Identification and functional characterization of a sex pheromone receptor in the silkmoth Bombyx mori

被引:317
|
作者
Sakurai, T
Nakagawa, T
Mitsuno, H
Mori, H
Endo, Y
Tanoue, S
Yasukochi, Y
Touhara, K [1 ]
Nishioka, T
机构
[1] Univ Tokyo, Grad Sch Frontier Sci, Dept Integrated Biosci, Chiba 2778562, Japan
[2] Kyoto Univ, Grad Sch Agr, Div Appl Biosci, Kyoto 6068502, Japan
[3] Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Kyoto 6068502, Japan
[4] Japan Sci & Technol Agcy, Core Res Evolut Sci & Technol, Tokyo 1350064, Japan
[5] Kyoto Inst Technol, Dept Appl Biol, Sakyo Ku, Kyoto 6068585, Japan
[6] Natl Inst Agrobiol Sci, Tsukuba, Ibaraki 3058634, Japan
关键词
baculovirus; bombykal; bombykol; olfactory receptor; Xenopus laevis oocyte;
D O I
10.1073/pnas.0407596101
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Sex pheromones released by female moths are detected with high specificity and sensitivity in the olfactory sensilla of antennae of conspecific males. Bombykol in the silkmoth Bombyx mori was the first sex pheromone to be identified. Here we identify a male-specific G protein-coupled olfactory receptor gene, B. mori olfactory receptor 1 (BmOR-1), that appears to encode a bombykol receptor. The BmOR-1 gene is located on the Z sex chromosome, has an eight-exon/seven-intron structure, and exhibits male-specific expression in the pheromone receptor neurons of male moth antenna during late pupal and adult stages. Bombykol stimulation of Xenopus laevis oocytes expressing BmOR-1 and BmGalphaq elicited robust dose-dependent inward currents on two-electrode voltage clamp recordings, demonstrating that the binding of bombykol to BmOR-1 leads to the activation of a BmGalphaq-mediated signaling cascade. Antennae of female moths infected with BmOR-1-recombinant baculovirus showed electrophysiological responses to bombykol but not to bombykal. These results provide evidence that BmOR-1 is a G protein-coupled sex pheromone receptor that recognizes bombykol.
引用
收藏
页码:16653 / 16658
页数:6
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