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Vulnerabilities in coronavirus glycan shields despite extensive glycosylation

Vulnerabilities in coronavirus glycan shields despite extensive glycosylation
Vulnerabilities in coronavirus glycan shields despite extensive glycosylation

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.

2041-1723
2688
Watanabe, Yasunori
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Berndsen, Zachary T
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Raghwani, Jayna
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Seabright, Gemma E
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Allen, Joel D
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Pybus, Oliver G
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McLellan, Jason S
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Wilson, Ian A
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Bowden, Thomas A
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Ward, Andrew B
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Crispin, Max
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Watanabe, Yasunori
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Berndsen, Zachary T
aff7a718-4e12-4574-94e1-f44ccdd5b72e
Raghwani, Jayna
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Seabright, Gemma E
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Allen, Joel D
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Pybus, Oliver G
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McLellan, Jason S
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Wilson, Ian A
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Bowden, Thomas A
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Ward, Andrew B
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Crispin, Max
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Watanabe, Yasunori, Berndsen, Zachary T, Raghwani, Jayna, Seabright, Gemma E, Allen, Joel D, Pybus, Oliver G, McLellan, Jason S, Wilson, Ian A, Bowden, Thomas A, Ward, Andrew B and Crispin, Max (2020) Vulnerabilities in coronavirus glycan shields despite extensive glycosylation. Nature Communications, 11 (1), 2688, [2688]. (doi:10.1038/s41467-020-16567-0).

Record type: Article

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.

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e-pub ahead of print date: 27 May 2020

Identifiers

Local EPrints ID: 441400
URI: http://eprints.soton.ac.uk/id/eprint/441400
ISSN: 2041-1723
PURE UUID: 7ff0d879-0cd5-483a-99ba-386bbe92c4f8
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

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Date deposited: 11 Jun 2020 16:31
Last modified: 04 Mar 2021 02:50

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Contributors

Author: Yasunori Watanabe
Author: Zachary T Berndsen
Author: Jayna Raghwani
Author: Gemma E Seabright
Author: Joel D Allen
Author: Oliver G Pybus
Author: Jason S McLellan
Author: Ian A Wilson
Author: Thomas A Bowden
Author: Andrew B Ward
Author: Max Crispin ORCID iD

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