| Title: | Two single-point mutations shift the ligand selectivity of a pheromone receptor between two closely related moth species |
| Author(s): | Yang K; Huang LQ; Ning C; Wang CZ; |
| Address: | "State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing, China. College of Life Sciences, University of Chinese Academy of Sciences, Beijing, China" |
| ISSN/ISBN: | 2050-084X (Electronic) 2050-084X (Linking) |
| Abstract: | "Male moths possess highly sensitive and selective olfactory systems that detect sex pheromones produced by their females. Pheromone receptors (PRs) play a key role in this process. The PR HassOr14b is found to be tuned to (Z)-9-hexadecenal, the major sex-pheromone component, in Helicoverpa assulta. HassOr14b is co-localized with HassOr6 or HassOr16 in two olfactory sensory neurons within the same sensilla. As HarmOr14b, the ortholog of HassOr14b in the closely related species Helicoverpa armigera, is tuned to another chemical (Z)-9-tetradecenal, we study the amino acid residues that determine their ligand selectivity. Two amino acids located in the transmembrane domains F232I and T355I together determine the functional difference between the two orthologs. We conclude that species-specific changes in the tuning specificity of the PRs in the two Helicoverpa moth species could be achieved with just a few amino acid substitutions, which provides new insights into the evolution of closely related moth species" |
| Keywords: | "Aldehydes/*metabolism Animals Ligands Moths/*genetics/*metabolism Mutant Proteins/genetics/metabolism *Point Mutation Protein Binding Receptors, Pheromone/*genetics/*metabolism Helicoverpa assulta Xenopus oocyte function neuroscience pheromone receptor si;" |
| Notes: | "MedlineYang, Ke Huang, Ling-Qiao Ning, Chao Wang, Chen-Zhu eng Research Support, Non-U.S. Gov't England 2017/10/25 Elife. 2017 Oct 24; 6:e29100. doi: 10.7554/eLife.29100" |
