Odorant receptor structures predict the major female sex pheromone component in a moth
Abstract
BACKGROUND: Species isolation in insects can be ensured by prezygotic barriers, such as species-specific sex pheromone blends that mediate sexual attraction and mate recognition. Yet, sex pheromone compositions of many species remain poorly characterized outside important agricultural pests, because of the necessity to access live insects for pheromone extraction, the difficulties in identifying the production period, and the precise identification of behaviorally relevant compounds in extracts. RESULTS: Here, we use an odorant receptor (OR)-guided approach to identify the major female sex pheromone component of the previously unexplored lily moth, Spodoptera picta. Genome analysis identified S. picta orthologs of the pheromone receptors OR5 and OR75, previously characterized in S. litura and S. littoralis. Structural modeling of OR5 and OR75 combined with molecular docking predicted conserved ligand binding to (Z,E)-9,11-14:OAc, which was confirmed by functional assays on the ORs. Gas chromatography-mass spectrometry analyses of female pheromone gland extracts identified this compound as the major pheromone component, and electrophysiological and behavioral assays further demonstrated that it elicits antennal responses and is sufficient to attract males. CONCLUSIONS: Together, these results establish an innovative receptor structure-based strategy for pheromone identification in non-model species, provide insights into the sexual chemical ecology of S. picta, and clarify the evolutionary pathway by which a unique class of pheromone receptors emerged by gene duplication and gained specificity.
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BibTeX
@article{comte2026odorant,
title = {{Odorant receptor structures predict the major female sex pheromone component in a moth}},
author = {Arthur Comte and Zhiqiang Wei and Hui Li and Wen-Zhe Xing and Riccardo Moracci and Jin Zhang and Sébastien Fiorucci and Emmanuelle Jacquin-Joly},
journal = {BMC Biology},
year = {2026},
month = sep,
doi = {10.1186/s12915-026-02717-1},
url = {https://hal.inrae.fr/hal-05757722v1},
note = {CC BY},
}
RIS
TY - JOUR
TI - Odorant receptor structures predict the major female sex pheromone component in a moth
AU - Arthur Comte
AU - Zhiqiang Wei
AU - Hui Li
AU - Wen-Zhe Xing
AU - Riccardo Moracci
AU - Jin Zhang
AU - Sébastien Fiorucci
AU - Emmanuelle Jacquin-Joly
PY - 2026
DA - 2026/09/21
JO - BMC Biology
DO - 10.1186/s12915-026-02717-1
UR - https://hal.inrae.fr/hal-05757722v1
AB - BACKGROUND: Species isolation in insects can be ensured by prezygotic barriers, such as species-specific sex pheromone blends that mediate sexual attraction and mate recognition. Yet, sex pheromone compositions of many species remain poorly characterized outside important agricultural pests, because of the necessity to access live insects for pheromone extraction, the difficulties in identifying the production period, and the precise identification of behaviorally relevant compounds in extracts. RESULTS: Here, we use an odorant receptor (OR)-guided approach to identify the major female sex pheromone component of the previously unexplored lily moth, Spodoptera picta. Genome analysis identified S. picta orthologs of the pheromone receptors OR5 and OR75, previously characterized in S. litura and S. littoralis. Structural modeling of OR5 and OR75 combined with molecular docking predicted conserved ligand binding to (Z,E)-9,11-14:OAc, which was confirmed by functional assays on the ORs. Gas chromatography-mass spectrometry analyses of female pheromone gland extracts identified this compound as the major pheromone component, and electrophysiological and behavioral assays further demonstrated that it elicits antennal responses and is sufficient to attract males. CONCLUSIONS: Together, these results establish an innovative receptor structure-based strategy for pheromone identification in non-model species, provide insights into the sexual chemical ecology of S. picta, and clarify the evolutionary pathway by which a unique class of pheromone receptors emerged by gene duplication and gained specificity.
SN - 1741-7007
SN - 1741-7007
ER -