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.
Learn about
- 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