Roles of Midgut Cadherin from Two Moths in Different Bacillus thuringiensis Action Mechanisms: Correlation among Toxin Binding, Cellular Toxicity, and Synergism
文献类型： 外文期刊
作者： Gao, Meijing 1 ; Dong, Sa 1 ; Hu, Xiaodan 1 ; Zhang, Xiao 1 ; Liu, Yuan 1 ; Zhong, Jianfeng 1 ; Lu, Lina 1 ; Wang, Yun 4 ; C 1 ;
作者机构： 1.Jiangsu Acad Agr Sci, Inst Food Safety & Nutr, State Key Lab Breeding Base, Key Lab Food Qual & Safety Jiangsu Prov, Nanjing 210014, Jiangsu, Peoples R China
2.Yangzhou Univ, Sch Hort & Plant Protect, Yangzhou 225009, Jiangsu, Peoples R China
3.Univ KwaZulu Natal, Sch Life Sci, Discipline Biol, Westville Campus,Private Bag X54001, ZA-4000 Durban, South Africa
4.Jinling Inst Technol, Hort Dept, Nanjing 210038, Jiangsu, Peoples R China
5.Lishui Acad Agr Sci, Lishui 323000, Peoples R China
关键词： Helicoverpa armigera; Plutella xylostella; cadherin; Bt toxins; mode of action
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）
ISSN： 0021-8561
年卷期： 2019 年 67 卷 48 期
页码：
收录情况： SCI
摘要： The midgut cadherin has been described as one of the main functional receptors for Bacillus thuringiensis (Bt) toxins. Plutella xylostella (P. xylostella) and Helicoverpa armigera (H. armigera) are two major target pests of Bt toxins in China, and the roles of their cadherins in the action of Bt toxins have been only partially studied. Here, we expressed the two cadherins in Sf9 cells and their partial extracellular domains in Escherichia coli and tested them for Bt toxin binding, cellular toxicity, and synergism with toxins. Our results suggested that PxCad might function as a Cry1Ac receptor, although it showed lower binding levels to Cry1Ac and reduced cytotoxicity compared with HaCad. PxCad and HaCad are not receptors for Cry2A, Cry1B, Cry1C, and Cry1F toxins, although some of them can bind to the cadherins. The PxCad-TBR exhibits higher enhancement of Cry1Ac and weak enhancement of Cry1F toxicity in P. xylostella larvae, although it is not the receptor of Cry1F.
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