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) glycoprotei...
| Main Authors: | , , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Springer Nature
2020
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| _version_ | 1797092832882720768 |
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| author | Watanabe, Y Berndsen, ZT Raghwani, J Seabright, GE Allen, JD Pybus, OG McLellan, JS Wilson, IA Bowden, TA Ward, AB Crispin, M |
| author_facet | Watanabe, Y Berndsen, ZT Raghwani, J Seabright, GE Allen, JD Pybus, OG McLellan, JS Wilson, IA Bowden, TA Ward, AB Crispin, M |
| author_sort | Watanabe, Y |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T03:51:41Z |
| format | Journal article |
| id | oxford-uuid:c17d4dd8-79b5-43ef-bf8c-61a1c7fbbdf7 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:51:41Z |
| publishDate | 2020 |
| publisher | Springer Nature |
| record_format | dspace |
| spelling | oxford-uuid:c17d4dd8-79b5-43ef-bf8c-61a1c7fbbdf72022-03-27T06:01:51ZVulnerabilities in coronavirus glycan shields despite extensive glycosylationJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:c17d4dd8-79b5-43ef-bf8c-61a1c7fbbdf7EnglishSymplectic ElementsSpringer Nature2020Watanabe, YBerndsen, ZTRaghwani, JSeabright, GEAllen, JDPybus, OGMcLellan, JSWilson, IABowden, TAWard, ABCrispin, MSevere 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. |
| spellingShingle | Watanabe, Y Berndsen, ZT Raghwani, J Seabright, GE Allen, JD Pybus, OG McLellan, JS Wilson, IA Bowden, TA Ward, AB Crispin, M Vulnerabilities in coronavirus glycan shields despite extensive glycosylation |
| title | Vulnerabilities in coronavirus glycan shields despite extensive glycosylation |
| title_full | Vulnerabilities in coronavirus glycan shields despite extensive glycosylation |
| title_fullStr | Vulnerabilities in coronavirus glycan shields despite extensive glycosylation |
| title_full_unstemmed | Vulnerabilities in coronavirus glycan shields despite extensive glycosylation |
| title_short | Vulnerabilities in coronavirus glycan shields despite extensive glycosylation |
| title_sort | vulnerabilities in coronavirus glycan shields despite extensive glycosylation |
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