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Vulnerabilities in coronavirus glycan shields despite extensive glycosylation

Author

Listed:
  • Yasunori Watanabe

    (University of Southampton
    University of Oxford
    Wellcome Centre for Human Genetics)

  • Zachary T. Berndsen

    (The Scripps Research Institute)

  • Jayna Raghwani

    (University of Oxford)

  • Gemma E. Seabright

    (University of Southampton
    University of Oxford)

  • 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
    Skaggs Institute for Chemical Biology, The Scripps Research Institute)

  • Thomas A. Bowden

    (Wellcome Centre for Human Genetics)

  • Andrew B. Ward

    (The Scripps Research Institute)

  • Max Crispin

    (University of Southampton)

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.

Suggested Citation

  • 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 & Max Crispin, 2020. "Vulnerabilities in coronavirus glycan shields despite extensive glycosylation," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16567-0
    DOI: 10.1038/s41467-020-16567-0
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    Cited by:

    1. David Chmielewski & Eric A. Wilson & Grigore Pintilie & Peng Zhao & Muyuan Chen & Michael F. Schmid & Graham Simmons & Lance Wells & Jing Jin & Abhishek Singharoy & Wah Chiu, 2023. "Structural insights into the modulation of coronavirus spike tilting and infectivity by hinge glycans," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. Nikhil Kumar Tulsian & Raghuvamsi Venkata Palur & Xinlei Qian & Yue Gu & Bhuvaneshwari D/O Shunmuganathan & Firdaus Samsudin & Yee Hwa Wong & Jianqing Lin & Kiren Purushotorman & Mary McQueen Kozma & , 2023. "Defining neutralization and allostery by antibodies against COVID-19 variants," Nature Communications, Nature, vol. 14(1), pages 1-23, December.

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