Occurrence of a common binding site in Mamestra brassicae, Phthorimaea operculella, and Spodoptera exigua for the insecticidal crystal proteins CryIA from Bacillus thuringiensis.

Specific binding to midgut membrane proteins is required for the toxicity of insecticidal crystal proteins (ICP) from Bacillus thuringiensis. A direct relationship between toxicity and binding has been proposed. It has been hypothesized that sharing of a single receptor by more than one ICP could lead to the occurrence of multiple resistance in the event of an alteration in the common receptor. Binding of CryIA(a), CryIA(b) and CryIA(c), three structurally related ICPs, has been studied in Phthorimaea operculella, Mamestra brassicae and, Spodoptera exigua using brush border membrane vesicles (BBMV) from the midgut tissue. Using iodinated CryIA(b), the three insects showed similar results: one binding site for CryIA(b), which is shared with CryIA(a) and CryIA(c). The binding site concentrations obtained for CryIA(b) in P. operculella, M. brassicae and S. exigua were 5.1, 16.3 and 2.2 pmol/mg vesicle protein, respectively. In the same way, dissociation constants were 3.8, 5.3 and 0.7 nM. Data show that binding for an ICP does not directly imply toxicity. The occurrence of a common receptor for the CryIA subgroup of ICPs in P. operculella, M. brassicae and S. exigua might theoretically discourage the use of combinations of these ICPs in integrated pest management programmes.