A Pheromone-binding protein mediates the bombykol-induced activation of a pheromone receptor in vitro

Institute of Physiology (230), University of Hohenheim, Garbenstrasse 30, 70599 Stuttgart, Germany.
Chemical Senses (Impact Factor: 3.16). 08/2006; 31(6):547-55. DOI: 10.1093/chemse/bjj059
Source: PubMed


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-1-expressing 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.

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    • "Both protein classes reversibly bind small ligands with dissociation constants in the micromolar range (Pelosi et al. 2006). OBPs are likely involved in chemosensory perception, participating in the solubilization and transfer of odorants through the sensillum lymph (Vogt et al. 1991; Pelosi 1994; Prestwich et al. 1995; Pophof 2004; Tsuchihara et al. 2005; Grosse-Wilde et al. 2006). Additionally, they are supposed to contribute to the sensitivity of the olfactory system (Gomez-Diaz et al. 2013) and could protect odors from enzymatic degradation (Chertemps et al. 2012; Gomez-Diaz et al. 2013). "
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    • "Based on the fact that MsexOR-4 is the OR with the highest expression level, we conclude that it is likely the bombykal receptor. The B. mori bomkykal receptor, BmorOR-3 (Grosse-Wilde et al., 2006; Nakagawa et al., 2005), is orthologous to MsexOR-1 (Fig. 1), and the putative bombykal receptor, MsexOR- 4, is orthologous to the B. mori bombykol receptor, BmorOR-1 (Grosse-Wilde et al., 2006; Nakagawa et al., 2005). Thus, it would seem likely for the orthologous genes MsexOR-4 and BmorOR-1 to detect the major compound of the pheromone blend. "
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    • "These six cysteines form three disulfide bridges, which play important roles in maintaining the protein tertiary structure. Experimental evidence has demonstrated that OBPs could selectively bind odorants or pheromones (Vogt and Riddiford, 1981; Plettner et al., 2000; Pophof, 2004; Grosse-Wilde et al., 2006; Syed et al., 2006; Gong et al., 2009b; Zhou et al., 2009). "
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