ABSTRACTCrystal toxin Cry1Ca fromBacillus thuringiensishas an insecticidal spectrum encompassing lepidopteran insects that are tolerant to current commercially usedB. thuringiensiscrops (Bt crops) expressing Cry1A toxins and may be useful as a potential bioinsecticide. The mode of action of Cry1A is fairly well understood. However, whether Cry1Ca interacts with the same receptor proteins as Cry1A remains unproven. In the present paper, we first cloned a cadherin-like gene,SeCad1b, fromSpodoptera exigua(relatively susceptible to Cry1Ca).SeCad1bwas highly expressed in the larval gut but scarcely detected in fat body, Malpighian tubules, and remaining carcass. Second, we bacterially expressed truncated cadherin rSeCad1bp and its interspecific homologue rHaBtRp fromHelicoverpa armigera(more sensitive to Cry1Ac) containing the putative toxin-binding regions. Competitive binding assays showed that both Cry1Ca and Cry1Ac could bind to rSeCad1bp and rHaBtRp, and they did not compete with each other. Third, Cry1Ca ingestion killed larvae and decreased the weight of surviving larvae. Dietary introduction ofSeCad1bdouble-stranded RNA (dsRNA) reduced approximately 80% of the target mRNA and partially alleviated the negative effect of Cry1Ca on larval survival and growth. Lastly, rSeCad1bp and rHaBtRp differentially enhanced the negative effects of Cry1Ca and Cry1Ac on the larval mortalities and growth ofS. exiguaandH. armigera. Thus, we provide the first lines of evidence to suggest that SeCad1b fromS. exiguais a functional receptor of Cry1Ca.