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Knockout of the delta11-desaturase SfruDES1 disrupts sex pheromone biosynthesis, mating and oviposition in the fall armyworm, Spodoptera frugiperda

文献类型： 外文期刊

作者： Shi L.;Liu X.;Liu H.;Shan S.;Shen S.;Bai M.;Lan H.;Khashaveh A.;Gu S.;Zhang Y.

作者机构：

关键词： CRISPR/Cas9;Desaturase;Fall armyworm;Mating behavior;Sex pheromone biosynthesis

期刊名称： Pesticide Biochemistry and Physiology

ISSN： 0048-3575

年卷期： 2024 年 200 卷

页码：

收录情况： SCIE（2024版）

摘要： Moth insects rely on sex pheromones for long distance attraction and searching for sex partners. The biosynthesis of moth sex pheromones involves the catalytic action of multiple enzymes, with desaturases playing a crucial role in the process of carbon chain desaturation. However, the specific desaturases involved in sex pheromone biosynthesis in fall armyworm (FAW), Spodoptera frugiperda, have not been clarified. In this study, a Δ11 desaturase (SfruDES1) gene in FAW was knocked out using the CRISPR/Cas9 genome editing system. A homozygous mutant of SfruDES1 was obtained through genetic crosses. The gas chromatography–mass spectrometry (GC–MS) analysis results showed that the three main sex pheromone components (Z7–12:Ac, Z9–14:Ac, and Z11–16:Ac) and the three minor components (Z9–14:Ald, E11–14:Ac and Z11–14:Ac) of FAW were not detected in homozygous mutant females compared to the wild type. Furthermore, behavioral assay demonstrated that the loss of SfruDES1 resulted in a significant reduction in the attractiveness of females to males, along with disruptions in mating behavior and oviposition. Additionally, in a heterologous expression system, recombinant SfruDES1 could introduce a cis double bond at the Δ11 position in palmitic acid, which resulted in the changes in components of the synthesized products. These findings suggest desaturase plays a key role in the biosynthesis of sex pheromones, and knockout of the SfruDES1 disrupts sex pheromone biosynthesis and mating behavior in FAW. The SfruDES1 could serve as tool to develop a control method for S. frugiperda. © 2024 Elsevier Inc.

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