Site-specific steric control of SARS-CoV-2 spike glycosylation

Author:

Allen Joel D.ORCID,Chawla HimanshiORCID,Samsudin FirdausORCID,Zuzic LorenaORCID,Shivgan Aishwary TukaramORCID,Watanabe YasunoriORCID,He Wan-tingORCID,Callaghan Sean,Song GeORCID,Yong PeterORCID,Brouwer Philip J. M.ORCID,Song YutongORCID,Cai YongfeiORCID,Duyvesteyn Helen M. E.ORCID,Malinauskas TomasORCID,Kint Joeri,Pino Paco,Wurm Maria J.ORCID,Frank MartinORCID,Chen BingORCID,Stuart David I.ORCID,Sanders Rogier W.ORCID,Andrabi RaieesORCID,Burton Dennis R.,Li SaiORCID,Bond Peter J.ORCID,Crispin MaxORCID

Abstract

AbstractA 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 between 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 infectious virus S protein. We find patterns which are conserved across all samples and this can be associated with site-specific stalling of glycan maturation which act as a highly sensitive reporter of protein structure. Molecular dynamics (MD) simulations of a fully glycosylated spike support s 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.

Publisher

Cold Spring Harbor Laboratory

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