Site-specific glycan analysis of the SARS-CoV-2 spike
Yasunori Watanabe1,2,3,*, Joel D. Allen1,*, Daniel Wrapp4, Jason S. McLellan4, Max Crispin1,†
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Science 04 May 2020:
eabb9983
DOI: 10.1126/science.abb9983
Abstract
The emergence of the betacoronavirus, SARS-CoV-2, the causative agent of COVID-19, represents a significant 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. 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.
