Discrimination of Oviposition Deterrent Volatile beta-Ionone by Odorant-Binding Proteins 1 and 4 in the Whitefly Bemisia tabaci
文献类型： 外文期刊
作者： Li, Fengqi 1 ; Li, Du 1 ; Dewer, Youssef 3 ; Qu, Cheng 1 ; Yang, Zhen 4 ; Tian, Jiahui 1 ; Luo, Chen 1 ;
作者机构： 1.Beijing Acad Agr & Forestry Sci, Inst Plant & Environm Protect, Beijing Key Lab Environm Friendly Management Frui, Beijing 100097, Peoples R China
2.Huazhong Agr Univ, Coll Plant Sci & Technol, Hubei Key Lab Insect Resource Applicat & Sustaina, Wuhan 430070, Hubei, Peoples R China
3.Agr Res Ctr, Bioassay Res Dept, Cent Agr Pesticide Lab, Sabahia Plant Protect Res Stn, Alexandria 21616, Egypt
4.Tianjin Univ Tradit Chinese Med, Chinese Mat Med Coll, Tianjin 300000, Peoples R China
关键词： Bemisia tabaci; odorant-binding protein; competitive binding; beta-ionone
期刊名称：BIOMOLECULES （ 影响因子：4.879； 五年影响因子：5.362 ）
ISSN：
年卷期： 2019 年 9 卷 10 期
页码：
收录情况： SCI
摘要： The whitefly, Bemisia tabaci, is an important invasive economic pest of agricultural crops worldwide. beta-ionone has a significant oviposition repellent effect against B. tabaci, but the olfactory molecular mechanism of this insect for recognizing beta-ionone is unclear. To clarify the binding properties of odorant-binding proteins (OBPs) with beta-ionone, we performed gene cloning, evolution analysis, bacterial expression, fluorescence competitive binding assay, and molecular docking to study the binding function of OBP1 and OBP4 on beta-ionone. The results showed that after the OBP1 and OBP4 proteins were recombined, the compound beta-ionone exhibited a reduction in the fluorescence binding affinity to <50%, with a dissociation constant of 5.15 and 3.62 mu M for OBP1 and OBP4, respectively. Our data indicate that beta-ionone has high affinity for OBP1 and OBP4, which play a crucial role in the identification of oviposition sites in B. tabaci. The findings of this study suggest that whiteflies employ beta-ionone compound in the selection of the suitable egg-laying sites on host plants during the oviposition behavior.
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