Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/34508
Title: Degradation of pheromone and plant volatile components by a same Odorant-Degrading Enzyme in the cotton leafworm, Spodoptera littoralis
Author: Durand, Nicolas
Carot-Sans, Gerard
Bozzolan, Françoise
Rosell Pellisé, Glòria
Siaussat, David
Debernard, Stéphane
Chertemps, Thomas
Maïbèche-Coisne, Martine
Keywords: Olors
Feromones
Enzims
Metabolisme de les plantes
Lepidòpters
Compostos orgànics volàtils
Esterases
Odors
Pheromones
Enzymes
Plant metabolism
Lepidoptera
Volatile organic compounds
Esterases
Issue Date: 27-Dec-2011
Publisher: Public Library of Science (PLoS)
Abstract: Background: Odorant-Degrading Enzymes (ODEs) are supposed to be involved in the signal inactivation step within the olfactory sensilla of insects by quickly removing odorant molecules from the vicinity of the olfactory receptors. Only three ODEs have been both identified at the molecular level and functionally characterized: two were specialized in the degradation of pheromone compounds and the last one was shown to degrade a plant odorant. Methodology: Previous work has shown that the antennae of the cotton leafworm Spodoptera littoralis , a worldwide pest of agricultural crops, express numerous candidate ODEs. We focused on an esterase overexpressed in males antennae, namely SlCXE7. We studied its expression patterns and tested its catalytic properties towards three odorants, i.e. the two female sex pheromone components and a green leaf volatile emitted by host plants. Conclusion: SlCXE7 expression was concomitant during development with male responsiveness to odorants and during adult scotophase with the period of male most active sexual behaviour. Furthermore, SlCXE7 transcription could be induced by male exposure to the main pheromone component, suggesting a role of Pheromone-Degrading Enzyme. Interestingly, recombinant SlCXE7 was able to efficiently hydrolyze the pheromone compounds but also the plant volatile, with a higher affinity for the pheromone than for the plant compound. In male antennae, SlCXE7 expression was associated with both long and short sensilla, tuned to sex pheromones or plant odours, respectively. Our results thus suggested that a same ODE could have a dual function depending of it sensillar localisation. Within the pheromone-sensitive sensilla, SlCXE7 may play a role in pheromone signal termination and in reduction of odorant background noise, whereas it could be involved in plant odorant inactivation within the short sensilla.
Note: Reproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0029147
It is part of: PLoS One, 2011, vol. 6, num. 12, p. e29147
Related resource: http://dx.doi.org/10.1371/journal.pone.0029147
URI: http://hdl.handle.net/2445/34508
ISSN: 1932-6203
Appears in Collections:Articles publicats en revistes (Farmacologia, Toxicologia i Química Terapèutica)

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