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MassIVE MSV000090155: The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2

MassIVE MSV000090155: The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2
MassIVE MSV000090155: 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.,MassIVE MSV000090155 - The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2
University of California San Diego
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9

(2022) MassIVE MSV000090155: The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2. University of California San Diego doi:10.25345/c5dz03587 [Dataset]

Record type: 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.,MassIVE MSV000090155 - The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2

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Published date: 2022

Identifiers

Local EPrints ID: 471619
URI: http://eprints.soton.ac.uk/id/eprint/471619
PURE UUID: 4d61e425-0617-4abb-a587-23a41f82debe
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

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Date deposited: 15 Nov 2022 17:33
Last modified: 16 Nov 2022 02:47

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