Synthesis and Characterization of Cry2Ab-AVM Bioconjugate: Enhanced Affinity to Binding Proteins and Insecticidal Activity
文献类型： 外文期刊
作者： Pan, Zhi-Zhen 1 ; Xu, Lian 3 ; Zheng, Yi-Shu 3 ; Niu, Li-Yang 3 ; Liu, Bo 2 ; Fu, Nan-Yan 4 ; Shi, Yan 3 ; Chen, Qing-Xi; 1 ;
作者机构： 1.Fujian Agr & Forestry Univ, Coll Plant Protect, State Key Lab Ecol Control Fujian Taiwan Crop Pes, Key Lab Biopesticide & Chem Biol,Minist Educ, Fuzhou 350002, Fujian, Peoples R China
2.Fujian Acad Agr Sci, Agr Bioresources Res Inst, Fuzhou 350003, Fujian, Peoples R China
3.Xiamen Univ, Sch Life Sci, Xiamen 361005, Fujian, Peoples R China
4.Fuzhou Univ, Coll Chem, MOE Key Lab Analyt Sci Food Safety & Biol, Fuzhou 350116, Fujian, Peoples R China
5.Fuzhou Univ, Coll Chem, Fujian Prov Key Lab Anal & Detect Technol Food Sa, Fuzhou 350116, Fujian, Peoples R China
关键词： Cry2Ab-AVM bioconjugate; binding affinity; molecular docking
期刊名称：TOXINS （ 影响因子：4.546； 五年影响因子：4.8 ）
ISSN：
年卷期： 2019 年 11 卷 9 期
页码：
收录情况： SCI
摘要： Bacillus thuringiensis insecticidal proteins (Bt toxins) have been widely used in crops for agricultural pest management and to reduce the use of chemical insecticides. Here, we have engineered Bt toxin Cry2Ab30 and bioconjugated it with 4"-O-succinyl avermectin (AVM) to synthesize Cry2Ab-AVM bioconjugate. It was found that Cry2Ab-AVM showed higher insecticidal activity against Plutella xylostella, up to 154.4 times compared to Cry2Ab30. The binding results showed that Cry2Ab-AVM binds to the cadherin-like binding protein fragments, the 10th and 11th cadherin repeat domains in the P. xylostella cadherin (PxCR(10-11)), with a much higher affinity (dissociation equilibrium constant K-D = 3.44 nM) than Cry2Ab30 (K-D = 28.7 nM). Molecular docking suggested that the macrolide lactone group of Cry2Ab-AVM ligand docking into the PxCR(10-11) is a potential mechanism to enhance the binding affinity of Cry2Ab-AVM to PxCR(10-11). These findings offer scope for the engineering of Bt toxins by bioconjugation for improved pest management.
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