Evidence map›Paper›PMID 35980012›Full record

ArticleACS infectious diseases2022

Sialic Acid and Fucose Residues on the SARS-CoV-2 Receptor-Binding Domain Modulate IgG Antibody Reactivity.

Ebba Samuelsson, Ekaterina Mirgorodskaya, Kristina Nyström, Malin Bäckström, Jan-Åke Liljeqvist, Rickard Nordén

Open access · hybridAbstract read
In one paragraph

Article in ACS infectious diseases, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Ebba SamuelssonDepartment of Infectious Diseases, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg 413 46, Sweden.
Ekaterina MirgorodskayaProteomics Core Facility, Sahlgrenska Academy, University of Gothenburg, Gothenburg 413 90, Sweden.
Kristina NyströmDepartment of Infectious Diseases, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg 413 46, Sweden.
Malin BäckströmMammalian Protein Expression Core Facility, Sahlgrenska Academy, University of Gothenburg, Gothenburg 413 90, Sweden.
Jan-Åke LiljeqvistDepartment of Infectious Diseases, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg 413 46, Sweden.
Rickard NordénDepartment of Infectious Diseases, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg 413 46, Sweden.ORCID 0000-0002-3866-7228
University of Gothenburg · SESahlgrenska University Hospital · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein is a conserved domain and a target for neutralizing antibodies. We defined the carbohydrate content of the recombinant RBD produced in different mammalian cells. We found a higher degree of complex-type N-linked glycans, with less sialylation and more fucosylation, when the RBD was produced in human embryonic kidney cells compared to the same protein produced in Chinese hamster ovary cells. The carbohydrates on the RBD proteins were enzymatically modulated, and the effect on antibody reactivity was evaluated with serum samples from SARS-CoV-2 positive patients. Removal of all carbohydrates diminished antibody reactivity, while removal of only sialic acids or terminal fucoses improved the reactivity. The RBD produced in Lec3.2.8.1-cells, which generate carbohydrate structures devoid of sialic acids and with reduced fucose content, exhibited enhanced antibody reactivity, verifying the importance of these specific monosaccharides. The results can be of importance for the design of future vaccine candidates, indicating that it is possible to enhance the immunogenicity of recombinant viral proteins.

Indexed as

COVID-19SARS-CoV-2AnimalsAntibodies, ViralCHO CellsCricetinaeCricetulusFucoseHumansImmunoglobulin GN-Acetylneuraminic AcidSpike Glycoprotein, CoronavirusAntibodies, ViralFucoseImmunoglobulin GN-Acetylneuraminic AcidSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2antibody reactivityglycoepitopeglycoproteomicsmass spectrometryreceptor binding domainSARS-CoV-2

Identifiers

PMID35980012
PMCPMC9469093
OpenAlexW4293066841

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.