ArticleApplied and environmental microbiology2013
A Spodoptera exigua cadherin serves as a putative receptor for Bacillus thuringiensis Cry1Ca toxin and shows differential enhancement of Cry1Ca and Cry1Ac toxicity.
Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 64 citations in OpenAlex.
- Calcineurin-dependent 20E signaling pathway enhances attacin expression to prime the immunity of Helicoverpa armigera against Bacillus thuringiensis Cry1Ac toxin.PLoS pathogens · 2026Article
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- Research Progresses on the Function and Detection Methods of Insect Gut Microbes.Microorganisms · 2023Review
- Effects of theFrontiers in microbiology · 2023Article
- The main component of the aphid alarm pheromone (Frontiers in plant science · 2022Article
- Large-scale genome-wide study reveals climate adaptive variability in a cosmopolitan pest.Nature communications · 2021Article
- Article
- Combined Transcriptomic Analysis and RNA Interference Reveal the Effects of Methoxyfenozide on Ecdysone Signaling Pathway ofInternational journal of molecular sciences · 2021Article
- Differences in midgut transcriptomes between resistant and susceptible strains of Chilo suppressalis to Cry1C toxin.BMC genomics · 2020Article
- Article
- iTRAQ-Based Comparative Proteomic Analysis of Larval Midgut From the Beet Armyworm,Frontiers in physiology · 2020Article
- Cadherin CsCad plays differential functional roles in Cry1Ab and Cry1C intoxication in Chilo suppressalis.Scientific reports · 2019Article
- Spodoptera frugiperda (J. E. Smith) Aminopeptidase N1 Is a Functional Receptor of the Bacillus thuringiensis Cry1Ca Toxin.Applied and environmental microbiology · 2018Article
- Identification and Characterization of Hyphantria cunea Aminopeptidase N as a Binding Protein of Bacillus thuringiensis Cry1Ab35 Toxin.International journal of molecular sciences · 2017Article
- Transgenic Bt rice lines producing Cry1Ac, Cry2Aa or Cry1Ca have no detrimental effects on Brown Planthopper and Pond Wolf Spider.Scientific reports · 2017Article
- Aminopeptidase N1 is involved in Bacillus thuringiensis Cry1Ac toxicity in the beet armyworm, Spodoptera exigua.Scientific reports · 2017Article
- Proteomic analysis of Cry2Aa-binding proteins and their receptor function in Spodoptera exigua.Scientific reports · 2017Article
- Article
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8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Crystal toxin Cry1Ca from Bacillus thuringiensis has an insecticidal spectrum encompassing lepidopteran insects that are tolerant to current commercially used B. thuringiensis crops (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, from Spodoptera exigua (relatively susceptible to Cry1Ca). SeCad1b was 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 from Helicoverpa 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 of SeCad1b double-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 of S. exigua and H. armigera. Thus, we provide the first lines of evidence to suggest that SeCad1b from S. exigua is a functional receptor of Cry1Ca.
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