Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike Proteins.
Mol Cell Proteomics
; 20: 100058, 2021.
Article
in English
| MEDLINE | ID: covidwho-1199368
ABSTRACT
The glycoprotein spike (S) on the surface of severe acute respiratory syndrome coronavirus (SARS-CoV-2) is a determinant for viral invasion and host immune response. Herein, we characterized the site-specific N-glycosylation of S protein at the level of intact glycopeptides. All 22 potential N-glycosites were identified in the S-protein protomer and were found to be preserved among the 753 SARS-CoV-2 genome sequences. The glycosites exhibited glycoform heterogeneity as expected for a human cell-expressed protein subunit. We identified masses that correspond to 157 N-glycans, primarily of the complex type. In contrast, the insect cell-expressed S protein contained 38 N-glycans, completely of the high-mannose type. Our results revealed that the glycan types were highly determined by the differential processing of N-glycans among human and insect cells, regardless of the glycosites' location. Moreover, the N-glycan compositions were conserved among different sizes of subunits. Our study indicates that the S protein N-glycosylation occurs regularly at each site, albeit the occupied N-glycans were diverse and heterogenous. This N-glycosylation landscape and the differential N-glycan patterns among distinct host cells are expected to shed light on the infection mechanism and present a positive view for the development of vaccines and targeted drugs.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Polysaccharides
/
Recombinant Proteins
/
Spike Glycoprotein, Coronavirus
Topics:
Vaccines
Limits:
Animals
/
Humans
Language:
English
Journal:
Mol Cell Proteomics
Journal subject:
Molecular Biology
/
Biochemistry
Year:
2021
Document Type:
Article
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