Pea aphid odorant-binding protein ApisOBP6 discriminates between aphid sex pheromone components, aphid alarm pheromone and a host plant volatile

被引:6
作者
Sims, Cassie [1 ,2 ]
Birkett, Michael A. [1 ]
Oldham, Neil J. [2 ]
Stockman, Robert A. [2 ]
Withall, David M. [1 ]
机构
[1] Protecting Crops & Environm, Rothamsted Res, Harpenden AL5 2JQ, Hertfordshire, England
[2] Univ Nottingham, Sch Chem, Univ Pk, Nottingham NG7 2RD, Nottinghamshire, England
基金
英国生物技术与生命科学研究理事会;
关键词
Insect olfaction; Pheromones; Odorant-binding protein; Aphids; Protein NMR; Molecular docking; TRANSFER-DIFFERENCE NMR; LIGAND; STEREOCHEMISTRY; RECEPTORS; DOCKING;
D O I
10.1016/j.ibmb.2023.104026
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Olfactory perception of pheromones in insects involves odorant-binding proteins (OBPs), relatively small proteins (ca.110-240 amino acid residues) that can bind reversibly to behaviourally active olfactory ligands. In this study, we investigated the binding in silico and in vitro of the aphid sex pheromone components (1R,4aS,7S,7aR)nepetalactol and (4aS,7S,7aR)-nepetalactone and the aphid alarm pheromone (E)-beta-farnesene by OBPs from the pea aphid, Acyrthosiphon pisum. Screening of protein models of ApisOBPs1-11 with the aphid sex pheromone components suggested that ApisOPB6 was a candidate. Fluorescence assays using ApisOBP6 suggested that ApisOBP6 was able to bind both sex pheromone components and discriminate from the aphid alarm pheromone and the generic plant compound (R/S)-linalool. Saturation transfer difference NMR experiments with ApisOBP6 yielded results consistent to those from the fluorescence experiments, with a clear interaction between ApisOBP6 and (4aS,7S,7aR)-nepetalactone. These results describe a novel interaction and potential function for ApisOBP6, point to pre-receptor odorant discrimination by OBPs, and provide a platform for investigating the function of other aphid olfactory proteins involved in aphid chemical ecology.
引用
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页数:7
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