Polycalin is involved in the toxicity and resistance to Cry1Ac toxin in Helicoverpa armigera (Hubner)

文献类型： 外文期刊

第一作者： Wang, Bingjie

作者： Wang, Bingjie;Wang, Bingjie;Wang, Yanan;Chen, Lin;Liang, Gemei;Wei, Jizhen

作者机构：

关键词： functional receptor; Helicoverpa armigera; polycalin; resistance mechanisms

期刊名称：ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY （ 影响因子：1.698； 五年影响因子：1.758 ）

ISSN： 0739-4462

年卷期： 2020 年 104 卷 1 期

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收录情况： SCI

摘要： Polycalin has been confirmed as a binding protein of the Cry toxins in a few Lepidoptera insects, but its function in the action mechanism of Cry1Ac and whether it is involved in resistance evolution are still unclear. In this study, Ligand blot and enzyme-linked immunosorbent assays showed that Helicoverpa armigera polycalin could specifically interact with Cry1Ac with a high affinity (K-d = 118.80 nM). Importantly, antisera blocking polycalin in H. armigera larvae decreased the toxicity of Cry1Ac by 31.84%. Furthermore, the relative gene and protein expressions were lower in Cry1Ac-resistant strain (LF60) than that in Cry1Ac-susceptible strain (LF). These findings indicated that H. armigera polycalin was a possible receptor of Cry1Ac and may be contributed to the resistance to Cry1Ac.

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