The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2
The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2
The animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the impact of SARS-CoV-2. Vaccines remain successful at limiting severe disease and death, however the continued emergence of variants, together with the potential for further zoonosis, motivates the search for pan-coronavirus vaccines that induce broadly neutralizing antibodies. 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 several sarbecovirus glycan shields. Many N-linked glycan attachment sites are shared by all sarbecoviruses, and the processing state of certain sites is highly conserved. However, there are significant differences in the processing state at several glycan sites that surround the receptor binding domain. Our studies reveal similarities and differences in the glycosylation of sarbecoviruses and show how subtle changes in the protein sequence can have pronounced impacts on the glycan shield. [doi:10.25345/C5DZ03587] [dataset license: CC0 1.0 Universal (CC0 1.0)]
University of California San Diego
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
(2022)
The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2.
University of California San Diego
doi:10.25345/c5dz03587
[Dataset]
Abstract
The animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the impact of SARS-CoV-2. Vaccines remain successful at limiting severe disease and death, however the continued emergence of variants, together with the potential for further zoonosis, motivates the search for pan-coronavirus vaccines that induce broadly neutralizing antibodies. 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 several sarbecovirus glycan shields. Many N-linked glycan attachment sites are shared by all sarbecoviruses, and the processing state of certain sites is highly conserved. However, there are significant differences in the processing state at several glycan sites that surround the receptor binding domain. Our studies reveal similarities and differences in the glycosylation of sarbecoviruses and show how subtle changes in the protein sequence can have pronounced impacts on the glycan shield. [doi:10.25345/C5DZ03587] [dataset license: CC0 1.0 Universal (CC0 1.0)]
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Published date: 2022
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Local EPrints ID: 471619
URI: http://eprints.soton.ac.uk/id/eprint/471619
PURE UUID: 4d61e425-0617-4abb-a587-23a41f82debe
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Date deposited: 15 Nov 2022 17:33
Last modified: 06 May 2023 01:54
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