Site-Specific Steric Control of SARS-CoV-2 Spike Glycosylation.
Biochemistry
; 60(27): 2153-2169, 2021 07 13.
Article
in English
| MEDLINE | ID: covidwho-1387101
Preprint
This scientific journal article is probably based on a previously available preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
See preprint
This scientific journal article is probably based on a previously available preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
See preprint
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.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Protein Conformation
/
Spike Glycoprotein, Coronavirus
/
SARS-CoV-2
/
COVID-19
Topics:
Vaccines
Limits:
Animals
/
Humans
Language:
English
Journal:
Biochemistry
Year:
2021
Document Type:
Article
Affiliation country:
ACS.BIOCHEM.1C00279
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