Site-directed mutations in the third domain of Bacillus thuringiensis delta-endotoxin CryIAa affect its ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles

Article Abstract:

Mutations in the third-domain of the Bacillus thuringiensis CryIAa delta-endotoxin protein changes its potency of enhancing the permeability of Bombyx mori midgut brush border membrane vesicles (BBMV). The first, second, and last arginine residues of the conserved third-domain sequence, R-521 YRVRIR-527, are substituted with other amino acids to form the mutant toxins. Three of the mutant toxins have an activity comparable to that of the wild-type toxin. The third-domain probably controls the pore- and channel-forming processes in BBMV.

Physiological aspects, Endotoxins, Mutagenesis, Permeability

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Aminopeptidase N purified from gypsy moth brush border membrane vesicles is a specific receptor for Bacillus thuringiensis CryIAc toxin

Article Abstract:

Aminopeptidase N (APN), which contains N-acetylgalactosamine, is the major functional receptor for Cry1Ac in Lymantria dispar (gypsy moth) brush border membrane vesicles (BBMV). In vitro competition binding study shows that the binding of Cry1Ac to L. dispar BBMV is inhibited by APN. Addition of phosphatidylinositol-specific phospholipase C reduces inhibition of short circuit current for Cry1Ac substantially, but not for Cry1Aa. The binding of Bacillus thuringiensis Cry toxins to APN purified from L. dispar BBMV has been analyzed.

Toxins, Aminopeptidases, Gypsy moth, Gypsy moths

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