کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2840533 | 1165330 | 2012 | 8 صفحه PDF | دانلود رایگان |
Three pheromone-binding proteins of Helicoverpa armigera were cloned and expressed in Escherichia coli. In order to characterize their physiological properties, ligand-binding experiments were performed using five biologically relevant substances including sex pheromones and interspecific signals. The results showed that one of the pheromone-binding proteins, HarmPBP1, binds strongly to each of the two principal pheromone components of H. armigera, (Z)-11-tetradecenal and (Z)-9-hexadecenal, but not to the interspecific signal (Z)-9-tetracecenal. The two remaining pheromone-binding proteins, HarmPBP2 and HarmPBP3, showed only weak affinities with the ligands tested. The 3-D structure of HarmPBP1 was predicted and the docking experiments indicate that the key binding site of (Z)-9-hexadecenal to HarmPBP1 includes Thr112, Lys111, and Phe119 whereas that of (Z)-11-tetradecenal includes Ser9, Trp37, Phe36, and Phe119.
Pheromone binding proteins of Helicoverpa armigera were binding with two sex pheromone components (Z) 11-tetradecenal and (Z) 9-hexadecenal, and some interspecific signals.Figure optionsDownload as PowerPoint slideHighlights
► We get three PBPs from the cDNA library of the antennae of Helicoverpa armigera.
► Analyzed the three PBP genes with other Lepidoptera.
► Expressed the three PBPs in E. coli and purified them.
► Tested five sex pheromones with each PBP by binding experiment.
Journal: Journal of Insect Physiology - Volume 58, Issue 7, July 2012, Pages 941–948