Yanjiao Feng
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Yanjiao Feng has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Binyan Jin
Innovation Center of Pesticide Research, Department of Applied Chemistry, College of Science, China Agricultural University, Beijing 100193, China
1 shared publication - Jialin Cui
Innovation Center of Pesticide Research, Department of Applied Chemistry, College of Science, China Agricultural University, Beijing 100193, China
1 shared publication - Li Zhang
China Agricultural University
1 shared publication - Libing Liu
Department of Nutrition and Health, China Agricultural University, Beijing 100193, China
1 shared publication - Xiaoming Zhang
Innovation Center of Pesticide Research, Department of Applied Chemistry, College of Science, China Agricultural University, Beijing 100193, China
1 shared publication - Xiuzhen Li
Innovation Center of Pesticide Research, Department of Applied Chemistry, College of Science, China Agricultural University, Beijing 100193, China
1 shared publication
Latest Publications
- Open Access
In Vitro Binding Effects of the Ecdysone Receptor−Binding Domain and PonA in Plutella xylostella
Both insect ecdysone receptors and ultraspiracle belong to the nuclear receptor family. They form a nanoscale self-assembling complex with ecdysteroids in cells, transit into the nucleus, bind with genes to initiate transcription, and perform specific biological functions to regulate the molting, metamorphosis, and growth processes of insects. Therefore, this complex is an important target for the development of eco-friendly insecticides. The diamondback moth (Plutella xylostella) is a devastating pest of cruciferous vegetable crops, wreaking havoc worldwide and causing severe economic losses, and this pest has developed resistance to most chemical insecticides. In this study, highly pure EcR and USP functional domains were obtained by constructing a prokaryotic expression system for the diamondback moth EcR and USP functional domain genes, and the differences between EcR and USP binding domain monomers and dimers were analyzed using transmission electron microscopy and zeta potential. Radioisotope experiments further confirmed that the binding affinity of PonA to the EcR/USP dimer was enhanced approximately 20-fold compared with the binding affinity to the PxGST−EcR monomer. The differences between PonA and tebufenozide in binding with EcR/USP were examined. Molecular simulations showed that the hydrogen bonding network formed by Glu307 and Arg382 on the EcR/USP dimer was a key factor in the affinity enhancement. This study provides a rapid and sensitive method for screening ecdysone agonists for ecdysone receptor studies in vitro.
Open AccessIn Vitro Binding Effects of the Ecdysone Receptor−Binding Domain and PonA in Plutella xylostella
Both insect ecdysone receptors and ultraspiracle belong to the nuclear receptor family. They form a nanoscale self-assembling complex with ecdysteroids in cells, transit into the nucleus, bind with genes to initiate transcription, and perform specific biological functions to regulate the molting, metamorphosis, and growth processes of insects. Therefore, this complex is an important target for the development of eco-friendly insecticides. The diamondback moth (Plutella xylostella) is a devastating pest of cruciferous vegetable crops, wreaking havoc worldwide and causing severe economic losses, and this pest has developed resistance to most chemical insecticides. In this study, highly pure EcR and USP functional domains were obtained by constructing a prokaryotic expression system for the diamondback moth EcR and USP functional domain genes, and the differences between EcR and USP binding domain monomers and dimers were analyzed using transmission electron microscopy and zeta potential. Radioisotope experiments further confirmed that the binding affinity of PonA to the EcR/USP dimer was enhanced approximately 20-fold compared with the binding affinity to the PxGST−EcR monomer. The differences between PonA and tebufenozide in binding with EcR/USP were examined. Molecular simulations showed that the hydrogen bonding network formed by Glu307 and Arg382 on the EcR/USP dimer was a key factor in the affinity enhancement. This study provides a rapid and sensitive method for screening ecdysone agonists for ecdysone receptor studies in vitro.