Synergism of Cry1 Toxins by a Fusion Protein Derived from a Cadherin Fragment and an Antibody Peptide
文献类型： 外文期刊
作者： Gao, Meijing 1 ; Zhong, Jianfeng 1 ; Lu, Lina 1 ; Li, Ying 1 ; Zhang, Zhiyong 1 ;
作者机构： 1.Jiangsu Acad Agr Sci, Inst Food Safety & Nutr, Jiangsu Key Lab Food Qual & Safety, State Key Lab Cultivat Base,Minist Sci & Technol, Nanjing 210014, Peoples R China
关键词： Bt toxins; cadherin; Bt antibody peptide; fusion expression; synergism
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.2； 五年影响因子：6.4 ）
ISSN： 0021-8561
年卷期： 2024 年 72 卷 36 期
页码：
收录情况： SCI
摘要： Synergistic factors can enhance the toxicity of Bt toxins and delay the development of Bt resistance. Previous research has demonstrated that a Helicoverpa armigera cadherin fragment (HaCad-TBR) increased the toxicity of Cry1Ac in Plutella xylostella larvae but did not have a synergistic effect on Cry1B, Cry1C, and Cry1F toxins. In this study, a fusion protein (HaCad-TBR-2D3 VL) derived from HaCad-TBR and a Bt Cry1-specific antibody peptide was expressed in Escherichia coli. The HaCad-TBR-2D3 VL enhanced Cry1Ac toxicity more efficiently in insects and Sf9 cells than HaCad-TBR and also significantly increased the toxicity of Cry1B, Cry1C, and Cry1F toxins in insects. Further investigation indicated that the improved stability in insect midguts and higher binding capacity with Bt toxins contributed to the enhanced synergism of HaCad-TBR-2D3 VL over HaCad-TBR. This study suggested that Bt antibody fragments can potentially broaden the synergistic range of Bt receptor fragments, providing a theoretical foundation for developing broad-spectrum synergists for other biopesticides.
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