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

Keywords

GlycanEpitopeGlycosylationSpike (software development)Recombinant DNAVirologyNeutralizationGlycoproteinAntibodyBiologySevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)VirusChemistryBiochemistryCoronavirus disease 2019 (COVID-19)ImmunologyMedicineGene

MeSH Terms

BetacoronavirusBinding SitesCOVID-19Coronavirus InfectionsGlycopeptidesGlycosylationHumansMass SpectrometryModelsMolecularOligosaccharidesPandemicsPneumoniaViralPolysaccharidesProtein StructureTertiaryRecombinant ProteinsSARS-CoV-2Spike GlycoproteinCoronavirus

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Publication Info

Year
2020
Type
article
Volume
369
Issue
6501
Pages
330-333
Citations
1648
Access
Closed

Social Impact

Social media, news, blog, policy document mentions

Citation Metrics

1648
OpenAlex
91
Influential
1381
CrossRef

Cite This

Yasunori Watanabe, Joel D. Allen, Daniel Wrapp et al. (2020). Site-specific glycan analysis of the SARS-CoV-2 spike. Science , 369 (6501) , 330-333. https://doi.org/10.1126/science.abb9983

Identifiers

DOI
10.1126/science.abb9983
PMID
32366695
PMCID
PMC7199903

Data Quality

Data completeness: 90%