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The Colorado potato beetle, Leptinotarsa decemlineata (Say) ([Coleoptera]: [Chrysomelidae]), is the most important defoliator of solanaceous plants worldwide. This insect displays a notorious ability in adapting to biological and synthetic insecticides, although in some cases this adaptation carries relevant fitness costs. Insecticidal gene silencing by RNA interference is a novel mode of action pesticide against L. decemlineata that is activated by ingestion of a double stranded RNA (dsRNA) targeting a vital L. decemlineata gene. We previously reported laboratory selection of a > 11,000-fold resistant strain of L. decemlineata to a dsRNA delivered topically to potato leaves. In this work, we tested the existence of fitness costs in this dsRNA-resistant colony by comparing biological parameters to the parental strain and an additional susceptible reference strain. Biological parameters included length of egg incubation period, number of eggs per clutch, egg viability, larval viability, length of larval and pupal periods, adult emergence, number of eggs laid per day, sex ratio, and adult longevity. Comparisons between the 3 beetle strains detected no fitness costs associated with resistance to dsRNA. This information is important to guide effective insect resistance management plans for dsRNA insecticides against L. decemlineata applied topically to potato leaves. [ABSTRACT FROM AUTHOR]

Insect midgut cadherins function as receptors and play critical roles as protein receptors of insecticidal Bacillus thuringiensis (Bt) toxins used as biopesticides and in Bt transgenic crops worldwide. Here, we cloned and characterized the full‐length midgut cadherin (CmCad) cDNA from the rice leaffolder (Cnaphalocrocis medinalis), a destructive pest of rice in many Asian countries. Expression of recombinant proteins corresponding to the extracellular domain of CmCad allowed testing binding of Cry proteins. Results from in vitro ligand blotting and enzyme‐linked immunosorbent assays supported that the extracellular domain of CmCad contains regions recognized by both Cry1Ac and Cry2Aa. Molecular modelling and docking simulations indicated that binding to both Cry1Ac and Cry2Aa is localized primarily within a CmCad motif corresponding to residues T1417–D1435. A recombinant CmCad protein produced without residues T1417–D1435 lacked binding to Cry1Ac and Cry2Aa, confirmed our modelling predictions that CmCad has a shared Cry1Ac and Cry2Aa binding site. The potential existence of a shared binding region in CmCad suggests that caution should be taken when using combinations of Cry1Ac and Cry2Aa in pyramided transgenic rice, as their combined use could speed the evolution of resistance to both toxins. [ABSTRACT FROM AUTHOR]

Insect midgut cadherins function as receptors and play critical roles as protein receptors of insecticidal Bacillus thuringiensis (Bt) toxins used as biopesticides and in Bt transgenic crops worldwide. Here, we cloned and characterized the full-length midgut cadherin (CmCad) cDNA from the rice leaffolder (Cnaphalocrocis medinalis), a destructive pest of rice in many Asian countries. Expression of recombinant proteins corresponding to the extracellular domain of CmCad allowed testing binding of Cry proteins. Results from in vitro ligand blotting and enzyme-linked immunosorbent assays supported that the extracellular domain of CmCad contains regions recognized by both Cry1Ac and Cry2Aa. Molecular modelling and docking simulations indicated that binding to both Cry1Ac and Cry2Aa is localized primarily within a CmCad motif corresponding to residues T1417-D1435. A recombinant CmCad protein produced without residues T1417-D1435 lacked binding to Cry1Ac and Cry2Aa, confirmed our modelling predictions that CmCad has a shared Cry1Ac and Cry2Aa binding site. The potential existence of a shared binding region in CmCad suggests that caution should be taken when using combinations of Cry1Ac and Cry2Aa in pyramided transgenic rice, as their combined use could speed the evolution of resistance to both toxins., (© 2021 The Royal Entomological Society.)