Simulation of the molecular interaction of CRY1A toxins and three Aminopeptidases N from the sugarcane giant borer (Telchin licus licus)

Background Accordingly to the pore formation model, Bacillus thuringiensis CRY1A toxins, once activated in the midgut of a susceptible insect, participates on a series of binding with protein receptors present in the intestinal epithelium. In Manduca sexta, where the mode of action is better characterized, the first interaction consists of a weak binding of a monomeric toxin to the aminopeptidase N (APN) receptor, allowing it ́s recognition by Cadherin receptors. The protein-protein interactions induce an oligomer formation of CRY molecules, which is introduced into the plasma membrane, forming a pore that causes osmotic lysis [1]. Although there is plenty information about the activity of CRY1A toxins in M. sexta, the same is not observed for Telchin licus licus, an insect that is emerging as a major pest of sugarcane fields in Brazil. The present study aimed at simulating and comparing the interaction of CRY1A toxins with APN receptors of M. sexta and T. licus licus using computational programs.