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A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses

Author

Listed:
  • Tiong Kit Tan

    (University of Oxford)

  • Pramila Rijal

    (University of Oxford
    University of Oxford)

  • Rolle Rahikainen

    (University of Oxford)

  • Anthony H. Keeble

    (University of Oxford)

  • Lisa Schimanski

    (University of Oxford
    University of Oxford)

  • Saira Hussain

    (The Francis Crick Institute)

  • Ruth Harvey

    (The Francis Crick Institute)

  • Jack W. P. Hayes

    (The Pirbright Institute)

  • Jane C. Edwards

    (The Pirbright Institute)

  • Rebecca K. McLean

    (The Pirbright Institute)

  • Veronica Martini

    (The Pirbright Institute)

  • Miriam Pedrera

    (The Pirbright Institute)

  • Nazia Thakur

    (The Pirbright Institute)

  • Carina Conceicao

    (The Pirbright Institute)

  • Isabelle Dietrich

    (The Pirbright Institute)

  • Holly Shelton

    (The Pirbright Institute)

  • Anna Ludi

    (The Pirbright Institute)

  • Ginette Wilsden

    (The Pirbright Institute)

  • Clare Browning

    (The Pirbright Institute)

  • Adrian K. Zagrajek

    (The Pirbright Institute)

  • Dagmara Bialy

    (The Pirbright Institute)

  • Sushant Bhat

    (The Pirbright Institute)

  • Phoebe Stevenson-Leggett

    (The Pirbright Institute)

  • Philippa Hollinghurst

    (The Pirbright Institute
    University of Surrey)

  • Matthew Tully

    (The Pirbright Institute)

  • Katy Moffat

    (The Pirbright Institute)

  • Chris Chiu

    (The Pirbright Institute)

  • Ryan Waters

    (The Pirbright Institute)

  • Ashley Gray

    (The Pirbright Institute)

  • Mehreen Azhar

    (The Pirbright Institute)

  • Valerie Mioulet

    (The Pirbright Institute)

  • Joseph Newman

    (The Pirbright Institute)

  • Amin S. Asfor

    (The Pirbright Institute)

  • Alison Burman

    (The Pirbright Institute)

  • Sylvia Crossley

    (The Pirbright Institute)

  • John A. Hammond

    (The Pirbright Institute)

  • Elma Tchilian

    (The Pirbright Institute)

  • Bryan Charleston

    (The Pirbright Institute)

  • Dalan Bailey

    (The Pirbright Institute)

  • Tobias J. Tuthill

    (The Pirbright Institute)

  • Simon P. Graham

    (The Pirbright Institute)

  • Helen M. E. Duyvesteyn

    (The Wellcome Centre for Human Genetics)

  • Tomas Malinauskas

    (The Wellcome Centre for Human Genetics)

  • Jiandong Huo

    (The Wellcome Centre for Human Genetics
    Research Complex at Harwell, and Rosalind Franklin Institute)

  • Julia A. Tree

    (Public Health England)

  • Karen R. Buttigieg

    (Public Health England)

  • Raymond J. Owens

    (The Wellcome Centre for Human Genetics
    Research Complex at Harwell, and Rosalind Franklin Institute)

  • Miles W. Carroll

    (Public Health England
    University of Oxford)

  • Rodney S. Daniels

    (The Francis Crick Institute)

  • John W. McCauley

    (The Francis Crick Institute)

  • David I. Stuart

    (University of Oxford
    The Wellcome Centre for Human Genetics
    Harwell Science & Innovation Campus)

  • Kuan-Ying A. Huang

    (Chang Gung University
    Chang Gung Memorial Hospital)

  • Mark Howarth

    (University of Oxford)

  • Alain R. Townsend

    (University of Oxford
    University of Oxford)

Abstract

There is need for effective and affordable vaccines against SARS-CoV-2 to tackle the ongoing pandemic. In this study, we describe a protein nanoparticle vaccine against SARS-CoV-2. The vaccine is based on the display of coronavirus spike glycoprotein receptor-binding domain (RBD) on a synthetic virus-like particle (VLP) platform, SpyCatcher003-mi3, using SpyTag/SpyCatcher technology. Low doses of RBD-SpyVLP in a prime-boost regimen induce a strong neutralising antibody response in mice and pigs that is superior to convalescent human sera. We evaluate antibody quality using ACE2 blocking and neutralisation of cell infection by pseudovirus or wild-type SARS-CoV-2. Using competition assays with a monoclonal antibody panel, we show that RBD-SpyVLP induces a polyclonal antibody response that recognises key epitopes on the RBD, reducing the likelihood of selecting neutralisation-escape mutants. Moreover, RBD-SpyVLP is thermostable and can be lyophilised without losing immunogenicity, to facilitate global distribution and reduce cold-chain dependence. The data suggests that RBD-SpyVLP provides strong potential to address clinical and logistic challenges of the COVID-19 pandemic.

Suggested Citation

  • Tiong Kit Tan & Pramila Rijal & Rolle Rahikainen & Anthony H. Keeble & Lisa Schimanski & Saira Hussain & Ruth Harvey & Jack W. P. Hayes & Jane C. Edwards & Rebecca K. McLean & Veronica Martini & Miria, 2021. "A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-020-20654-7
    DOI: 10.1038/s41467-020-20654-7
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    Cited by:

    1. Yin-Feng Kang & Cong Sun & Jing Sun & Chu Xie & Zhen Zhuang & Hui-Qin Xu & Zheng Liu & Yi-Hao Liu & Sui Peng & Run-Yu Yuan & Jin-Cun Zhao & Mu-Sheng Zeng, 2022. "Quadrivalent mosaic HexaPro-bearing nanoparticle vaccine protects against infection of SARS-CoV-2 variants," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. James Logue & Robert M. Johnson & Nita Patel & Bin Zhou & Sonia Maciejewski & Bryant Foreman & Haixia Zhou & Alyse D. Portnoff & Jing-Hui Tian & Asma Rehman & Marisa E. McGrath & Robert E. Haupt & Stu, 2023. "Immunogenicity and protection of a variant nanoparticle vaccine that confers broad neutralization against SARS-CoV-2 variants," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    3. Susan K. Vester & Rolle Rahikainen & Irsyad N. A. Khairil Anuar & Rory A. Hills & Tiong Kit Tan & Mark Howarth, 2022. "SpySwitch enables pH- or heat-responsive capture and release for plug-and-display nanoassembly," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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