| Title: | Aphid Odorant-Binding Protein 9 Is Narrowly Tuned to Linear Alcohols and Aldehydes of Sixteen Carbon Atoms |
| Author(s): | D'Onofrio C; Knoll W; Pelosi P; |
| Address: | "Biosensor Technologies, AIT Austrian Institute of Technology GmbH, Konrad-Lorenz Strasse 24, 3430 Tulln, Austria. Department of Physics and Chemistry of Materials, Faculty of Medicine/Dental Medicine, Danube Private University, 3500 Krems, Austria" |
| ISSN/ISBN: | 2075-4450 (Print) 2075-4450 (Electronic) 2075-4450 (Linking) |
| Abstract: | "Aphid odorant-binding protein 9 is almost exclusively expressed in antennae and is well conserved between different aphid species. In order to investigate its function, we have expressed this protein and measured ligand-binding affinities to a number of common natural compounds. The best ligands are long-chain aldehydes and alcohols, in particular Z9-hexadecenal and Z11-hexadecenal, as well as 1-hexadecanol and Z11-1-hexadecenol. A model of this protein indicated Lys37 as the residue that is likely to establish strong interactions with the ligands, probably a Schiff base with aldehydes and a hydrogen bond with alcohols. Indeed, when we replaced this lysine with a leucine, the mutated protein lost its affinity to both long aldehydes and alcohols, while the binding of other volatiles was unaffected. Long-chain linear alcohols are common products of molds and have been reported as aphid antifeedants. Corresponding aldehydes, instead, are major components of sex pheromones for several species of Lepidoptera. We speculate that aphids might use OBP9 to avoid mold-contaminated plants as well as competition with lepidopteran larvae" |
| Keywords: | 1-hexadecanol aphids lepidopteran sex pheromones ligand-binding assays odorant-binding protein site-directed mutagenesis; |
| Notes: | "PubMed-not-MEDLINED'Onofrio, Chiara Knoll, Wolfgang Pelosi, Paolo eng Switzerland 2021/08/28 Insects. 2021 Aug 18; 12(8):741. doi: 10.3390/insects12080741" |
