Vulnerabilities in coronavirus glycan shields despite extensive glycosylation

Yasunori Watanabe, Zachary T. Berndsen, Jayna Raghwani, Gemma E. Seabright, Joel D. Allen, Oliver G. Pybus, Jason S. McLellan, Ian A. Wilson, Thomas A. Bowden, Andrew B. Ward and Max Crispin ()
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Yasunori Watanabe: University of Southampton
Zachary T. Berndsen: The Scripps Research Institute
Jayna Raghwani: University of Oxford
Gemma E. Seabright: University of Southampton
Joel D. Allen: University of Southampton
Oliver G. Pybus: University of Oxford
Jason S. McLellan: The University of Texas at Austin
Ian A. Wilson: The Scripps Research Institute
Thomas A. Bowden: Wellcome Centre for Human Genetics
Andrew B. Ward: The Scripps Research Institute
Max Crispin: University of Southampton

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract Severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS) coronaviruses (CoVs) are zoonotic pathogens with high fatality rates and pandemic potential. Vaccine development focuses on the principal target of the neutralizing humoral immune response, the spike (S) glycoprotein. Coronavirus S proteins are extensively glycosylated, encoding around 66–87 N-linked glycosylation sites per trimeric spike. Here, we reveal a specific area of high glycan density on MERS S that results in the formation of oligomannose-type glycan clusters, which were absent on SARS and HKU1 CoVs. We provide a comparison of the global glycan density of coronavirus spikes with other viral proteins including HIV-1 envelope, Lassa virus glycoprotein complex, and influenza hemagglutinin, where glycosylation plays a known role in shielding immunogenic epitopes. Overall, our data reveal how organisation of glycosylation across class I viral fusion proteins influence not only individual glycan compositions but also the immunological pressure across the protein surface.

Date: 2020
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DOI: 10.1038/s41467-020-16567-0

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