Site-specific steric control of SARS-CoV-2 spike glycosylation

  1. Joel D. Allen
  2. Himanshi Chawla
  3. Firdaus Samsudin
  4. Lorena Zuzic
  5. Aishwary Tukaram Shivgan
  6. Yasunori Watanabe
  7. Wan-ting He
  8. Sean Callaghan
  9. Ge Song
  10. Peter Yong
  11. Philip J. M. Brouwer
  12. Yutong Song
  13. Yongfei Cai
  14. Helen M. E. Duyvesteyn
  15. Tomas Malinauskas
  16. Joeri Kint
  17. Paco Pino
  18. Maria J. Wurm
  19. Martin Frank
  20. Bing Chen
  21. David I. Stuart
  22. Rogier W. Sanders
  23. Raiees Andrabi
  24. Dennis R. Burton
  25. Sai Li
  26. Peter J. Bond
  27. Max Crispin
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Abstract

A central tenet in the design of vaccines is the display of native-like antigens in the elicitation of protective immunity. The abundance of N-linked glycans across the SARS-CoV-2 spike protein is a potential source of heterogeneity between the many different vaccine candidates under investigation. Here, we investigate the glycosylation of recombinant SARS-CoV-2 spike proteins from five different laboratories and compare them against infectious virus S protein. We find patterns which are conserved across all samples and this can be associated with site-specific stalling of glycan maturation which act as a highly sensitive reporter of protein structure. Molecular dynamics (MD) simulations of a fully glycosylated spike support s a model of steric restrictions that shape enzymatic processing of the glycans. These results suggest that recombinant spike-based SARS-CoV-2 immunogen glycosylation reproducibly recapitulates signatures of viral glycosylation.

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