Site-specific glycan analysis of the SARS-CoV-2 spike
- PMID: 32366695
- PMCID: PMC7199903
- DOI: 10.1126/science.abb9983
Site-specific glycan analysis of the SARS-CoV-2 spike
Abstract
The emergence of the betacoronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), represents a considerable threat to global human health. Vaccine development is focused on the principal target of the humoral immune response, the spike (S) glycoprotein, which mediates cell entry and membrane fusion. The SARS-CoV-2 S gene encodes 22 N-linked glycan sequons per protomer, which likely play a role in protein folding and immune evasion. Here, using a site-specific mass spectrometric approach, we reveal the glycan structures on a recombinant SARS-CoV-2 S immunogen. This analysis enables mapping of the glycan-processing states across the trimeric viral spike. We show how SARS-CoV-2 S glycans differ from typical host glycan processing, which may have implications in viral pathobiology and vaccine design.
Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.
Figures
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Update of
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Site-specific analysis of the SARS-CoV-2 glycan shield.bioRxiv [Preprint]. 2020 Mar 28:2020.03.26.010322. doi: 10.1101/2020.03.26.010322. bioRxiv. 2020. Update in: Science. 2020 Jul 17;369(6501):330-333. doi: 10.1126/science.abb9983. PMID: 32511336 Free PMC article. Updated. Preprint.
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