Loss of Binding Capabilities in an Ecologically Important Odorant Receptor of the Fall Armyworm, Spodoptera frugiperda, by a Single Point Mutation

J Agric Food Chem. 2023 Sep 6;71(35):13003-13013. doi: 10.1021/acs.jafc.3c04247. Epub 2023 Aug 25.

Abstract

Olfaction plays a crucial role in locating food sources, mates, and spawning sites in the fall armyworm (FAW), Spodoptera frugiperda (Lepidoptera: Noctuidae). In the current study, SfruOR14, a highly conserved odorant receptor (OR) in lepidopteran species, was newly uncovered in S. frugiperda. In two-electrode voltage clamp recordings, the SfruOR14/Orco complex was narrowly tuned to six volatile compounds including phenylacetaldehyde (PAA), benzaldehyde, heptaldehyde, (E)-2-hexen-1-al, cinnamaldehyde, and 2-phenylethanol, among which PAA showed the strongest binding affinity. Subsequent homology modeling and molecular docking revealed that Phe79, His83, Tyr149, Pro176, Gln177, Leu202, and Thr348 in SfruOR14 were the key binding residues against the six ligands. Finally, as a result of site-directed mutagenesis, the SfruOR14His83Ala mutant completely lost its binding capabilities toward all ligands. Taken together, our findings provide valuable insights into understanding the interaction between SfruOR14 and the chemical ligands including PAA, which can help to design novel olfactory modulators for pest control.

Keywords: evolution and conservation; key binding residues; ligand compounds; odorant receptors; site-directed mutagenesis.

MeSH terms

  • Animals
  • Ligands
  • Molecular Docking Simulation
  • Point Mutation*
  • Receptors, Odorant*
  • Spodoptera

Substances

  • Ligands
  • Receptors, Odorant
  • phenylacetaldehyde