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Key site residues of pheromone-binding protein 1 involved in interacting with sex pheromone components of Helicoverpa armigera.
- Source :
-
Scientific reports [Sci Rep] 2017 Dec 04; Vol. 7 (1), pp. 16859. Date of Electronic Publication: 2017 Dec 04. - Publication Year :
- 2017
-
Abstract
- Pheromone binding proteins (PBPs) are widely distributed in insect antennae, and play important roles in the perception of sex pheromones. However, the detail mechanism of interaction between PBPs and odorants remains in a black box. Here, a predicted 3D structure of PBP1 of the serious agricultural pest, Helicoverpa armigera (HarmPBP1) was constructed, and the key residues that contribute to binding with the major sex pheromone components of this pest, (Z)-11- hexadecenal (Z11-16:Ald) and (Z)-9- hexadecenal (Z9-16:Ald), were predicted by molecular docking. The results of molecular simulation suggest that hydrophobic interactions are the main linkage between HarmPBP1 and the two aldehydes, and four residues in the binding pocket (Phe12, Phe36, Trp37, and Phe119) may participate in binding with these two ligands. Then site-directed mutagenesis and fluorescence binding assays were performed, and significant decrease of the binding ability to both Z11-16:Ald and Z9-16:Ald was observed in three mutants of HarmPBP1 (F12A, W37A, and F119A). These results revealed that Phe12, Trp37, and Phe119 are the key residues of HarmPBP1 in binding with the Z11-16:Ald and Z9-16:Ald. This study provides new insights into the interactions between pheromone and PBP, and may serve as a foundation for better understanding of the pheromone recognition in moths.
- Subjects :
- Aldehydes chemistry
Aldehydes metabolism
Amino Acid Sequence
Animals
Binding Sites
Insect Proteins chemistry
Insect Proteins genetics
Molecular Docking Simulation
Mutagenesis, Site-Directed
Protein Binding
Protein Structure, Tertiary
Recombinant Proteins biosynthesis
Recombinant Proteins chemistry
Recombinant Proteins isolation & purification
Sequence Alignment
Sex Attractants chemistry
Insect Proteins metabolism
Moths metabolism
Sex Attractants metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 7
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 29203785
- Full Text :
- https://doi.org/10.1038/s41598-017-17050-5