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ORIGINAL ARTICLES

Structural basis of sex pheromone detection in aphids

Zhi Dong^1,† , Yidong Wang^1,† , Ying Tian^2,3,† , Zeyuan Guan¹ , Minghui Bai¹ , Bo Zhang^1,4 , Zhongqiang Jia^2,4 , Jinan Wu² , Song Cao⁵ , Zhou Gong⁶ , Xincheng Zhao³ , Weihua Ma¹ , Bing Wang^2,* , Guirong Wang^2,4,* , Ping Yin^1,*

¹National Key Laboratory of Crop Genetic Improvement, College of Bio-X, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan, Hubei, China
²State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China
³Henan International Joint Laboratory of Green Pest Control, College of Plant Protection, Henan Agricultural University, Zhengzhou, Henan, China
⁴Shenzhen Branch, Guangdong Laboratory for Lingnan Modern Agriculture, Synthetic Biology Laboratory of the Ministry of Agriculture and Rural Affairs, Agricultural Genomics Institute at Shenzhen, Chinese Academy of Agricultural Sciences, Shenzhen, Guangdong, China
⁵School of Life Sciences, Central China Normal University, Wuhan, Hubei, China
⁶Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan, Hubei, China
^†These authors contributed equally: Zhi Dong, Yidong Wang, Ying Tian
* Correspondence: Bing Wang(wangbing02@caas.cn)Guirong Wang(wangguirong@caas.cn)Ping Yin(yinping@mail.hzau.edu.cn)

Sex pheromones play a central role in regulating animal behavior and reproduction. In insects, these signals are perceived through specialized odorant receptors (ORs) that mediate species-specific communication and safeguard genetic integrity. However, the structural basis of sex pheromone detection remains largely unresolved. Here, we identified two ORs in the pea aphid Acyrthosiphon pisum, along with the conserved OR co-receptor (Orco), which together mediate recognition of the pheromone components nepetalactone and nepetalactol. Functional assays demonstrated that ApOR21–Orco and ApOR22–Orco specifically respond to nepetalactol and nepetalactone, respectively. Using cryo-electron microscopy, we resolved the structure of the ApOR22–Orco complex in three states — unbound closed, nepetalactone-bound closed, and nepetalactone-bound open — revealing a heterotetrameric ion channel formed by one ApOR22 and three ApOrco subunits. Ligand binding to ApOR22 triggers conformational rearrangements that induce asymmetric pore dilation, thereby enabling ion conduction. Together, these results provide a mechanistic framework for understanding sex pheromone perception in insects and establish a structural foundation for the rational development of environmentally sustainable pest-control strategies.

https://doi.org/10.1038/s41422-026-01267-z

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