In Person & By Zoom

Zoom Link: https://us02web.zoom.us/j/81853192041?pwd=DlS9NR8Q7JLSk7wgYACVanVFiTtcnz.1
Meeting ID: 818 5319 2041
Passcode: 563519

Mary Kay McLean
Ph.D. Student
Department of Tropical Medicine, Medical Microbiology and Pharmacology
John A. Burns School of Medicine, University of Hawaii at Manoa

According to the World Health Organization, there are around a billion cases of seasonal influenza annually with 3-5 million cases of severe illness resulting in 290,000 to 650,000 deaths. Current influenza vaccinations target the more abundant hemagglutinin surface protein and have shown to be suboptimal in preventing disease due to the high mutation rate of circulating virus throughout the year. Studies have demonstrated that Neuraminidase (NA), the second most abundant influenza surface protein, may be a more effective target due to its slower evolution rate compared to HA and its similarities across strains. Attempts at producing a stable recombinant NA protein in the laboratory setting have been met with challenges. There are promising results utilizing a Measles virus phosphoprotein to ensure the intermolecular tetramer formation required for production of stable and enzymatically active NA is maintained. To date, the production of this NA globular head stabilized by the Measles virus phosphoprotein tetramerization domain (N1-MPP) for the use as vaccine antigen has been performed utilizing the baculovirus expression system. This study aims to utilize the Drosophila S2 expression system to grow high concentrations of protein in suspension cultures allowing scaling up and maximizing yield. The use of this system to generate N1-MPP could aid in quick and sustainable production of this candidate vaccine antigen.