Glutathione S-Transferase Highly Expressed in Holotrichia parallela Antennae Inactivates the Odorant Unsaturated Aldehyde Volatiles

J Agric Food Chem. 2023 Jun 14;71(23):8797-8807. doi: 10.1021/acs.jafc.3c00915. Epub 2023 May 31.

Abstract

Odorant-degrading enzymes in insects play a vital role in maintaining olfactory sensitivity. However, the role and molecular mechanism of glutathione S-transferases (GSTs) in odorant inactivation has been rarely studied. In the present study, 31 GSTs were identified from the antennal transcriptome of Holotrichia parallela. HpGSTd1 possesses the highest transcriptome expression level. Recombinant HpGSTd1 showed degradation activity toward various unsaturated aldehyde volatiles. Furthermore, the metabolite of cinnamaldehyde was identified by high-resolution mass spectrometry (HRMS). The molecular docking analysis and site-directed mutagenesis revealed the key residues of HpGSTd1 in degrading odorants. In addition, the unsaturated aldehyde volatiles elicited the behavioral and electrophysiological responses of H. parallela. Taken together, our findings suggest that HpGSTd1 may play an essential role in inactivating odorants in H. parallela, which provides new insights for identifying molecular targets and exploring effective olfactory regulators for this underground pest.

Keywords: Holotrichia parallela; glutathione S-transferases; odorant degradation enzymes; semiochemicals.

MeSH terms

  • Aldehydes / metabolism
  • Animals
  • Arthropod Antennae / metabolism
  • Coleoptera* / metabolism
  • Glutathione Transferase / genetics
  • Glutathione Transferase / metabolism
  • Insect Proteins / metabolism
  • Molecular Docking Simulation
  • Odorants
  • Receptors, Odorant* / genetics
  • Receptors, Odorant* / metabolism

Substances

  • Glutathione Transferase
  • Aldehydes
  • Insect Proteins
  • Receptors, Odorant