Functional differentiation of three pheromone binding proteins in Orthaga achatina using mixed-type sex pheromones
Functional differentiation of three pheromone binding proteins in Orthaga achatina using mixed-type sex pheromones
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DOI：
10.1016/j.pestbp.2022.105097
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发表时间：
2022-06-14
影响因子：
4.7
通讯作者：
Yan, Qi
中科院分区：
文献类型：
--
作者：
Si, Yu-Xiao;Guo, Jin-Meng;Yan, Qi
信息素结合蛋白（PBP）在昆虫性信息素的感知中发挥着重要作用，其功能是识别信息素成分并将其转运到气味感知神经元的嗅觉受体上。 Orthaga achatina 是樟树的一种严重害虫，其性通讯使用三种 I 型（Z11-16:OAc、Z11-16:OH 和 Z11-16:Ald）和一种 II 型（Z3、Z6、Z9、Z12、Z15-23:H）性信息素成分的混合物，其中 Z11-16:OAc 为主要成分，其他成分为次要成分。在这项研究中，我们首次证明了使用混合型性信息素的蛾中三种PBP在信息素成分的识别上存在差异。首先，组织表达研究表明，O. achatina 的所有三种 PBP 均仅在触角中表达，并且高度男性化，表明它们参与了性信息素的感知。其次，这三种PBP在大肠杆菌中表达，并通过荧光竞争结合测定测定了PBP与四种性信息素成分和一些信息素类似物的结合亲和力。结果表明，OachPBP1对所有四种性信息素成分均具有高结合亲和力，而OachPBP2仅对三种I型成分具有高或中度结合亲和力，OachPBP3仅对三种次要信息素成分具有高结合亲和力。此外，通过 3D 结构建模和配体分子对接，在三个 PBP 中鉴定了与性信息素成分结合的关键氨基酸残基，预测了 PBP 与信息素成分之间的相互作用。我们的研究为使用混合型性信息素的飞蛾的嗅觉机制提供了基本的见解。
Pheromone-binding proteins (PBPs) play important roles in perception of insect sex pheromones, functioning to recognize and transport pheromone components onto the olfactory receptors of the odorant sensing neurons. Orthaga achatina, a serious pest of camphor trees, uses a mixture of three Type I (Z11-16:OAc, Z11-16:OH and Z11-16:Ald) and one Type II (Z3,Z6,Z9,Z12,Z15-23:H) sex pheromone components in its sex communication, in which Z11-16:OAc is the major component and others are minor components. In this study, we for the first time demonstrated that the three PBPs differentiated in recognition among pheromone components in a moth using mixed-type sex pheromones. First, tissue expression study showed that all three PBPs of O. achatina were expressed only in antennae and highly male-biased, suggesting their involvement in perception of the sex pheromones. Second, the three PBPs were expressed in Escherichia coli and the binding affinities of PBPs to four sex pheromone components and some pheromone analogs were determined by the fluorescence competition binding assays. The results showed that OachPBP1 bound all four sex pheromone components with high binding affinity, while OachPBP2 had high or moderate binding affinity only to three Type I components, and OachPBP3 had high binding affinity only to three minor pheromone components. Furthermore, key amino acid residues that bind to sex pheromone components were identified in three PBPs by 3-D structure modeling and ligand mo-lecular docking, predicting the interactions between PBPs and pheromone components. Our study provides a fundamental insight into the olfactory mechanism in moths that use mixed-type sex pheromones.