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Binding Properties of Chemosensory Protein 1 to Plant Volatiles Guiding Nicotiana rustica Recognition in Helicoverpa armigera

文献类型： 外文期刊

作者： Sun, Ya-Lan 1 ; Sun, Ya-Hui 1 ; Wang, Ke 2 ; Xu, Pengjun 3 ; Dong, Jun-Feng 1 ;

作者机构： 1.Henan Univ Sci & Technol, Coll Hort & Plant Protect, Luoyang 471000, Peoples R China

2.Chinese Acad Agr Sci, Inst Vegetables & Flowers, Dept Plant Protect, Beijing 100081, Peoples R China

3.Chinese Acad Agr Sci, Inst Tobacco Res, Key Lab Tobacco Pest Monitoring Controlling & Inte, Qingdao 266101, Peoples R China

关键词： Helicoverpa armigera; chemosensory protein; Nicotiana rustica; oviposition test; fluorescencebinding assay

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.2； 五年影响因子：6.4 ）

ISSN： 0021-8561

年卷期： 2025 年 73 卷 11 期

页码：

收录情况： SCI

摘要： Helicoverpa armigera is one of the most serious pests attacking tobacco around the world. Nicotiana rustica is widely used as a trap crop in the fields of Nicotiana tabacum in China. However, the chemical and molecular bases guiding N. rustica recognition in H. armigera are still unknown. In this study, we found 15 volatiles emitted from N. rustica induced EAG responses of H. armigera, while beta-ocimene, alpha-pinene, and linalool were attractive to the moths in Y-tubes. Oviposition tests showed that H. armigera prefers to lay eggs on tobacco plants treated with beta-ocimene and alpha-pinene. Further assays showed that an antenna-enriched chemosensory protein, HarmCSP1, binds robustly with beta-ocimene, benzaldehyde, and (Z)-3-hexenyl acetate. Structural analyses revealed that several key amino acid residues are involved in ligand binding. This study increases the understanding of the chemosensory mechanism of H. armigera's recognition of N. rustica and provides the foundation for the design of attractants for H. armigera management.

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