Roles of glycosylation and redox states on SARS-CoV-2 spike protein actions

Abstract The pandemic of Coronavirus Disease 2019 (COVID-19) is caused by Severe Acute Respiratory Syndrome 2 (SARS-CoV-2). viral fusion protein, spike binds to its receptor Angiotensin-Converting Enzyme (ACE2) enter host cells. Further, the S1 subunit protein may be cleaved off virus and affect various organs. In addition tightly binding ACE2, also enhances peptidase activity ACE2 activate cell signaling. present study compared effects recombinant proteins expressed in HEK cells E. coli. heavily glycosylated strongly while coli not exhibits no binding. SulfoBiotics Protein Redox State Monitoring assay determined that cysteine residues are fully oxidized, those reduced. deglycosylation Glycopeptidase F attenuates binding, although completely, oxidation hydrogen peroxide contrast highly distinct capacities E coli, both systems enhance promote These results suggest state contributes introduce a new concept regulation protein-ACE2 redox mechanisms. Glycosylation states, however, do define abilities enzyme or Supported grants from NIH (R03 AG71596, R21 AG73919)