| Title: | Functional characterization of a binding protein for Type-II sex pheromones in the tea geometrid moth Ectropis obliqua Prout |
| Author(s): | Yan Y; Zhang Y; Tu X; Wang Q; Li Y; Li H; Wang Q; Zhang Y; Sun L; |
| Address: | "Key Laboratory of Tea Quality and Safety Control, Ministry of Agriculture and Rural Affairs, Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou 310008, China. College of Agriculture and Food Science, Zhejiang A & F University, Hangzhou 311300, China. State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, China. Key Laboratory of Tea Quality and Safety Control, Ministry of Agriculture and Rural Affairs, Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou 310008, China. Electronic address: liangsun@tricaas.com" |
| DOI: | 10.1016/j.pestbp.2020.02.008 |
| ISSN/ISBN: | 1095-9939 (Electronic) 0048-3575 (Linking) |
| Abstract: | "The tea geometrid moth Ectropis obliqua Prout is one of the most serious moth pests in tea plants, and its sex pheromones have been identified as typical Type-II polyunsaturated hydrocarbons and epoxide derivatives. Therefore, the E. obliqua male olfactory system provides a good model to study the molecular basis of Type-II sex pheromone recognition as well as functional gene evolution towards structurally different types of moth sex pheromones. In this study, we identified the full-length sequence of a pheromone-binding protein, EoblPBP2 and revealed that it clustered together with the lepidopteran PBP2 subfamily, which binds Type I acetate pheromones. These findings suggest that the EoblPBP2 sequence and physiological function are conserved, although E. obliqua evolved Type II hydrocarbon and epoxide sex pheromones structurally different from Type I acetates. To examine this hypothesis, we studied the expression patterns and in vitro functions of EoblPBP2 in detail. Quantitative real-time PCR experiments showed that EoblPBP2 was predominantly expressed in male E. obliqua antennae. Fluorescence in situ hybridization further demonstrated that the EoblPBP2 gene was abundantly expressed in the pheromone-sensitive sensilla trichodea Str-I in male E. obliqua. The physiological function of recombinant EoblPBP2 was then examined using a competitive binding assay. The results showed that EoblPBP2 had high affinities for three E. obliqua Type II sex pheromone components and Type I acetate pheromones in comparison to some plant volatiles. These results indicate that PBP2 is involved in the detection of Type II pheromones in E. obliqua and it still retains high binding affinities to acetate pheromones and some green leaf ester volatiles" |
| Keywords: | "Animals Carrier Proteins In Situ Hybridization, Fluorescence Insect Proteins Male *Moths Pheromones *Sex Attractants Tea Ectropis obliqua Prout Fluorescence in situ hybridization Functional evolution Pheromone-binding protein Type II sex pheromones;" |
| Notes: | "MedlineYan, Yuting Zhang, Yuxing Tu, Xiaohui Wang, Qian Li, Yujie Li, Hongyue Wang, Qi Zhang, Yongjun Sun, Liang eng 2020/05/04 Pestic Biochem Physiol. 2020 May; 165:104542. doi: 10.1016/j.pestbp.2020.02.008. Epub 2020 Feb 11" |
