Mohanty, SmitaRussell, Jennie LynnPaudel, PratikshyaCombs, PatrickJackson, Emily2024-04-252024-04-252024-04-16Russell, J. L., Paudel, P., Combs, P., Jackson, E., Mohanty, S. (2024, April 16). Pheromone binding to pest control: investigating olfaction mechanisms in Ostrinia furnacalis. Poster session presented at the Oklahoma State University Undergraduate Research Symposium, Stillwater, OK.https://hdl.handle.net/20.500.14446/344051Understanding the molecular intricacies of pheromone binding and release in insects is paramount for developing innovative and eco-friendly pest control strategies. Pheromones are hydrophobic and volatile chemicals that are secreted by female insects to attract the male insects for mating. Pheromone-binding proteins (PBPs) in the antennae of male insects serve a crucial role in transporting hydrophobic pheromone molecules to olfactory receptor neurons (ORN). This process enables male insects to locate a mate. Unraveling this mechanism opens the door to designing synthetic ligands that can compete with natural pheromones, confusing male pests and impeding their mating. Such an approach offers an effective pest mitigation strategy without the reliance on traditional pesticides.The invasive agricultural pest, Ostrinia furnacalis, inflicts substantial damage to crops globally. The highly sensitive olfactory system in male O. furnacalis moths depends on pheromone detection facilitated by PBP. However, the intricate details of pheromone recognition, binding, and release by O. furnacalis PBP2 (OfurPBP2) remain largely unexplored. The current study focuses on the production of recombinant OfurPBP2 and its mutants through bacterial expression, laying the groundwork for future in-depth mechanistic analyses.application/pdfIn the Oklahoma State University Library's institutional repository this paper is made available through the open access principles and the terms of agreement/consent between the author(s) and the publisher. The permission policy on the use, reproduction or distribution of the article falls under fair use for educational, scholarship, and research purposes. Contact Digital Resources and Discovery Services at lib-dls@okstate.edu or 405-744-9161 for further information.Posterpheromone binding proteinligand mimeticspesticide alternativebacterial transformationprotein structure