The University of Southampton
University of Southampton Institutional Repository
Warning ePrints Soton is experiencing an issue with some file downloads not being available. We are working hard to fix this. Please bear with us.

Site-specific glycan analysis of the SARS-CoV-2 spike

Site-specific glycan analysis of the SARS-CoV-2 spike
Site-specific glycan analysis of the SARS-CoV-2 spike

The emergence of the betacoronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus 2019 (COVID-19), represents a considerable threat to global human health. Vaccine development is focused on the principal target of the humoral immune response, the spike (S) glycoprotein, which mediates cell entry and membrane fusion. The SARS-CoV-2 S gene encodes 22 N-linked glycan sequons per protomer, which likely play a role in protein folding and immune evasion. Here, using a site-specific mass spectrometric approach, we reveal the glycan structures on a recombinant SARS-CoV-2 S immunogen. This analysis enables mapping of the glycan-processing states across the trimeric viral spike. We show how SARS-CoV-2 S glycans differ from typical host glycan processing, which may have implications in viral pathobiology and vaccine design.

0036-8075
330-333
Watanabe, Yasunori
8c0ee4af-a293-4de5-9036-3ce2051b380c
Allen, Joel D.
c89d5569-7659-4835-b535-c9586e956b3a
Wrapp, Daniel
b9734176-e5df-418c-b58d-54ca42164430
Mclellan, Jason S.
622a5b66-c119-4eb8-a102-96503d80e585
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Watanabe, Yasunori
8c0ee4af-a293-4de5-9036-3ce2051b380c
Allen, Joel D.
c89d5569-7659-4835-b535-c9586e956b3a
Wrapp, Daniel
b9734176-e5df-418c-b58d-54ca42164430
Mclellan, Jason S.
622a5b66-c119-4eb8-a102-96503d80e585
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9

Watanabe, Yasunori, Allen, Joel D., Wrapp, Daniel, Mclellan, Jason S. and Crispin, Max (2020) Site-specific glycan analysis of the SARS-CoV-2 spike. Science, 369 (6501), 330-333. (doi:10.1126/science.abb9983).

Record type: Article

Abstract

The emergence of the betacoronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus 2019 (COVID-19), represents a considerable threat to global human health. Vaccine development is focused on the principal target of the humoral immune response, the spike (S) glycoprotein, which mediates cell entry and membrane fusion. The SARS-CoV-2 S gene encodes 22 N-linked glycan sequons per protomer, which likely play a role in protein folding and immune evasion. Here, using a site-specific mass spectrometric approach, we reveal the glycan structures on a recombinant SARS-CoV-2 S immunogen. This analysis enables mapping of the glycan-processing states across the trimeric viral spike. We show how SARS-CoV-2 S glycans differ from typical host glycan processing, which may have implications in viral pathobiology and vaccine design.

Text
Watanabe_Science_2020_accepted
Download (6MB)

More information

Accepted/In Press date: 29 April 2020
e-pub ahead of print date: 4 May 2020
Published date: 17 July 2020

Identifiers

Local EPrints ID: 440603
URI: http://eprints.soton.ac.uk/id/eprint/440603
ISSN: 0036-8075
PURE UUID: 3e1944dc-7579-4271-a2ca-39397393c65e
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

Catalogue record

Date deposited: 12 May 2020 16:30
Last modified: 10 Jan 2022 03:10

Export record

Altmetrics

Contributors

Author: Yasunori Watanabe
Author: Joel D. Allen
Author: Daniel Wrapp
Author: Jason S. Mclellan
Author: Max Crispin ORCID iD

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.

×