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Updated: Jan 1, 2026
Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
Published on: November 30, 2018
Identification of a Cry1Fa binding site of cadherin in Plutella xylostella through fragment exchanging and molecular
Meijing Gao1, Xiaodan Hu1, Xiao Zhang1
1Key Lab of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Institute of Food Safety and Nutrition, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China.
Abstract:
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.
