Molecular Characterization and Key Binding Sites of Sex Pheromone-Binding Proteins from the Meadow Moth, Loxostege sticticalis
文献类型： 外文期刊
第一作者： Wen, Ming
作者： Wen, Ming;Chen, Qi;Zhou, Haifeng;Ren, Bingzhong;Wang, Yinliang;Wen, Ming;Chen, Qi;Zhou, Haifeng;Ren, Bingzhong;Wang, Yinliang;Li, Ertao;Li, Jinqiao;Zhang, Shuai;Li, Kebin;Yin, Jiao
作者机构：
关键词： L. sticticalis; LstiPBP1; sex pheromone; molecular docking; site-directed mutagenesis
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）
ISSN： 0021-8561
年卷期： 2019 年 67 卷 46 期
页码：
收录情况： SCI
摘要： 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.
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