Comprehensive study of glycosylation effects on COVID-19 using mass spectrometry

The pandemic of coronavirus disease 2019 (COVID-19), caused by a novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has become a considerable threat to global human health.

The entry of SARS-CoV-2 into the infected host cell is mediated by the highly glycosylated spike (S) protein on the virus surface, binding to angiotensin-converting enzyme 2 (ACE2).

After infection, specific antibodies can bind to S proteins, forming immune complexes that can neutralize or mediate clearance of the virus.

Since the glycosylation motifs play an important role in protein structure, function and immune evasion, this project aims at studying the glycosylation effects on COVID-19 using mass spectrometry (MS).

In the first 18 months, the glycosylation patterns in different groups of patients will be investigated using nanoscale liquid chromatography mass spectrometry (nanoLC-MS), to elucidate the correlation between glycosylation and severity.

In the 18-36 months, the glycosylation effect on protein-protein interactions involved in COVID-19, such as S protein-ACE2 and S protein-antibody, will be investigated using matrix assisted laser desorption/ionization mass spectrometry (MALDI-MS) with high mass detector.

This project may provide implications in vaccine design, antibody therapies and viral pathobiology for COVID-19, and could be applied in the future for the study of other severe diseases associated with glycosylation.