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Antenna-Specific TabsOBP45 and TabsOBP46 Mediate Plant Volatile Recognition in Tuta absoluta (Lepidoptera: Gelechiidae)

文献类型： 外文期刊

作者： Liu, Qingyu 1 ; Wang, Liuyang 1 ; Liu, Panjing 2 ; Li, Lingrui 3 ; Ning, Jun 1 ; Zhang, Tao 2 ;

作者机构： 1.Chinese Acad Agr Sci, State Key Lab Biol Plant Dis & Insect Pests, Inst Plant Protect, Beijing 100193, Peoples R China

2.Minist Agr & Rural Affairs, China IPM Innovat Ctr Hebei Prov,Plant Protect Ins, Int Sci & Technol Joint Res Ctr IPM Hebei Prov, HAAFS Key Lab IPM Crops Northern Reg North China, Baoding 071000, Peoples R China

3.Plant Protect & Quarantine Gen Stn Hebei, Shijiazhuang 050035, Peoples R China

关键词： the tomato leaf miner; semiochemicals; fluorescence competitive binding; molecular docking; host volatile recognition

期刊名称：AGRONOMY-BASEL （ 影响因子：3.4； 五年影响因子：3.8 ）

ISSN：

年卷期： 2025 年 15 卷 7 期

页码：

收录情况： SCI

摘要： The tomato leaf miner, Tuta absoluta (Lepidoptera: Gelechiidae), is a destructive pest of Solanaceae crops worldwide. Its olfactory system plays an important role in locating mating partners and recognizing host plants. Understanding its olfactory recognition mechanism, particularly the function of odorant-binding proteins (OBPs), may reveal potential targets for pest management. In this study, we characterized two antenna-specific OBPs, TabsOBP45 and TabsOBP46, which were identified from the T. absoluta genome. Sequence analysis revealed that both TabsOBPs belong to the classic OBP subfamily, which is characterized by the presence of six conserved cysteine residues and an N-terminal signal peptide. Both TabsOBPs showed predominant antennal expression in quantitative real-time PCR (qRT-PCR) assays, suggesting their key roles in olfactory perception. Fluorescence competitive binding assays with a total of 63 tested volatiles revealed that 13 compounds exhibited strong binding affinities (Ki < 22 M) to TabsOBP45, with the highest binding affinity to beta-ionone, beta-caryophyllene, terpinolene, and cinnamaldehyde. Nine compounds showed strong binding affinities to TabsOBP46, with the strongest binding to 4-anisaldehyde, 4-methoxybenzaldehyde, cinnamaldehyde, and beta-ionone. Molecular docking analysis revealed the key residues involved in beta-ionone binding: TabsOBP45 interacted with ILE8, ALA9, PHE12, TRP37, ILE92, PHE94, THR115, and PHE118, while TabsOBP46 interacted with ILE8, PHE12, PHE36, TRP37, ILE92, LEU94, PHE118, and VAL134. These results provide new insights into the olfactory mechanism of T. absoluta and potential molecular targets for the development of olfactory-based pest control strategies.

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