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• W2951260214 abstract "Abstract Transgenic rice lines expressing Bacillus thuringiensis (Bt) toxins have been successfully developed for the control of Chilo suppressalis . However, the evolution of insect resistance is a major threat to Bt rice durability. Bt toxins function by binding specific receptors in the midgut of target insects; specifically, cadherin proteins have been identified as Cry toxin receptors in diverse lepidopteran species. Here, we report the functional roles of cadherin CsCad in the midgut of C . suppressalis in Cry1Ab and Cry1C toxicity. We expressed a recombinant truncated CsCad peptide (CsCad-CR11-MPED) in Escherichia coli that included the eleventh cadherin repeat and MPED region. Based on ligand blotting and ELISA binding assays, the CsCad-CR11-MPED peptide specifically bound Cry1Ab with high affinity but weakly bound Cry1C. The CsCad-CR11-MPED peptide significantly enhanced the susceptibility of C . suppressalis larvae to Cry1Ab but not Cry1C. Furthermore, the knockdown of endogenous CsCad with Stealth siRNA reduced C . suppressalis larval susceptibility to Cry1Ab but not Cry1C, suggesting that CsCad plays differential functional roles in Cry1Ab and Cry1C intoxication in C . suppressalis . This information directly enhances our understanding of the potential resistance mechanisms of C . suppressalis against Bt toxins and may assist in the development of effective strategies for delaying insect resistance." @default.
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• W2951260214 date "2019-06-11" @default.
• W2951260214 modified "2023-10-17" @default.
• W2951260214 title "Cadherin CsCad plays differential functional roles in Cry1Ab and Cry1C intoxication in Chilo suppressalis" @default.
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• W2951260214 doi "https://doi.org/10.1038/s41598-019-44451-5" @default.
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