Site-Specific Steric Control of SARS-CoV-2 Spike Glycosylation.
Biochemistry
; 60(27): 2153-2169, 2021 07 13.
Article
em En
| MEDLINE
| ID: mdl-34213308
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
/
Glicoproteína da Espícula de Coronavírus
/
SARS-CoV-2
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COVID-19
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article
País de afiliação:
Reino Unido