数字农科院2.0

Cloning, expression and binding specificity analysis of odorant binding protein 3 of the lucerne plant bug, Adelphocoris lineolatus (Goeze)

文献类型： 外文期刊

作者： Gu ShaoHua;Sun Yang;Ren LiYan;Zhang XueYing;Zhang YongJun;Wu KongMing;Guo YuYuan;Sun Yang;Ren LiYan

作者机构：

关键词： Adelphocoris lineolatus (Goeze);odorant binding protein;gene expression;Western blot;expression pattern;fluorescence competitive binding assays

期刊名称： CHINESE SCIENCE BULLETIN

ISSN： 1001-6538

年卷期： 2010 年 55 卷 34 期

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收录情况： SCI

摘要： Credible evidence shows that odorant binding proteins (OBPs) are required for insect olfaction perception and play a key role in transporting hydrophobic odorants across the sensillum lymph to the olfactory receptors (ORs). In the present study, a novel OBP (AlinOBP3) gene from the lucerne plant bug, Adelphocoris lineolatus, was cloned and expressed. The expression pattern of AlinOBP3 was evaluated by qPCR, which indicated that AlinOBP3 was dominantly expressed in antennae. The binding properties of AlinOBP3 with 9 cotton volatiles and 5 sex pheromone analogs were measured by fluorescence competitive binding assays with the fluorescence probe 1-NPN. The results revealed that of 9 cotton volatiles, Myrcene, beta-Ocimene and alpha-Phellandrene can bind with AlinOBP3. alpha-Phellandrene especially bound to AlinOBP3 with a high binding affinity, with a dissociation constant of 56.68 mu mol/L. Of the 5 sex pheromone analogs, Hexyl butyrate had the strongest binding affinity with AlinOBP3, with a dissociation constant as 59.53 mu mol/L. Butyl butyrate, trans-2-Hexenyl butyrate and Ethyl butyrate had medium binding affinities with AlinOBP3, with dissociation constants of 227.39, 108.77 and 143.47 mu mol/L, respectively. The results suggest that AlinOBP3 might be a pheromone binding protein (PBP) with a dual-function for the perception of sex pheromones and plant volatiles.

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