Roles of midgut cadherin from two moths in different Bt action mechanisms: correlation among toxin binding, cellular toxicity and synergism

The midgut cadherin has been described as one of the main functional receptors for Bacillus thuringiensis (Bt) toxins. Plutella xylostella (P. xylostella) and Helicoverpa armigera (H. armigera) are two major target pests of Bt toxins in China, and the roles of their cadherins in the action of Bt toxins have been only partially studied. Here, we expressed the two cadherins in Sf9 cells and their partial extracellular domains in Escherichia coli and tested them for Bt toxin binding, cellular toxicity, and synergism with toxins. Our results suggested that PxCad might function as a Cry1Ac receptor, although it showed lower binding levels to Cry1Ac and reduced cytotoxicity compared with HaCad. PxCad and HaCad are not receptors for Cry2A, Cry1B, Cry1C, and Cry1F toxins, although some of them can bind to the cadherins. The PxCad-TBR exhibits higher enhancement of Cry1Ac and weak enhancement of Cry1F toxicity in P. xylostella larvae, although it is not the receptor of Cry1F.