity in the case of <it>B. mori</it>.</p