Search for a Presentation
B07 - Investigation of SARS-CoV-2 Envelope Protein Structure and Insights into Therapeutic Potential
The envelope protein from SARS-CoV-2 (E) is a single pass transmembrane protein which accumulates in the endoplasmic reticulum golgi intermediate compartment in host cells, where it acts as a viroporin and an ion channel which plays a critical role in viral budding and assembly.
B07 - Investigation of SARS-CoV-2 Envelope Protein Structure and Insights into Therapeutic Potential
Mentors: Andrew Morris, Ph.D., Gary Lorigan, Ph.D.
The envelope protein from SARS-CoV-2 (E) is a single pass transmembrane protein which accumulates in the endoplasmic reticulum golgi intermediate compartment in host cells, where it acts as a viroporin and an ion channel which plays a critical role in viral budding and assembly. A recent study produced a structure of the pentameric transmembrane domain (TMD) but no structural information is available for the entire protein, and the conformation and dynamics of the C-terminal domain (CTD), which is presumed to be a soluble region, is unknown. Here we present preliminary investigation into the full length of the protein in a native lipid environment utilizing power saturation EPR spectroscopy with site specific introduction of nitroxyl spin-labels as well as Double Electron-Electron Resonance EPR (DEER-EPR) to examine topology of the protein with respect to the lipid bilayer. Our results support a model with moderately buried amphipathic CTD ending in an exposed C terminus.
