Chemical Senses Advance Access originally published online on May 5, 2006
Chemical Senses 2006 31(6):547-555; doi:10.1093/chemse/bjj059
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A Pheromone-Binding Protein Mediates the Bombykol-Induced Activation of a Pheromone Receptor In Vitro
Svato
21 Institute of Physiology (230), University of Hohenheim, Garbenstrasse 30, 70599 Stuttgart, Germany 2 Research Group Mass Spectroscopy, Max-Planck-Institute for Chemical Ecology, Hans-Knöll-Street 8, 07745 Jena, Germany
Correspondence to be sent to: Jürgen Krieger, Institute of Physiology (230), University of Hohenheim, Garbenstrasse 30, 70599 Stuttgart, Germany. e-mail: krieger{at}uni-hohenheim.de
The enormous capacity of the male silkmoth Bombyx mori in recognizing and discriminating bombykol and bombykal is based on distinct sensory neurons in the antennal sensilla hairs. The hydrophobic pheromonal compounds are supposed to be ferried by soluble pheromone-binding proteins (PBPs) through the sensillum lymph toward the receptors in the dendritic membrane. We have generated stable cell lines expressing the candidate pheromone receptors of B. mori, BmOR-1 or BmOR-3, and assessed their responses to hydrophobic pheromone compounds dissolved by means of dimethyl sulfoxide. BmOR-1expressing cells were activated by bombykol but also responded to bombykal, whereas cells expressing BmOR-3 responded to bombykal only. In experiments employing the B. mori PBP, no organic solvent was necessary to mediate an activation of BmOR-1 by bombykol, indicating that the PBP solubilizes the hydrophobic compound. Furthermore, the employed PBP selectively mediated a response to bombykol but not to bombykal, supporting a ligand specificity of PBPs. This study provides evidence that both distinct pheromone receptors and PBPs play an important role in insect pheromone recognition.
Key words: Bombyx mori, expression, olfaction, pheromone detection, receptor
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