Coordinated binding of a two-component insecticidal protein from Alcaligenes faecalis to western corn rootworm midgut tissue

Dissecting Out the Molecular Mechanism of Insecticidal Activity of Ostreolysin A6/Pleurotolysin B Complexes on Western Corn Rootworm

“…Further, there have been reports of Cry34Ab1 protein receptor(s) in WCR larva midgut membranes [42,47], which appear to be unique and unrelated to other Cry toxins [48]. The binary insecticidal protein complex AflP-1A/AfIP-1B likely shares the same binding sites as Cry34Ab1/Cry35Ab1 in WCR BBMVs [16,46].…”

“…Similar to the action of OlyA6/PlyB, the swelling and disruption of WCR midgut cells by Cry34Ab1/Cry35Ab1 [37] indicate a membrane-targeted mechanism that might derive from the formation of ion channels. Indeed, it has been shown that bacterial aegerolysin-based insecticidal complexes active against WCR (Cry34Ab1/Cry35Ab1 from B. thuringiensis and AfIP-1A/AfIP-1B from Alcaligenes faecalis) can permeabilise artificial phospholipid membranes that are devoid of proteins [45,46]. However, this membrane activity appears to be weaker and not as lipid-specific as for the aegerolysins produced by the Pleurotus mushrooms [25].…”

IPD072Aa from Pseudomonas chlororaphis Targets Midgut Epithelial Cells in Killing Western Corn Rootworm ( Diabrotica virgifera virgifera )

“…AfIP-1A/1B exhibited specific binding to WCR BBMVs at binding sites that were different from Cry3 proteins, but the same as those that bind Gpp34Ab1/Tpp35Ab1. The shared binding sites corresponded to cross-resistance to Gpp34Ab1/Tpp35Ab1 which was demonstrated using a resistant strain of WCR ( 6 , 21 ). The basis of the shared binding sites and cross-resistance was illuminated when the experimental structure of AfIP-1A was solved and found to have an aegerolysin fold with strong similarity to the structure of Gpp34Ab1, another aegerolysin.…”