Aggregation of Bacillus thuringiensis Cry1A toxins upon binding to target insect larval midgut vesicles

Article Abstract:

Bacillus thuringiensis produces crystalline inclusions comprised of a mixture of delta-endotoxins during sporulation. Following ingestion by insect larvae, these inclusion proteins are solubilized, and the protoxins are converted to toxins. Research findings showed a greater extent of oligomerization of the Cry1Ac toxin with vesicles from the Heliothis virescens midgut than with those from the Manduca sexta midgut, which correlated with observed differences in toxicity. Tight binding of virtually the entire toxin molecule to the membrane is an important step in toxicity.

Microbial aggregation, Endotoxins, Insects, Insect larvae

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Single-site mutations in the conserved alternating-arginine region affect ionic channels formed by CryLAa, a Bacillus thuringiensis toxin

Article Abstract:

A study was conducted on the function of the third domain of Bacillus thuringiensis insecticidal toxin CryIAa in membrane permeabilization under a receptor-free environment. Mutants were developed by replacing arginine with glutamine, lysine, histidine and glutamic acid. Results demonstrate the functional role of domain II and indicates that domain I interacts with the residues of the positive arginine face of block 4.

Ion exchange membranes, Ion channels, Arginine, Ion-permeable membranes

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