Molecular Characterization and Key Binding Sites of Sex Pheromone-Binding Proteins from the Meadow Moth, Loxostege sticticalis
| Autor: | Yinliang Wang, Ertao Li, Bingzhong Ren, Haifeng Zhou, Jin-Qiao Li, Zhang Shuai, Ming Wen, Jiao Yin, Kebin Li, Qi Chen |
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| Rok vydání: | 2019 |
| Předmět: |
Loxostege sticticalis
biology Chemistry Ligand binding assay General Chemistry biology.organism_classification DNA-binding protein Biochemistry Sex pheromone embryonic structures Mating Binding site General Agricultural and Biological Sciences Site-directed mutagenesis Gene reproductive and urinary physiology |
| Zdroj: | Journal of Agricultural and Food Chemistry. 67:12685-12695 |
| ISSN: | 1520-5118 0021-8561 |
| Popis: | The meadow moth, Loxostege sticticalis, is a typical agricultural pest that uses sex pheromones to mediate mating behavior; however, the mechanism underlying the selectivity of its pheromone-binding proteins (PBPs) remains unknown. In this study, LstiPBP1 and LstiPBP3 were cloned, expressed, and purified, and the fluorescence binding assay showed that LstiPBP1 binds to the major sex pheromone component, E-11-tetradecenol (E11-14:OH), with high affinity; moreover, E11-14:OH could evoke a significant antennal electrophysiological response and attract L. sticticalis males. After LstiPBP1 was silenced, both the antennal response and attractiveness of E11-14:OH decreased significantly. Molecular docking predicted that a hydrogen bonding site, Leu37, played key role in the binding of LstiPBP1 to E11-14:OH. After Leu37 was mutated, the E11-14:OH-binding affinity decreased drastically. These results suggest that LstiPBP1 participates in E11-14:OH recognition and could be used as a target gene to disturb the mating behavior of L. sticticalis and develop new odorants for pest control. |
| Databáze: | OpenAIRE |
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