Expression, Affinity, and Functional Characterization of the Specific Binding of Two Putative Pheromone-Binding Proteins in the Omnivorous German Cockroach .

The German cockroach (L.) is an important pest in medical, veterinary, and public health. Studies on the olfaction mechanism of hemimetabolous insects have rarely been reported, especially in cockroaches. Pheromone-binding proteins (PBPs) play a vital role in insect sex pheromone recognition, which solubilize and carry the hydrophobic pheromonal compounds through the antennal lymph to receptors. In this study, two potential PBPs ( and ) were identified on the basis of their biased expression in male antennae using tissue transcriptome data and verified by the quantitative real-time polymerase chain reaction approach. We then expressed and purified the two identified odorant-binding proteins (OBPs) using the expression system and affinity purification. binding studies showed that the two OBPs display stronger binding affinities to the female volatile sex pheromone blattellaquinone than to its analogues and contact sex pheromone components. Finally, three-dimensional modeling of the two OBPs and dock conformation with sex pheromone molecules showed BgerOBP26 has a larger odorant cavity and more conservative active amino acid residues than BgerOBP40. These results illuminated the binding characteristics of potential PBPs of , which could lay the groundwork for improved understanding of many aspects of the chemical ecology of . Moreover, this information complements the understanding of the olfactory molecular mechanism in cockroaches and provides potential gene targets for control.