The University of Southampton
University of Southampton Institutional Repository

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 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]

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. [doi:10.25345/C5DZ03587] [dataset license: CC0 1.0 Universal (CC0 1.0)]

This record has no associated files available for download.

More information

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

Catalogue record

Date deposited: 15 Nov 2022 17:33
Last modified: 06 May 2023 01:54

Export record

Altmetrics

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×