<br>狂风草触角和跗节中富含的三种化学感应蛋白对杀虫剂的结合有不同的贡献,Pesticide Biochemistry and Physiology

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狂风草触角和跗节中富含的三种化学感应蛋白对杀虫剂的结合有不同的贡献
Pesticide Biochemistry and Physiology ( IF 4.2 ) Pub Date : 2024-01-19 , DOI: 10.1016/j.pestbp.2024.105797
Yu-Juan Yao ₁ , Ning-Na Yin ₁ , Lin-Mei Pu ₁ , An-Jing Yang ₁ , Nai-Yong Liu ₁

Affiliation

昆虫的触角和腿（主要是跗节）是接触各种有毒化学物质（包括杀虫剂）的最重要的感觉器官。在这两种组织中表达的结合蛋白是潜在的候选分子，可用作杀虫剂的结合和隔离，例如化学感应蛋白（CSP）。具有多种作用的昆虫 CSP 被认为参与杀虫剂抗性，主要针对飞蛾、蚜虫和蚊子。然而，天牛酸 CSP 和杀虫剂相互作用的分子基础仍未得到探索。在这里，我们展示了三种富含触角和跗节的 RhorCSP（RhorCSP1、CSP2 和 CSP3）与八种杀虫剂类别（总计 15 种化学物质）的结合特性。从该甲虫的转录组中，共发现了16个CSP编码基因，其中有7个全长序列。在系统发育中，这些RhorCSP分散分布在不同的进化枝中。表达谱揭示了、和在触角和跗节中的丰富表达，因此可以作为研究蛋白质与杀虫剂相互作用的代表。结合测定表明，三种 RhorCSP 对杀虫剂的调节存在差异，但与氟铃脲、毒死蜱和鱼藤酮表现出最高的亲和力（解离常数 <13 μM）。特别是，RhorCSP3 可以与 10 种测试的杀虫剂发生强烈相互作用，其中 4 个残基（Tyr25、Phe42、Val65 和 Phe68）分别对 6、4、3 和 4 个配体的结合有显着贡献。其中，与野生型蛋白相比，四种突变的 RhorCSP3 与植物杀虫剂鱼藤酮的结合显着减弱。此外，我们还证明 RhorCSP3 是一种广泛调节的载体蛋白，可响应杀虫剂以外的多种植物气味。总而言之，我们的研究结果揭示了三种 RhorCSP 的不同结合机制和气味调节特征，并鉴定了 RhorCSP3 与杀虫剂相互作用的关键残基。

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Three chemosensory proteins enriched in antennae and tarsi of Rhaphuma horsfieldi differentially contribute to the binding of insecticides

Antennae and legs (primarily the tarsal segments) of insects are the foremost sensory organs that contact a diverse range of toxic chemicals including insecticides. Binding proteins expressed in the two tissues are potential molecular candidates serving as the binding and sequestering of insecticides, like chemosensory proteins (CSPs). Insect CSPs endowed with multiple roles have been suggested to participate in insecticide resistance, focusing mainly on moths, aphids and mosquitos. Yet, the molecular underpinnings underlying the interactions of cerambycid CSPs and insecticides remain unexplored. Here, we present binding properties of three antenna- and tarsus-enriched RhorCSPs (RhorCSP1, CSP2 and CSP3) in to eight insecticide classes totaling 15 chemicals. From the transcriptome of this beetle, totally 16 CSP-coding genes were found, with seven full-length sequences. In phylogeny, these RhorCSPs were distributed dispersedly in different clades. Expression profiles revealed the abundant expression of , and in antennae and tarsi, thus as representatives for studying the protein-insecticide interactions. Binding assays showed that the three RhorCSPs were tuned differentially to insecticides but exhibited the highest affinities with hexaflumuron, chlorpyrifos and rotenone (dissociation constants <13 μM). In particular, RhorCSP3 could interact strongly with 10 of tested insecticides, of which four residues (Tyr25, Phe42, Val65 and Phe68) contributed significantly to the binding of six, four, three and four ligands, respectively. Of these, the binding of four mutated RhorCSP3s to a botanical insecticide rotenone was significantly weakened compared to the wildtype protein. Furthermore, we also evidenced that RhorCSP3 was a broadly-tuned carrier protein in response to a wide variety of plant odorants outside insecticides. Altogether, our findings shed light on different binding mechanisms and odorant-tuning profiles of three RhorCSPs in and identify key residues of the RhorCSP3-insecticide interactions.

更新日期：2024-01-19

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