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Identification and characterization of the bombykal receptor in the hawkmoth Manduca sexta

MPG-Autoren
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Wicher,  Dieter
Department of Evolutionary Neuroethology, Prof. B. S. Hansson, MPI for Chemical Ecology, Max Planck Society;

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Halty-deLeon,  Lorena
Department of Evolutionary Neuroethology, Prof. B. S. Hansson, MPI for Chemical Ecology, Max Planck Society;
IMPRS on Ecological Interactions, MPI for Chemical Ecology, Max Planck Society;

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Hansson,  Bill S.
Department of Evolutionary Neuroethology, Prof. B. S. Hansson, MPI for Chemical Ecology, Max Planck Society;

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Zitation

Wicher, D., Morinaga, S., Halty-deLeon, L., Funk, N., Hansson, B. S., Touhara, K., et al. (2017). Identification and characterization of the bombykal receptor in the hawkmoth Manduca sexta. The Journal of Experimental Biology, 220(10), 1781-1786. doi:10.1242/jeb.154260.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002C-E7AA-7
Zusammenfassung
Manduca sexta females attract their mates with the release of a species-specific sex-pheromone blend with bombykal (E,Z)-10,12-hexadcadienal and (E,E,Z)-10,12,14-hexadecatrienal being the two major components. Here, we searched for the hawkmoth bombykal receptor in heterologous expression systems. The putative pheromone receptor MsexOr1 co-expressed with MsexOrco in Xenopus oocytes elicited dose-dependent inward currents upon bombykal application (10 - 300 μM), and coexpressed in HEK293 and CHO cells caused bombykal-dependent rises in the intracellular free Ca2+ concentration. Also the bombykal receptor of Bombyx mori BmOr3 coexpressed with MsexOrco responded to bombykal (30 - 100 μM) with inward currents. In contrast, MsexOr4 coexpressed with MsexOrco neither responded to bombykal (30 - 100 μM) nor to the (E,E,Z)-10,12,14-hexadecatrienal mimic. Thus, MsexOr1, but probably not MsexOr4, and also not MsexOrco, is the bombykal-binding pheromone receptor in the hawkmoth. Finally, we obtained evidence that phospholipase C- and protein kinase C-activity is involved in the hawkmoth´s bombykal-receptor-mediated Ca2+ signals in HEK293 and CHO cells.