Cell Reports
Volume 42, Issue 4, 25 April 2023, 112307
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Article
The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2

https://doi.org/10.1016/j.celrep.2023.112307Get rights and content
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Highlights

  • N-linked glycans are prevalent across SARS-CoV-2-like sarbecoviruses

  • 3D maps of sarbecovirus glycan shields demonstrate localized changes in structure

  • Key regions of conservation include the C-terminal S2 glycan sites

  • SARS-CoV-2 lacks the conserved N370 glycan, which influences viral infectivity

Summary

Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoonosis motivates the search for pan-coronavirus vaccines. This necessitates a better understanding of the glycan shields of coronaviruses, which can occlude potential antibody epitopes on spike glycoproteins. Here, we compare the structure of 12 sarbecovirus glycan shields. Of the 22 N-linked glycan attachment sites present on SARS-CoV-2, 15 are shared by all 12 sarbecoviruses. However, there are significant differences in the processing state at glycan sites in the N-terminal domain, such as N165. Conversely, glycosylation sites in the S2 domain are highly conserved and contain a low abundance of oligomannose-type glycans, suggesting a low glycan shield density. The S2 domain may therefore provide a more attractive target for immunogen design efforts aiming to generate a pan-coronavirus antibody response.

Keywords

SARS-CoV-2
pan-coronavirus
N-linked glycosylation
glycan shielding

Research topic(s)

CP: Microbiology
CP: Immunology

Data and code availability

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