Evidence map›Paper›PMID 35682724›Full record

ArticleInternational journal of molecular sciences2022

Determination of IgG1 and IgG3 SARS-CoV-2 Spike Protein and Nucleocapsid Binding-Who Is Binding Who and Why?

Jason K Iles, Raminta Zmuidinaite, Christoph Sadee, Anna Gardiner, Jonathan Lacey, Stephen Harding, Gregg Wallis, Roshani Patel, Debra Roblett, Jonathan Heeney and 2 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

9 citing papers in PubMed, 14 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

12 authors at 3 institutions in 1 country.

Jason K IlesMAPSciences, The iLab, Stannard Way, Bedford MK44 3RZ, UK.
Raminta ZmuidinaiteMAPSciences, The iLab, Stannard Way, Bedford MK44 3RZ, UK.ORCID 0000-0001-7728-6623
Christoph SadeeThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Anna GardinerMAPSciences, The iLab, Stannard Way, Bedford MK44 3RZ, UK.
Jonathan LaceyMAPSciences, The iLab, Stannard Way, Bedford MK44 3RZ, UK.
Stephen HardingThe Binding Site Group Ltd., 8 Calthorpe Road, Edgbaston, Birmingham B15 1QT, UK.
Gregg WallisThe Binding Site Group Ltd., 8 Calthorpe Road, Edgbaston, Birmingham B15 1QT, UK.
Roshani PatelThe Binding Site Group Ltd., 8 Calthorpe Road, Edgbaston, Birmingham B15 1QT, UK.
Debra RoblettThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Jonathan HeeneyLaboratory of Viral Zoonotics, Department of Veterinary Medicine, University of Cambridge, Madingley Road, Cambridge CB3 0ES, UK.
Helen BaxendaleRoyal Papworth Hospital NHS Foundation Trust, Cambridge CB3 0ES, UK.
Ray Kruse IlesMAPSciences, The iLab, Stannard Way, Bedford MK44 3RZ, UK.
University of Cambridge · GBThe Francis Crick Institute · GBPapworth Hospital NHS Foundation Trust · GB

Funding

National Institute for Health Research G107217
6 · The paper itself

Abstract

The involvement of immunoglobulin (Ig) G3 in the humoral immune response to SARS-CoV-2 infection has been implicated in the pathogenesis of acute respiratory distress syndrome (ARDS) in COVID-19. The exact molecular mechanism is unknown, but it is thought to involve this IgG subtype's differential ability to fix, complement and stimulate cytokine release. We examined the binding of convalescent patient antibodies to immobilized nucleocapsids and spike proteins by matrix-assisted laser desorption/ionization-time of flight (MALDI-ToF) mass spectrometry. IgG3 was a major immunoglobulin found in all samples. Differential analysis of the spectral signatures found for the nucleocapsid versus the spike protein demonstrated that the predominant humoral immune response to the nucleocapsid was IgG3, whilst for the spike protein it was IgG1. However, the spike protein displayed a strong affinity for IgG3 itself, as it would bind from control plasma samples, as well as from those previously infected with SARS-CoV-2, similar to the way protein G binds IgG1. Furthermore, detailed spectral analysis indicated that a mass shift consistent with hyper-glycosylation or glycation was a characteristic of the IgG3 captured by the spike protein.

Indexed as

COVID-19Spike Glycoprotein, CoronavirusAntibodies, ViralHumansImmunoglobulin GNucleocapsidSARS-CoV-2Antibodies, ViralImmunoglobulin GSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2convalescent plasmaCOVID-19IgG1IgG3nucleocapsidpredictive profilespike protein

Identifiers

PMID35682724
PMCPMC9181569
OpenAlexW4281752128

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.