Evidence map›Paper›PMID 35505068›Full record

ArticleScientific reports2022

COVID-19 patient serum less potently inhibits ACE2-RBD binding for various SARS-CoV-2 RBD mutants.

Daniel Junker, Alex Dulovic, Matthias Becker, Teresa R Wagner, Philipp D Kaiser, Bjoern Traenkle, Katharina Kienzle, Stefanie Bunk, Carlotta Struemper, Helene Haeberle and 11 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  10. Article
  11. Antibody Binding and Angiotensin-Converting Enzyme 2 Binding Inhibition Is Significantly Reduced for Both the BA.1 and BA.2 Omicron Variants.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2023
    Article
  12. Article
  13. Article
  14. Small molecules in the treatment of COVID-19.Signal transduction and targeted therapy · 2022
    Review
  15. Article
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

21 authors at 5 institutions in 1 country.

Daniel JunkerNMI Natural and Medical Sciences Institute at the University of Tübingen, Markwiesenstrasse 55, 72770, Reutlingen, Germany.
Alex DulovicNMI Natural and Medical Sciences Institute at the University of Tübingen, Markwiesenstrasse 55, 72770, Reutlingen, Germany.
Matthias BeckerNMI Natural and Medical Sciences Institute at the University of Tübingen, Markwiesenstrasse 55, 72770, Reutlingen, Germany.
Teresa R WagnerNMI Natural and Medical Sciences Institute at the University of Tübingen, Markwiesenstrasse 55, 72770, Reutlingen, Germany.
Philipp D KaiserNMI Natural and Medical Sciences Institute at the University of Tübingen, Markwiesenstrasse 55, 72770, Reutlingen, Germany.
Bjoern TraenkleNMI Natural and Medical Sciences Institute at the University of Tübingen, Markwiesenstrasse 55, 72770, Reutlingen, Germany.
Katharina KienzleDepartment Internal Medicine I, University Hospital Tübingen, Otfried-Müller-Strasse 10, 72076, Tübingen, Germany.
Stefanie BunkDepartment Internal Medicine I, University Hospital Tübingen, Otfried-Müller-Strasse 10, 72076, Tübingen, Germany.
Carlotta StruemperDepartment Internal Medicine I, University Hospital Tübingen, Otfried-Müller-Strasse 10, 72076, Tübingen, Germany.
Helene HaeberleDepartment of Anesthesiology and Intensive Care Medicine, University Hospital Tübingen, Tübingen, Germany.
Kristina SchmauderInstitute for Medical Microbiology and Hygiene, University Hospital Tübingen, Tübingen, Germany.
Natalia RuetaloInstitute for Medical Virology and Epidemiology, University Hospital Tübingen, Tübingen, Germany.
Nisar MalekDepartment Internal Medicine I, University Hospital Tübingen, Otfried-Müller-Strasse 10, 72076, Tübingen, Germany.
Karina AlthausInstitute for Clinical and Experimental Transfusion Medicine, University Hospital Tübingen, Tübingen, Germany.
Michael KoeppenDepartment of Anesthesiology and Intensive Care Medicine, University Hospital Tübingen, Tübingen, Germany.
Ulrich RothbauerNMI Natural and Medical Sciences Institute at the University of Tübingen, Markwiesenstrasse 55, 72770, Reutlingen, Germany.
Juliane S WalzDepartment of Internal Medicine, Clinical Collaboration Unit Translational Immunology, German Cancer Consortium (DKTK), University Hospital Tübingen, Tübingen, Germany.
Michael SchindlerInstitute for Medical Virology and Epidemiology, University Hospital Tübingen, Tübingen, Germany.
Michael BitzerDepartment Internal Medicine I, University Hospital Tübingen, Otfried-Müller-Strasse 10, 72076, Tübingen, Germany.
Siri Göpel *Department Internal Medicine I, University Hospital Tübingen, Otfried-Müller-Strasse 10, 72076, Tübingen, Germany. siri.goepel@med.uni-tuebingen.de.
Nicole Schneiderhan-Marra *NMI Natural and Medical Sciences Institute at the University of Tübingen, Markwiesenstrasse 55, 72770, Reutlingen, Germany. Nicole.schneiderhan@nmi.de.
University Children's Hospital Tübingen · DENatural and Medical Sciences Institute · DEUniversity of Tübingen · DEDeutschen Konsortium für Translationale Krebsforschung · DEInstitute of Medical Microbiology and Hygiene · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As global vaccination campaigns against SARS-CoV-2 proceed, there is particular interest in the longevity of immune protection, especially with regard to increasingly infectious virus variants. Neutralizing antibodies (Nabs) targeting the receptor binding domain (RBD) of SARS-CoV-2 are promising correlates of protective immunity and have been successfully used for prevention and therapy. As SARS-CoV-2 variants of concern (VOCs) are known to affect binding to the ACE2 receptor and by extension neutralizing activity, we developed a bead-based multiplex ACE2-RBD inhibition assay (RBDCoV-ACE2) as a highly scalable, time-, cost-, and material-saving alternative to infectious live-virus neutralization tests. By mimicking the interaction between ACE2 and the RBD, this serological multiplex assay allows the simultaneous analysis of ACE2 binding inhibition to the RBDs of all SARS-CoV-2 VOCs and variants of interest (VOIs) in a single well. Following validation against a classical virus neutralization test and comparison of performance against a commercially available assay, we analyzed 266 serum samples from 168 COVID-19 patients of varying severity. ACE2 binding inhibition was reduced for ten out of eleven variants examined compared to wild-type, especially for those displaying the E484K mutation such as VOCs beta and gamma. ACE2 binding inhibition, while highly individualistic, positively correlated with IgG levels. ACE2 binding inhibition also correlated with disease severity up to WHO grade 7, after which it reduced.

Indexed as

COVID-19SARS-CoV-2Angiotensin-Converting Enzyme 2HumansSpike Glycoprotein, CoronavirusAngiotensin-Converting Enzyme 2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID35505068
PMCPMC9062870
OpenAlexW4225310481

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.