Evidence map›Paper›PMID 33806155›Full record

ArticleViruses2021

Site-Specific O-Glycosylation Analysis of SARS-CoV-2 Spike Protein Produced in Insect and Human Cells.

Ieva Bagdonaite, Andrew J Thompson, Xiaoning Wang, Max Søgaard, Cyrielle Fougeroux, Martin Frank, Jolene K Diedrich, John R Yates, Ali Salanti, Sergey Y Vakhrushev and 2 more

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 80 citations in OpenAlex.

  1. Site-specific O-glycans influence lacritin structure and multimerization in tears.Protein science : a publication of the Protein Society · 2026
    Article
  2. The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025
    Review
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  15. Variations inBiomolecules · 2023
    Article
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  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 3 countries.

Ieva BagdonaiteCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, University of Copenhagen, 2200 Copenhagen, Denmark.ORCID 0000-0002-9383-8448
Andrew J ThompsonDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0001-7865-1856
Xiaoning WangDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0003-0153-324X
Max SøgaardExpreS2ion Biotechnologies, SCION-DTU Science Park, 2970 Hørsholm, Denmark.ORCID 0000-0001-6224-4818
Cyrielle FougerouxCentre for Medical Parasitology at Department of Immunology and Microbiology, University of Copenhagen and Department of Infectious Diseases, Copenhagen University Hospital, 2200 Copenhagen, Denmark.
Martin FrankBiognos AB, 417 05 Gothenburg, Sweden.ORCID 0000-0002-1006-6746
Jolene K DiedrichDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.
John R YatesDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.
Ali SalantiCentre for Medical Parasitology at Department of Immunology and Microbiology, University of Copenhagen and Department of Infectious Diseases, Copenhagen University Hospital, 2200 Copenhagen, Denmark.
Sergey Y VakhrushevCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, University of Copenhagen, 2200 Copenhagen, Denmark.
James C PaulsonDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.
Hans H WandallCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, University of Copenhagen, 2200 Copenhagen, Denmark.ORCID 0000-0003-0240-9232
Scripps Research Institute · USUniversity of Copenhagen · DKBiognos (Sweden) · SEExpreS2ion Biotechnologies (Denmark) · DK

Funding

Danmarks Grundforskningsfond DNRF107H2020 European Research Council GlycoSkin H2020-ERCLundbeckfonden R219-2016-545NIH HHS AI113867NIH HHS AI144462
6 · The paper itself

Abstract

Enveloped viruses hijack not only the host translation processes, but also its glycosylation machinery, and to a variable extent cover viral surface proteins with tolerogenic host-like structures. SARS-CoV-2 surface protein S presents as a trimer on the viral surface and is covered by a dense shield of N-linked glycans, and a few O-glycosites have been reported. The location of O-glycans is controlled by a large family of initiating enzymes with variable expression in cells and tissues and hence is difficult to predict. Here, we used our well-established O-glycoproteomic workflows to map the precise positions of O-linked glycosylation sites on three different entities of protein S-insect cell or human cell-produced ectodomains, or insect cell derived receptor binding domain (RBD). In total 25 O-glycosites were identified, with similar patterns in the two ectodomains of different cell origin, and a distinct pattern of the monomeric RBD. Strikingly, 16 out of 25 O-glycosites were located within three amino acids from known N-glycosites. However, O-glycosylation was primarily found on peptides that were unoccupied by N-glycans, and otherwise had low overall occupancy. This suggests possible complementary functions of O-glycans in immune shielding and negligible effects of O-glycosylation on subunit vaccine design for SARS-CoV-2.

Indexed as

Amino Acid MotifsAnimalsCell LineCOVID-19GlycosylationHumansInsectaPolysaccharidesSARS-CoV-2Species SpecificitySpike Glycoprotein, CoronavirusPolysaccharidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2COVID-19GalNAcmolecular modellingO-glycoproteomicsO-glycosylationSARS-CoV-2site-specific glycosylation

Identifiers

PMID33806155
PMCPMC8064498
OpenAlexW3138090109

What OpenQuestion holds

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LicenceCC BY
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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.