Gao Meijing, Zhong Jianfeng, Lu Lina, Li Ying, Zhang Zhiyong
State Key Laboratory Cultivation Base, Ministry of Science and Technology─Jiangsu Key Laboratory for Food Quality and Safety, Institute of Food Safety and Nutrition, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China.
J Agric Food Chem. 2024 Sep 11;72(36):19689-19698. doi: 10.1021/acs.jafc.4c05875. Epub 2024 Aug 27.
Synergistic factors can enhance the toxicity of Bt toxins and delay the development of Bt resistance. Previous research has demonstrated that a cadherin fragment (HaCad-TBR) increased the toxicity of Cry1Ac in larvae but did not have a synergistic effect on Cry1B, Cry1C, and Cry1F toxins. In this study, a fusion protein (HaCad-TBR-2D3 V) derived from HaCad-TBR and a Bt Cry1-specific antibody peptide was expressed in . The HaCad-TBR-2D3 V 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 V 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.
协同因子可以增强Bt毒素的毒性并延缓Bt抗性的发展。先前的研究表明，一种钙黏蛋白片段（HaCad-TBR）可增加Cry1Ac对幼虫的毒性，但对Cry1B、Cry1C和Cry1F毒素没有协同作用。在本研究中，一种源自HaCad-TBR和Bt Cry1特异性抗体肽的融合蛋白（HaCad-TBR-2D3 V）在[具体表达宿主未给出]中表达。与HaCad-TBR相比，HaCad-TBR-2D3 V在昆虫和Sf9细胞中更有效地增强了Cry1Ac的毒性，并且还显著增加了Cry1B、Cry1C和Cry1F毒素对昆虫的毒性。进一步研究表明，在昆虫中肠中稳定性的提高以及与Bt毒素更高的结合能力有助于HaCad-TBR-2D3 V比HaCad-TBR具有更强的协同作用。本研究表明，Bt抗体片段可能会拓宽Bt受体片段的协同范围，为开发其他生物杀虫剂的广谱增效剂提供理论基础。
