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Polycalin is involved in the action mechanism of Cry2Aa toxin in Helicoverpa armigera(Hübner)

Polycalin is involved in the action mechanism of Cry2Aa toxin in Helicoverpa armigera(Hübner)
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摘要 Receptor proteins on the brush border membrane of the insect midgut epithelium are involved in the mode of action of insecticidal Cry proteins from Bacillus thuringiensis(Bt). Polycalin has been identified as a binding protein of the Bt Cry1 Ac toxin in several Lepidoptera including Helicoverpa armigera, but its role in the action mechanism of Cry2 Aa is still unclear. In this study, we investigated the binding characteristics of polycalin from the midgut of H. armigera with Cry2 Aa and its role in the toxicity of Cry2 Aa. The results demonstrated that heterologously expressed H. armigera polycalin peptide could bind with Cry2 Aa with high affinity(K_d=32 nmol L^(–1)). The toxicity of Cry2 Aa decreased by 27% after H. armigera larvae ingested polycalin antisera. These results suggested that polycalin could be a potential functional receptor for Cry2 Aa, and it plays an important role in the susceptibility of H. armigera to Cry2 Aa. Receptor proteins on the brush border membrane of the insect midgut epithelium are involved in the mode of action of insecticidal Cry proteins from Bacillus thuringiensis(Bt). Polycalin has been identified as a binding protein of the Bt Cry1 Ac toxin in several Lepidoptera including Helicoverpa armigera, but its role in the action mechanism of Cry2 Aa is still unclear. In this study, we investigated the binding characteristics of polycalin from the midgut of H. armigera with Cry2 Aa and its role in the toxicity of Cry2 Aa. The results demonstrated that heterologously expressed H. armigera polycalin peptide could bind with Cry2 Aa with high affinity(K_d=32 nmol L^(–1)). The toxicity of Cry2 Aa decreased by 27% after H. armigera larvae ingested polycalin antisera. These results suggested that polycalin could be a potential functional receptor for Cry2 Aa, and it plays an important role in the susceptibility of H. armigera to Cry2 Aa.
出处 《Journal of Integrative Agriculture》 SCIE CAS CSCD 2019年第3期627-635,共9页 农业科学学报(英文版)
基金 supported by the Key Project for Breeding Genetically Modified Organisms, China (2016ZX08011002) the National Natural Science Foundation of China (31621064) the Fundamental Research Funds for Central Non-profit Scientific Institution, China (Y2017JC34)
关键词 HELICOVERPA ARMIGERA polycalin INSECTICIDAL toxicity ANTISERA binding AFFINITY Helicoverpa armigera polycalin insecticidal toxicity antisera binding affinity
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