Predicted structure of odorant-binding protein 12 from Monochamus alternatus (Hope) suggests a mechanism of flexible odorant-binding

Odorant-binding proteins (OBPs) are thought to bind and deliver hydrophobic odorants from the environment to receptors on insect sensory neurons, and have been used to screen behaviorally active compounds of insects. In order to screen behaviorally active compounds for Monochamus alternatus by OBPs, we cloned full length of Obp12 coding sequence from M. alternatus and proved secretion property of MaltOBP12, then tested binding affinities of recombinant MaltOBP12 to 12 pine volatiles in vitro. We confirmed MaltOBP12 has binding affinities to 9 pine volatiles. The structure of MaltOBP12 and protein-ligand interactions were further analyzed by homology modeling, molecular docking, site-directed mutagenesis, and ligand-binding assays. These results demonstrated that the binding pocket of MaltOBP12 consists of several large aromatic and hydrophobic residues, and four aromatic residues (Tyr50, Phe109, Tyr112, Phe122) are essential for odorant-binding; ligands adopt extensive hydrophobic interactions with an overlapping subset of residues in the binding pocket. Finally, based on non-directional hydrophobic interactions, MaltOBP12 binds odorants flexibly. These findings will not only help us understand how OBPs flexibly bind odorants but also promote to screen of behaviourally active compounds by computer methods to prevent M. alternatus in the future.

Automated summary

This study discovered that MaltOBP12 has binding affinities to 9 pine volatiles and revealed the structure and protein-ligand interaction mechanism through modeling and molecular docking. These findings not only help us understand how odorant-binding proteins flexibly bind odorants, but also promote the screening of behaviorally active compounds through computer methods to prevent M. alternatus.