Synthesis and Characterization of Cry2Ab-AVM Bioconjugate: Enhanced Affinity to Binding Proteins and Insecticidal Activity

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 fou...

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Bibliographic Details
Published in:Toxins 2019-08, Vol.11 (9), p.497
Main Authors: Pan, Zhi-Zhen, Xu, Lian, Zheng, Yi-Shu, Niu, Li-Yang, Liu, Bo, Fu, Nan-Yan, Shi, Yan, Chen, Qing-Xi, Zhu, Yu-Jing, Guan, Xiong
Format: Article
Language:English
Subjects:
Affinity
Avermectin
binding affinity
Binding sites
Cadherins
Cry2Ab–AVM bioconjugate
Insecticides
Ligands
Molecular docking
Molecular weight
Pest control
Pests
Proteins
Toxins
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Summary: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 , 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 cadherin (PxCR ), with a much higher affinity (dissociation equilibrium constant = 3.44 nM) than Cry2Ab30 ( = 28.7 nM). Molecular docking suggested that the macrolide lactone group of Cry2Ab-AVM ligand docking into the PxCR is a potential mechanism to enhance the binding affinity of Cry2Ab-AVM to PxCR . These findings offer scope for the engineering of Bt toxins by bioconjugation for improved pest management.
ISSN:2072-6651
2072-6651
DOI:10.3390/toxins11090497