The Odorant Binding Protein 6 Expressed in Sensilla Chaetica Displays Preferential Binding Affinity to Host Plants Volatiles in Ectropis obliqua

文献类型： 外文期刊

第一作者： Li, Zhaoqun

作者： Li, Zhaoqun;Cai, Xiaoming;Luo, Zongxiu;Chen, Zongmao;Zhang, Wanna;Zhang, Yongjun

作者机构：

关键词： Ectropis obliqua; odorant-binding protein; immunolocalization; sensilla chaetica; fluorescence competition assay

期刊名称：FRONTIERS IN PHYSIOLOGY （ 影响因子：4.566； 五年影响因子：4.804 ）

ISSN： 1664-042X

年卷期： 2018 年 9 卷

页码：

收录情况： SCI

摘要： The monophagous tea geometrid Ectropis obliqua selectively feed on tea plants, requiring the specialized chemosensory system to forage for certain host. A deep insight into the molecular basis would accelerate the design of insect-behavior-modifying stimuli. In the present study, we focused on the odorant-binding protein 6 (EoblOBP6) with the high abundance in legs transcriptome of E. obliqua moths. qRT-PCR coupled with western blot analyses revealed the dual expression pattern of EoblOBP6 in antennae and legs. Cellular Immunolocalization indicated that EoblOBP6 was predominantly labeled in the outer sensillum lymph of uniporous sensilla chaetica, which is not innervated by sensory neurons. No specific staining was observed in other sensillum types. The fluorescence competition assay showed a relatively narrow binding spectrum of recombinant EoblOBP6. EoblOBP6 could not only bind with intact tea plant volatiles benzaldehyde but also display high binding ability to nerolidol and alpha-farnesene which are tea plant volatiles dramatically induced by herbivore infestation. Besides, EoblOBP6 tightly bound to the aversive bitter alkaloid berberine. Taken together, EoblOBP6 displayed an unusual expression in sensilla chaetica, exhibited the potential involvement in olfaction and gustation, and may play a functional role in host location of female E. obliqua moths.

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