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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.

Original publication

DOI

10.1021/acs.biochem.1c00279

Type

Journal article

Journal

Biochemistry

Publication Date

02/07/2021

Volume

60

Pages

2153 - 2169

Addresses

School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, U.K.

Keywords

Vero Cells, Animals, Humans, Protein Conformation, Protein Binding, Glycosylation, Molecular Dynamics Simulation, Spike Glycoprotein, Coronavirus, Chlorocebus aethiops, COVID-19, SARS-CoV-2, COVID-19 Vaccines