Site-specific glycan analysis of the SARS-CoV-2 spike-Reference-Cited by-同舟云学术

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

Published:2020-07-17 Issue:6501 Volume:369 Page:330-333
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Watanabe Yasunori¹²³^ORCID,Allen Joel D.¹^ORCID,Wrapp Daniel⁴^ORCID,McLellan Jason S.⁴^ORCID,Crispin Max¹^ORCID

Affiliation:

1. School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, UK.

2. Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.

3. Division of Structural Biology, University of Oxford, Wellcome Centre for Human Genetics, Oxford OX3 7BN, UK.

4. Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.

Abstract

SARS-CoV-2 spike protein, elaborated Vaccine development for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is focused on the trimeric spike protein that initiates infection. Each protomer in the trimeric spike has 22 glycosylation sites. How these sites are glycosylated may affect which cells the virus can infect and could shield some epitopes from antibody neutralization. Watanabe et al. expressed and purified recombinant glycosylated spike trimers, proteolysed them to yield glycopeptides containing a single glycan, and determined the composition of the glycan sites by mass spectrometry. The analysis provides a benchmark that can be used to measure antigen quality as vaccines and antibody tests are developed. Science this issue p. 330

Funder

National Institutes of Health

Bill and Melinda Gates Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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