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Background   Bacillus thuringiensis  Cry1Aa insecticidal protein is the most active known  B. thuringiensis  toxin against the forest insect pest  Lymantria dispar  (gypsy moth), unfortunately it is also highly toxic against the non-target insect  Bombyx mori  (silk worm).    Results  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  Bombyx mori  cadherin by 23-fold, reduced biological activity against  B. mori  by 4-fold, while retaining activity against  Lymantria dispar .    Conclusion  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  B. mori .

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