Delta endotoxin

Delta endotoxins (δ-endotoxins) are pore-forming toxins produced by Bacillus thuringiensis species of bacteria. They are useful for their insecticidal action and are the primary toxin produced by Bt maize/corn. During spore formation the bacteria produce crystals of such proteins (hence the name Cry toxins) that are also known as parasporal bodies, next to the endospores; as a result some members are known as a parasporin. The Cyt (cytolytic) toxin group is a group of delta-endotoxins different from the Cry group. When an insect ingests these proteins, they are activated by proteolytic cleavage. The N-terminus is cleaved in all of the proteins and a C-terminal extension is cleaved in some members. Once activated, the endotoxin binds to the gut epithelium and causes cell lysis by the formation of cation-selective channels, which leads to death. For many years there was no clarity as to the relationship between aminopeptidase N and Bt toxins. Although AP-N does bind Cry proteins in vitro (reviewed by Soberón et al. 2009 and Pigott & Ellar 2007), no cases of resistance or even reduced in vitro binding due to AP-N structure alteration were known through 2002, and there was some doubt that the resistance mechanism was so straight forward. Indeed, Luo et al. 1997, Mohammed et al. 1996, and Zhu et al. 2000 positively found this to not occur in Lepidoptera examples. Subsequently, however Herrero et al. 2005 showed correlation between nonexpression and Bt resistance, and actual resistance was found in Helicoverpa armigera by Zhang et al. 2009, in Ostrinia nubilalis by Khajuria et al. 2011, and in Trichoplusia ni by Baxter et al. 2011 and Tiewsiri & Wang 2011 (also all Lepidoptera). There continues to be confirmation that AP-Ns do not by themselves affect resistance in some cases, possibly due to sequential binding by the toxin being required to produce its effect. In this sequence each binding step is theoretically not indispensable, but if it occurs does contribute to the final pore formation result.