| Title: | Function and Characterization Analysis of BodoOBP8 from Bradysia odoriphaga (Diptera: Sciaridae) in the Recognition of Plant Volatiles and Sex Pheromones |
| Author(s): | Yang Y; Luo L; Tian L; Zhao C; Niu H; Hu Y; Shi C; Xie W; Zhang Y; |
| Address: | "Forewarning and Management of Agricultural and Forestry Pests, Hubei Engineering Technology Center, Yangtze University, Jingzhou 434025, China. Institute of Plant and Environment Protection Beijing Academy of Agriculture and Forestry Sciences, Beijing 100081, China. Department of Plant Protection, Institute of Vegetables and Flowers, Chinese Academy of Agricultural Sciences, Beijing 100081, China" |
| ISSN/ISBN: | 2075-4450 (Print) 2075-4450 (Electronic) 2075-4450 (Linking) |
| Abstract: | "The belowground pest Bradysia odoriphaga (Diptera: Sciaridae) has a sophisticated and sensitive olfactory system to detect semiochemical signals from the surrounding environment. In particular, odorant-binding proteins (OBPs) are crucial in capturing and transporting these semiochemical signals across the sensilla lymph to the corresponding odorant receptors. In this study, we cloned a full-length cDNA sequence of BodoOBP8 from B. odoriphaga. Real-time PCR (qRT-PCR) analysis revealed that BodoOBP8 has the highest expression levels in males, with more pronounced expression in the male antennae than in other tissues. In this study, the recombinant protein BodoOBP8 was successfully expressed by a bacterial system to explore its function. Competitive binding assays with 33 host plant volatiles and one putative sex pheromone (n-heptadecane) revealed that purified BodoOBP8 strongly bound to two sulfur compounds (methyl allyl disulfide and diallyl disulfide) and to n-heptadecane; the corresponding dissolution constants (Ki) were 4.04, 6.73, and 4.04 muM, respectively. Molecular docking indicated that Ile96, Ile103, Ala107, and Leu111, located in the hydrophobic cavity of BodoOBP8, are the key residues mediating the interaction of BodoOBP8 with two sulfur compounds (methyl allyl disulfide and diallyl disulfide) and n-heptadecane. These results show that BodoOBP8 plays a role in the recognition of plant volatiles and sex pheromones, suggesting its application as a molecular target for the screening of B. odoriphaga attractants and repellents and facilitating a new mechanism of B. odoriphaga control" |
| Keywords: | Bradysia odoriphaga competitive binding assay homology modeling molecular docking odorant-binding protein; |
| Notes: | "PubMed-not-MEDLINEYang, Yuting Luo, Liang Tian, Lixia Zhao, Changwei Niu, Hongli Hu, Yifeng Shi, Caihua Xie, Wen Zhang, Youjun eng SKJC-2020-02-012/the 2020 Research Program of Sanya Yazhou Bay Science and Technology City/ CARS-24-C-02/China Agriculture Research System/ CAAS-ASTIP-IVFCAAS/the Beijing Key Laboratory for Pest Control and Sustainable Cultivation of Vegetables and the Science, and Technology Innovation Program of the Chinese Academy of Agricultural Sciences/ 31772170/National Natural Science Foundation of China/ 32001904/National Natural Science Foundation/ 32102202/National Natural Science Foundation/ Switzerland 2021/10/24 Insects. 2021 Sep 28; 12(10):879. doi: 10.3390/insects12100879" |
