Polycalin is involved in the toxicity and resistance to Cry1Ac toxin in Helicoverpa armigera (Hubner)
文献类型： 外文期刊
作者： Wang, Bingjie 1 ; Wei, Jizhen 3 ; Wang, Yanan 2 ; Chen, Lin 2 ; Liang, Gemei 2 ;
作者机构： 1.Minist Agr & Rural Affairs, Environm & Plant Protect Inst, Chinese Acad Trop Agr Sci, Key Lab Integrated Pest Management Trop Crops, Haikou, Hainan, Peoples R China
2.Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing 100193, Peoples R China
3.Henan Agr Univ, Coll Plant Protect, State Key Lab Wheat & Maize Crop Sci, Zhengzhou, Peoples R China
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
页码：
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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