NSF Award
2332459
The Historically Black Colleges and Universities - Undergraduate Program (HBCU-UP) provides support to strengthen STEM undergraduate education and research at HBCUs. Viruses appear to change their aggregation state depending on the solution conditions in the transmission pathway. This project is designed to determine the extent to which the solution state is universally determined by the virus glycosylation. Since virus infectivity, immune-stealth, and transmissibility changes with aggregation, our goal is to determine if highly mutable viruses like influenza can be additionally intercepted based on the susceptibility of their solution state. The broader impact of the project is to better understand disparities in virus transmission from differences in the solution conditions in different populations. <br/><br/>While there has been a lot of interest in how these virus sugars are recognized by proteins of the immune system and signaling pathways, little is known about how the biophysics of the sugars fundamentally and broadly protects viruses in their twin purposes of transmission and infection. This project has two goals: 1) To investigate if complex N-glycans broadly determine virus aggregation state of viruses, and the infectivity, antibody (Ab) resistance, mucin binding in different solution conditions; and 2) To determine how NA and Hb envelop proteins on influenza A virus, which have Sialic acid -cleaving and -binding properties, respectively, systematically change the solution behavior and vulnerability of Influenza A virus to suits its virulence needs. Methodologies include dynamic light scattering, atomic force microscopy, florescence microscopy, rheology, and cell culture.<br/><br/>This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.
