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Identification of a Cry1Fa binding site of cadherin in Plutella xylostella through fragment exchanging and molecular docking methods

文献类型： 外文期刊

作者： Gao, Meijing 1 ; Hu, Xiaodan 1 ; Zhang, Xiao 1 ; Zhong, Jianfeng 1 ; Lu, Lina 1 ; Liu, Yuan 1 ; Dong, Sa 2 ; Wang, Yun 3 ; L 1 ;

作者机构： 1.Jiangsu Acad Agr Sci, Key Lab Food Qual & Safety Jiangsu Prov, State Key Lab Breeding Base, Inst Food Safety & Nutr, Nanjing 210014, Peoples R China

2.Yangzhou Univ, Sch Hort & Plant Protect, Yangzhou, Jiangsu, Peoples R China

3.Jinling Inst Technol, Hort Dept, Nanjing, Peoples R China

关键词： Cryl Fa; Cad herin; Binding sites; Fragment exchanging; Molecular docking

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：6.953； 五年影响因子：6.737 ）

ISSN： 0141-8130

年卷期： 2020 年 146 卷

页码：

收录情况： SCI

摘要： Binding to the cadherin in target pests is the primary step in the action mechanism of Cry toxins, but little is known regarding the interaction of Cry1Fa with cadherin. Our previous study suggested that a Plutella xylostella cadherin fragment (PxCad-TBR) can bind to Cry1Fa, while its homologous fragment (HaCad-TBR) in Helicoverpa armigera cannot. In this study, we expressed two cadherin fragments that combine parts of PxCad-TBR and HaCad-TBR in Escherichia coli and tested their binding to the Cry1Fa. The results showed that the fragment containing amino acids T1202-A1341 of P. xylostella cadherin showed binding ability to Cry1Fa. Furthermore, two regions (V1219-E1233 and D1326-F1337) were predicted as hot spot regions that are involved in the interaction of Cry1Fa and PxCad-TBR with computer-aided molecular docking. We then constructed two PxCad-TBR mutations by fragment exchanging based on the molecular docking results and verified the mutations' binding abilities to the Cry1Fa. The results showed that the region that contains amino acids D1326-F1337 was one important binding site to Cry1Fa in P. xylostella cadherin. These results suggested that a combination of computer-aided molecular docking and fragment exchanging is an effective way to locate the key binding sites of Bt toxins in receptors. (C) 2019 Elsevier B.V. All rights reserved.

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