Abstract

Although the new dual model of the Bacillus thuringiensis insecticidal mechamism indicated that both Cry1A protoxin and activated toxin have the potency to kill insects, the difference in the toxic pathways elicited by the protoxin and activated toxin was less understood at the molecular level. Through utilizing the CF-203 cell line derived from the midgut of Choristoneura fumiferana, we found that there existed obvious differences in the binding sites and endocytosis pathways for the two forms of Cry1Ac. In addition, it was revealed that Cry1Ac protoxin existed predominantly in the midgut of Plutella xylostella at the early stage after ingesting Cry1Ac crystals, which brought about obvious damage to the midgut epithelium and exhibited different binding sites on the brush border membrane vesicle compared to the toxin. These findings supported the dual mode of action of B. thuringiensis Cry1A proteins and improved our understanding of the molecular features that contribute to the protoxin toxicity.

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