Key Residues Affecting Binding Affinity of Sirex noctilio Fabricius Odorant-Binding Protein (SnocOBP9) to Aggregation Pheromone

Sirex noctilio Fabricius (Hymenoptera Siricidae) is a major quarantine pest responsible for substantial economic losses in the pine industry. To achieve better pest control, (Z)-3-decen-ol was identified as the male pheromone and used as a field chemical trapping agent. However, the interactions bet...

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Bibliographic Details
Published in:International journal of molecular sciences 2022-08, Vol.23 (15), p.8456
Main Authors: Hao, Enhua, Li, Yini, Guo, Bing, Yang, Xi, Lu, Pengfei, Qiao, Haili
Format: Article
Language:English
Subjects:
Affinity
Aggregation pheromone
Alanine
Amino acids
Behavior
computational simulation
Computer applications
Economic impact
Experiments
Females
fluorescence binding assay
Hydrophobicity
Insects
Ligands
Molecular dynamics
Mutation
Odorant-binding protein
odorant-binding proteins
Peptides
Pest control
Pheromone traps
Pheromones
Proteins
Residues
Sirex noctilio
Site-directed mutagenesis
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Summary:Sirex noctilio Fabricius (Hymenoptera Siricidae) is a major quarantine pest responsible for substantial economic losses in the pine industry. To achieve better pest control, (Z)-3-decen-ol was identified as the male pheromone and used as a field chemical trapping agent. However, the interactions between odorant-binding proteins (OBPs) and pheromones are poorly described. In this study, SnocOBP9 had a higher binding affinity with Z3D (Ki = 1.53 ± 0.09 μM) than other chemical ligands. Molecular dynamics simulation and binding mode analysis revealed that several nonpolar residues were the main drivers for hydrophobic interactions between SnocOBP9 and Z3D. Additionally, computational alanine scanning results indicated that five amino acids (MET54, PHE57, PHE71, PHE74, LEU116) in SnocOBP9 could potentially alter the binding affinity to Z3D. Finally, we used single-site-directed mutagenesis to substitute these five residues with alanine. These results imply that the five residues play crucial roles in the SnocOBP9-Z3D complex. Our research confirmed the function of SnocOBP9, uncovered the key residues involved in SnocOBP9-Z3D interactions, and provides an inspiration to improve the effects of pheromone agent traps.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms23158456