Interactions between insecticidal cry toxins and their receptors.

Bacillus thuringiensis is a prominent, eco-friendly entomopathogenic bacterium used as a plant-incorporated toxin in genetically modified crops and as a stomach poison for insects in the form of spore formulations. Upon entering the alkaline environment of the insect gut, the toxin undergoes proteolytic breakdown, converting the protoxin into its activated form. The activated toxin then binds to receptors, forming pores that disrupt the ionic balance within the cell, ultimately leading to the insect's death. Alongside the four major receptors (Cadherin, ABCC, APN, and ALP), several other notable receptors are present on the Brush Border Membrane Vesicle of insects. Binding to these receptors plays a crucial role, and any mutations in these receptors can result in improper binding, leading to the development of resistant insect strains. This review explores the major receptors of insecticidal Cry toxins, the intricate interactions between toxins and receptors, receptor mutations, and strategies to overcome the resistance.