A conserved pheromone receptor in the American and the Asian palm weevils is also activated by host plant volatiles

• Published in: Current research in insect science Vol. 6; p. 100090
• Main Authors: Brajon, Ludvine, Comte, Arthur, Capoduro, Rémi, Meslin, Camille, Antony, Binu, Al-Saleh, Mohammed Ali, Pain, Arnab, Jacquin-Joly, Emmanuelle, Montagné, Nicolas
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01-01-2024; Elsevier
• Subjects: 3D structure modelling; Aggregation pheromone; Life Sciences; Odorant receptors; Palm tree volatiles; Aggregation pheromone; Palm tree volatiles; 3D structure modelling; Odorant receptors
• ISSN: 2666-5158; 2666-5158
• DOI: 10.1016/j.cris.2024.100090

•An odorant receptor from the American palm weevil detects aggregation pheromones of other species.•The response spectrum of this odorant receptor is highly conserved in the American and the Asian palm weevils.•In both species, this receptor is broadly tuned and is also activated by host plant volatiles.
The evolution of chemosensory receptors is key for the adaptation of animals to their environment. Recent knowledge acquired on the tri-dimensional structure of insect odorant receptors makes it possible to study the link between modifications in the receptor structure and evolution of response spectra in more depth. We investigated this question in palm weevils, several species of which are well-known invasive pests of ornamental or cultivated palm trees worldwide. These insects use aggregation pheromones to gather on their host plants for feeding and reproduction. An odorant receptor detecting the aggregation pheromone components was characterised in the Asian palm weevil Rhynchophorus ferrugineus. This study compared the response spectra of this receptor, RferOR1, and its ortholog in the American palm weevil R. palmarum, RpalOR1. Sequences of these two receptors exhibit more than 70 amino acid differences, but modelling of their 3D structures revealed that their putative binding pockets differ by only three amino acids, suggesting possible tuning conservation. Further functional characterization of RpalOR1 confirmed this hypothesis, as RpalOR1 and RferOR1 exhibited highly similar responses to coleopteran aggregation pheromones and chemically related molecules. Notably, we showed that R. ferrugineus pheromone compounds strongly activated RpalOR1, but we did not evidence any response to the R. palmarum pheromone compound rhynchophorol. Moreover, we discovered that several host plant volatiles also activated both pheromone receptors, although with lower sensitivity. This study not only reveals evolutionary conservation of odorant receptor tuning across the two palm weevil species, but also questions the specificity of pheromone detection usually observed in insects.