Evidence map›Paper›PMID 36969164›Full record

ArticleFrontiers in immunology2023

Novel ACE2 fusion protein with adapting activity against SARS-CoV-2 variants

Latifa Zekri, Natalia Ruetalo, Mary Christie, Carolin Walker, Timo Manz, Hans-Georg Rammensee, Helmut R Salih, Michael Schindler, Gundram Jung

Open access · goldFull text read
In one paragraph

Article in Frontiers in immunology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

5 citing papers in PubMed, 5 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. 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

9 authors at 4 institutions in 2 countries.

Latifa ZekriDepartment of Immunology, Institute for Cell Biology, Eberhard Karls Universität Tübingen, Tübingen, Germany.
Natalia RuetaloInstitute for Medical Virology and Epidemiology, University Hospital Tübingen, Tübingen, Germany.
Mary ChristieSchool of Life and Environmental Sciences and School of Life of Medical Sciences, The University of Sydney, Sydney, NSW, Australia.
Carolin WalkerDepartment of Immunology, Institute for Cell Biology, Eberhard Karls Universität Tübingen, Tübingen, Germany.
Timo ManzDepartment of Immunology, Institute for Cell Biology, Eberhard Karls Universität Tübingen, Tübingen, Germany.
Hans-Georg RammenseeDepartment of Immunology, Institute for Cell Biology, Eberhard Karls Universität Tübingen, Tübingen, Germany.
Helmut R SalihGerman Cancer Research Center (DKFZ) Partner Site Tübingen, German Cancer Consortium (DKTK), Tübingen, Germany.
Michael SchindlerInstitute for Medical Virology and Epidemiology, University Hospital Tübingen, Tübingen, Germany.
Gundram JungDepartment of Immunology, Institute for Cell Biology, Eberhard Karls Universität Tübingen, Tübingen, Germany.
German Cancer Research Center · DEDeutschen Konsortium für Translationale Krebsforschung · DEThe University of Sydney · AUUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite the successful development of vaccines and neutralizing antibodies to limit the spread of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), emerging variants prolong the pandemic and emphasize the persistent need to develop effective antiviral treatment regimens. Recombinant antibodies directed to the original SARS-CoV-2 have been successfully used to treat established viral disease. However, emerging viral variants escape the recognition by those antibodies. Here we report the engineering of an optimized ACE2 fusion protein, designated ACE2-M, which comprises a human IgG1 Fc domain with abrogated Fc-receptor binding linked to a catalytically-inactive ACE2 extracellular domain that displays increased apparent affinity to the B.1 spike protein. The affinity and neutralization capacity of ACE2-M is unaffected or even enhanced by mutations present in the spike protein of viral variants. In contrast, a recombinant neutralizing reference antibody, as well as antibodies present in the sera of vaccinated individuals, lose activity against such variants. With its potential to resist viral immune escape ACE2-M appears to be particularly valuable in the context of pandemic preparedness towards newly emerging coronaviruses.

Indexed as

Angiotensin-Converting Enzyme 2COVID-19SARS-CoV-2Antibodies, NeutralizingHumansProtein EngineeringRecombinant Fusion ProteinsSpike Glycoprotein, CoronavirusAngiotensin-Converting Enzyme 2Antibodies, NeutralizingRecombinant Fusion ProteinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE-2fusion proteinimmune escapeneutralizing antibodiesSARS-CoV-2 therapy

Identifiers

PMID36969164
PMCPMC10030959
OpenAlexW4323567797

What Socratic holds

Textfull text, public
LicenceCC BY
measurements read34
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 Socratic graph.