Evidence map›Paper›PMID 32929138›Full record

ArticleScientific reports2020

Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition.

Oliver C Grant, David Montgomery, Keigo Ito, Robert J Woods

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 249 papers.

0numbers the graph read from it
0cells of the map it votes in
249citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

249 citing papers in PubMed, 409 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Host Glycan-Lectin Interplay in SARS-CoV-2 Infection.International journal of molecular sciences · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Molecular mechanisms of SARS-CoV-2 entry: implications for biomedical strategies.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  18. Article
  19. Biochemistry and biophysics reports · 2025
    Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Oliver C GrantComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Rd, Athens, GA, 30602, USA.
David MontgomeryComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Rd, Athens, GA, 30602, USA.
Keigo ItoComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Rd, Athens, GA, 30602, USA.
Robert J WoodsComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Rd, Athens, GA, 30602, USA. rwoods@ccrc.uga.edu.
University of Georgia · US

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
Tools to enable non-specialists to model glycoconjugates and glycan-protein interactionsU01CA207824 · NCI · UNIVERSITY OF GEORGIA · PI FOLEY, B. LACHELE, WOODS, ROBERT J · 2016 to 2018
$1.7M
Glycoscience Training ProgramT32GM107004 · NIGMS · UNIVERSITY OF GEORGIA · PI AMSTER, I JONATHAN, HALTIWANGER, ROBERT S. · 2014 to 2021
$1.3M
NCI NIH HHS U01 CA207824NIGMS NIH HHS P41 GM103390NIGMS NIH HHS T32 GM107004NIH HHS U01 CA207824
6 · The paper itself

Abstract

Here we have generated 3D structures of glycoforms of the spike (S) glycoprotein from SARS-CoV-2, based on reported 3D structures and glycomics data for the protein produced in HEK293 cells. We also analyze structures for glycoforms representing those present in the nascent glycoproteins (prior to enzymatic modifications in the Golgi), as well as those that are commonly observed on antigens present in other viruses. These models were subjected to molecular dynamics (MD) simulation to determine the extent to which glycan microheterogeneity impacts the antigenicity of the S glycoprotein. Lastly, we have identified peptides in the S glycoprotein that are likely to be presented in human leukocyte antigen (HLA) complexes, and discuss the role of S protein glycosylation in potentially modulating the innate and adaptive immune response to the SARS-CoV-2 virus or to a related vaccine. The 3D structures show that the protein surface is extensively shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain, and also that the degree of shielding is largely insensitive to the specific glycoform. Despite the relatively modest contribution of the glycans to the total molecular weight of the S trimer (17% for the HEK293 glycoform) they shield approximately 40% of the protein surface.

Indexed as

Adaptive ImmunityAmino Acid SequenceAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntigen-Antibody ComplexBetacoronavirusBinding SitesCoronavirus InfectionsCOVID-19GlycosylationHEK293 CellsHLA AntigensHumansImmunity, InnateMolecular Dynamics SimulationPandemicsACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntigen-Antibody ComplexHLA AntigensPeptidyl-Dipeptidase APolysaccharidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID32929138
PMCPMC7490396
OpenAlexW3086603362

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.