Evidence map›Paper›PMID 32366695›Full record

ArticleScience (New York, N.Y.)2020

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

Yasunori Watanabe, Joel D Allen, Daniel Wrapp, Jason S McLellan, Max Crispin

Open access · hybridAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1,009 papers.

0numbers the graph read from it
0cells of the map it votes in
1,009citing papers in PubMed
35.8field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1,009 citing papers in PubMed, 1,673 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Switching Spike Plasticity Shapes ACE2 Engagement Across SARS-CoV-2 Variants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Canonical Antibodies Adopt Distinct Binding Modes to Recognize Viral Glycan Shields.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Spatial Glyco-Codes Define Human Liver Pathology and Progression.bioRxiv : the preprint server for biology · 2026
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

949 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Yasunori Watanabe *School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, UK.ORCID 0000-0002-7952-1268
Joel D Allen *School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, UK.ORCID 0000-0003-2547-968X
Daniel WrappDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.ORCID 0000-0002-0538-9647
Jason S McLellanDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.ORCID 0000-0003-3991-542X
Max CrispinSchool of Biological Sciences, University of Southampton, Southampton SO17 1BJ, UK. max.crispin@soton.ac.uk.ORCID 0000-0002-1072-2694
The University of Texas at Austin · USUniversity of Southampton · GBCentre for Human Genetics · GB

Funding

Identification of neutralizing epitopes on SARS-CoV-2 spike for design of vaccines and small-molecule antiviralsUM1AI144462 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI BURTON, DENNIS R. · 2019 to 2025
$201.6M
Structure, Function and Antigenicity of Coronavirus Spike ProteinsR01AI127521 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI MCLELLAN, JASON SCOTT, WARD, ANDREW BARRETT · 2017 to 2021
$3.1M
NIAID NIH HHS R01 AI127521NIAID NIH HHS UM1 AI144462
6 · The paper itself

Abstract

The emergence of the betacoronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 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.

Indexed as

BetacoronavirusBinding SitesCoronavirus InfectionsCOVID-19GlycopeptidesGlycosylationHumansMass SpectrometryModels, MolecularOligosaccharidesPandemicsPneumonia, ViralPolysaccharidesProtein Structure, TertiaryRecombinant ProteinsSARS-CoV-2GlycopeptidesoligomannosideOligosaccharidesPolysaccharidesRecombinant ProteinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID32366695
PMCPMC7199903
OpenAlexW3023376619

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.