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« Previous Abstract"A herbivore-induced plant volatile of the host plant acts as a collective foraging signal to the larvae of the meadow moth, Loxostege sticticalis (Lepidoptera: Pyralidae)"    Next Abstract"Homogeneous and heterogeneous atmospheric ozonolysis of chlorobenzene:Mechanism, kinetics and ecotoxicity assessment" »

J Agric Food Chem


Title:"Molecular Characterization and Key Binding Sites of Sex Pheromone-Binding Proteins from the Meadow Moth, Loxostege sticticalis"
Author(s):Wen M; Li E; Li J; Chen Q; Zhou H; Zhang S; Li K; Ren B; Wang Y; Yin J;
Address:"Jilin Provincial Key Laboratory of Animal Resource Conservation and Utilization , Northeast Normal University , Changchun , Jilin 130024 , China. Key Laboratory of Vegetation Ecology, MOE , Northeast Normal University , Changchun 130024 , China. State Key Laboratory for Biology of Plant Diseases and Insect Pests , Institute of Plant Protection, Chinese Academy of Agricultural Sciences , Beijing 100193 , China"
Journal Title:J Agric Food Chem
Year:2019
Volume:20191108
Issue:46
Page Number:12685 - 12695
DOI: 10.1021/acs.jafc.9b03235
ISSN/ISBN:1520-5118 (Electronic) 0021-8561 (Linking)
Abstract:"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"
Keywords:Animals Binding Sites Carrier Proteins/*chemistry/genetics/metabolism Female Insect Proteins/*chemistry/genetics/metabolism Male Molecular Docking Simulation Moths/chemistry/genetics/*metabolism Sex Attractants/chemistry/*metabolism L.sticticalis LstiPBP;
Notes:"MedlineWen, Ming Li, Ertao Li, Jinqiao Chen, Qi Zhou, Haifeng Zhang, Shuai Li, Kebin Ren, Bingzhong Wang, Yinliang Yin, Jiao eng 2019/10/29 J Agric Food Chem. 2019 Nov 20; 67(46):12685-12695. doi: 10.1021/acs.jafc.9b03235. Epub 2019 Nov 8"

 
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Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
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