Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2

The current emergence of the novel coronavirus pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) demands the development of new therapeutic strategies to prevent rapid progress of mortalities. The coronavirus spike (S) protein, which facilitates viral attachment, entry and membrane fusion is heavily glycosylated and plays a critical role in the elicitation of the host immune response. The spike protein is comprised of two protein subunits (S1 and S2), which together possess 22 potential N-glycosylation sites. Herein, we report the glycosylation mapping on spike protein subunits S1 and S2 expressed on human cells through high-resolution mass spectrometry. We have characterized the…

• UD
  U.S. Department of Energy

  Awards: SC0015662, -SC0015662, DE-SC0015662
• NI
  National Institutes of Health

  Award: S10OD018530
• OO
  Office of Science

  Award: DE-SC0015662
• BE
  Basic Energy Sciences

  Award: DE-SC0015662