文献类型：期刊文献

英文题名：Role of odorant binding proteins in the response of Tetranychus cinnabarinus to repellent activity of ethyl oleate

作者：Chen, Yi-Juan[1];Zhang, Tong-Yao[1];Wan, Nian-Feng[2];Zhao, Jie[3];Jiang, Jie-Xian[1];Ji, Xiang-Yun[1]

机构：[1]Shanghai Acad Agr Sci, Shanghai Engn Res Ctr Low Carbon Agr, Shanghai Key Lab Protected Hort Technol, Ecoenvironm Protect Inst, Shanghai 201403, Peoples R China;[2]East China Univ Sci & Technol, Sch Pharm, Shanghai Key Lab Chem Biol, Shanghai 200237, Peoples R China;[3]Shanghai Pudong New Dist Agro Technol Extens Ctr, 66 Changxin East Rd, Shanghai 201201, Peoples R China

年份：2025

卷号：185

外文期刊名：INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:001608461500002)】；

基金：This work was supported by the National Natural Science Foundation of China (31801746), Shanghai Rising-Star Program (21QB1404100), Shanghai Agriculture Commission of China (2018-1-25), Shanghai Academy of Agriculture Science Program for Excellent Research Team ((2022) 017). We thank the staff at the core facility of molecular biology center of Center for Excellence in Molecular Cell Science for their technical assistance in binding affinity experiment.

语种：英文

外文关键词：Microscale thermophoresis (MST); RNA interference (RNAi); Molecular Dynamics (MD) simulations; Site-directed mutagenesis

摘要：Novel pest population control strategies that use natural products to disrupt the host-seeking behaviors of pests are imperative in modern pest management. Odorant-binding proteins (OBPs), which are responsible for odorant recognition and signal transduction in the pest olfactory system, play key roles in host localization. We previously reported that ethyl oleate (EO) exhibits significant repellent properties against the highly destructive polyphagous crop pest Tetranychus cinnabarinus; however, the molecular mechanism remains unknown. In the present study, two OBPs (TcinOBP1 and TcinOBP2) from T. cinnabarinus were identified and their EO-induced expression profiles were detected. The results suggested that TcinOBP1 exhibited significant upregulation at 15 min and gradual decrease at 45 min post-EO-treatment. Microscale thermophoresis (MST) showed that the recombinant TcinOBP1 protein displayed a strong binding affinity to EO (Kd = 32.3 mu M). RNA interference (RNAi) analysis demonstrated that a significant inhibition of TcinOBP1 transcript led to a remarkable reduction in the sensitivity of T. cinnabarinus to the repellent activity of EO. Furthermore, computational simulations indicated that TcinOBP1 employed five alpha-helices and three disulfide bridges, forming a hydrophobic pocket composed of several nonpolar and polar amino acid residues to bind with EO, and hydrophobic interactions was the dominating driving force. Among these residues, six amino acid residues (Leu83, Trp132, Glu147, Ile148, Met190, and Ile194) were confirmed to be essential for the binding of TcinOBP1 to EO through site-directed mutagenesis and binding assays. These results demonstrated that TcinOBP1 is likely involved in mediating the responses of T. cinnabarinus to EO. This finding provides new insights into the olfactory molecular mechanism of OBPs with chemicals in mites and reveals that TcinOBP1 serves as a novel target for developing new and efficient mite control strategies.