Comparison of N- and O-glycosylation on Spike Glycoprotein 1 of SARS-CoV-1 and MERS-CoV

ABSTRACT: Coronaviruses (CoVs) are enveloped pathogens causing multiple respiratory disorders in humans with varying severity. Spike protein is one of the major proteins expressed on coronavirus surface, which mediates coronavirus entry into host cells. Spike proteins are extensively glycosylated and the glycans displayed on spike proteins play a key role in host pathogenesis and immune evasion. In this study, we aim to investigate whether glycosylation patterns are conservative at certain glycosites across different coronaviruses and how different host cells impact on the glycosylation profile. We analyzed site-specific glycans of S1 subunit from SARS-CoV and MERS-CoV spike proteins using hydrophilic interaction chromatography (HILIC) and LC-MS/MS on an Orbitrap Eclipse Tribrid mass spectrometer. We also compared glycosylation of MERS-CoV spike protein derived from HEK293 and insect cells. Our results show that SARS-CoV S1 and MERS-CoV S1 N-glycosylation presents some common patterns and also reveals the similar O-glycosites locations. Consistent with published data, confirming glycan and glycan subtype in specific positions, our data support that some monoclonal antibodies recognize glycan as part of their target epitope and cross react between SARS Cov and SARS CoV2 spike. The coronavirus spike proteins are highly glycosylated. The glycosylation sites, within each virus, are conserved with few changes over time.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Middle East Respiratory Syndrome-related Coronavirus Severe Acute Respiratory Syndrome Coronavirus

SUBMITTER: John Bettinger  

LAB HEAD: John Cipollo

PROVIDER: PXD062150 | Pride | 2025-04-07

REPOSITORIES: Pride