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Site-Specific Steric Control of SARS-CoV-2 Spike Glycosylation.
- Source :
-
Biochemistry [Biochemistry] 2021 Jul 13; Vol. 60 (27), pp. 2153-2169. Date of Electronic Publication: 2021 Jul 02. - Publication Year :
- 2021
-
Abstract
- A central tenet in the design of vaccines is the display of native-like antigens in the elicitation of protective immunity. The abundance of N-linked glycans across the SARS-CoV-2 spike protein is a potential source of heterogeneity among the many different vaccine candidates under investigation. Here, we investigate the glycosylation of recombinant SARS-CoV-2 spike proteins from five different laboratories and compare them against S protein from infectious virus, cultured in Vero cells. We find patterns that are conserved across all samples, and this can be associated with site-specific stalling of glycan maturation that acts as a highly sensitive reporter of protein structure. Molecular dynamics simulations of a fully glycosylated spike support a model of steric restrictions that shape enzymatic processing of the glycans. These results suggest that recombinant spike-based SARS-CoV-2 immunogen glycosylation reproducibly recapitulates signatures of viral glycosylation.
- Subjects :
- Animals
COVID-19 immunology
COVID-19 virology
COVID-19 Vaccines genetics
COVID-19 Vaccines immunology
Chlorocebus aethiops
Glycosylation
Humans
Molecular Dynamics Simulation
Protein Binding genetics
SARS-CoV-2 genetics
SARS-CoV-2 pathogenicity
Spike Glycoprotein, Coronavirus chemistry
Spike Glycoprotein, Coronavirus genetics
Spike Glycoprotein, Coronavirus immunology
Vero Cells
COVID-19 genetics
Protein Conformation
SARS-CoV-2 ultrastructure
Spike Glycoprotein, Coronavirus ultrastructure
Subjects
Details
- Language :
- English
- ISSN :
- 1520-4995
- Volume :
- 60
- Issue :
- 27
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 34213308
- Full Text :
- https://doi.org/10.1021/acs.biochem.1c00279