Structural and Functional Characterization of European Corn Borer, Ostrinia nubilalis, Pheromone Binding Protein 3

Ostrinia nubilalis, a lepidopteran moth, also known as the European corn borer, has a major impact on the production of economically important crops in the United States and Europe. The female moth invites the male moth for mating through the release of pheromones, a volatile chemical signal. Pheromone binding proteins (PBPs) present in the male moth antennae are believed to pick up the pheromones, transport them across the aqueous sensillum lymph, and deliver them to the olfactory receptor neurons. Here we report for the first time the cloning, expression, refolding, purification, and structural characterization of Ostrinia nubilalis PBP3 (OnubPBP3). The recombinant protein showed nanomolar affinity to each isomer of the Ostrinia pheromones, E- and Z-11-tetradecenyl acetate. In a pH titration study by nuclear magnetic resonance, the protein exhibited an acid-induced unfolding at pH below 5.5. The molecular dynamics simulation study demonstrated ligand-induced conformational changes in the protein with both E- and Z-isomers of the Ostrinia pheromone. The simulation studies showed that while protein flexibility decreases upon binding to E-pheromone, it increases when bound to Z-pheromone. This finding suggests that the OnubPBP3 complex with E-pheromone is more stable than with Z-pheromone.

Automated summary

The lepidopteran moth Ostrinia nubilalis plays a significant role in impacting crop production in the US and Europe. The Pheromone binding proteins (PBPs) in male moth antennae are crucial in detecting and delivering pheromones for mating. The study on Ostrinia nubilalis PBP3 (OnubPBP3) revealed nanomolar affinity to pheromones, pH-induced unfolding behavior, and ligand-induced conformational changes, suggesting stability differences when bound to E- versus Z-isomers of the pheromone.