The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and cumulative COVID-19 human health impacts have provided a global case study for the need to maintain a responsive and effective ability to rapidly understand emerging viruses.
The COVID-19 pandemic is caused by the SARS-CoV-2 betacoronavirus, which utilizes its highly glycosylated trimeric spike protein to bind to the cell surface receptor ACE2 glycoprotein and facilitate host cell entry. This presentation will describe studies applying glycomics-informed glycoproteomics to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer spike mimetic immunogen and for a soluble version of human ACE2.
Combining this information with bioinformatic analyses of natural variants and with existing 3D-structures of both glycoproteins can generate molecular dynamic simulations of each glycoprotein alone and interacting with one another.
- The role of glycans in modulating virus spike protein-ACE2 interactions
- How innovations in Thermo Scientific Orbitrap technology can aid in the characterization and localization of glycans on the spike protein
- How mass spectrometry combined with bioinformatic analyses and molecular dynamics simulations can enable visualization of virus spike protein-ACE2 interaction
About the presenter
Dr. Lance Wells, Co-Director, Center of Excellence in Glycoproteomics
Dr. Wells is the co-director of the Thermo Fisher Scientific appointed Center of Excellence in Glycoproteomics. Dr. Wells received the MCP lectureship award in 2016 and has published over 140 manuscripts. He has pioneered several approaches including BEMAD, IDAWG, pseudo-NL triggered MS, and HCD-triggered ETD for the analyses of glycans and glycoproteins.