RESUMO
The insecticidal Cry toxins from Bacillus thuringiensis bacteria are pore-forming toxins that lyse midgut epithelial cells in insects. We have previously proposed that they form pre-pore oligomeric intermediates before membrane insertion. For formation of these oligomers coiled-coil structures are important, and helix alpha-3 from Cry toxins could form coiled-coils. Our data shows that different mutations in helix alpha-3 are affected in pore formation and toxicity. Mutants affected in toxicity bind Bt-R(1) receptor with a similar K(D) as the wild type toxin but do not form oligomers nor induce pore formation in planar lipid bilayers, indicating that the pre-pore oligomer is an obligate intermediate in the intoxication of Cry1Ab toxin and that interaction of monomeric Cry1Ab with Bt-R(1) is not enough to kill susceptible larvae.
