Evidence map›Paper›PMID 34774603›Full record

ArticleAntiviral research2021

Picomolar inhibition of SARS-CoV-2 variants of concern by an engineered ACE2-IgG4-Fc fusion protein.

Hristo L Svilenov, Julia Sacherl, Alwin Reiter, Lisa S Wolff, Cho-Chin Cheng, Marcel Stern, Vincent Grass, Martin Feuerherd, Frank-Peter Wachs, Nicole Simonavicius and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Antiviral research, 2021. 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
1.0field-weighted citation impact, top 20% 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, 19 citations in OpenAlex.

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  4. Antibody-dependent enhancement of coronaviruses.International journal of biological sciences · 2025
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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

16 authors at 4 institutions in 1 country.

Hristo L SvilenovDepartment of Chemistry, Technical University of Munich, Garching, Germany.
Julia SacherlInstitute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany.
Alwin ReiterFormycon AG, Martinsried/Planegg, Germany.
Lisa S WolffInstitute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany.
Cho-Chin ChengInstitute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany; German Center for Infection Research, Munich Partner Site, Munich, Germany.
Marcel SternMax von Pettenkofer Institute & Gene Center, Virology, LMU München, Munich, Germany; German Center for Infection Research, Munich Partner Site, Munich, Germany.
Vincent GrassInstitute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany.
Martin FeuerherdInstitute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany.
Frank-Peter WachsFormycon AG, Martinsried/Planegg, Germany.
Nicole SimonaviciusFormycon AG, Martinsried/Planegg, Germany.
Susanne PippigFormycon AG, Martinsried/Planegg, Germany.
Florian WolschinFormycon AG, Martinsried/Planegg, Germany.
Oliver T KepplerMax von Pettenkofer Institute & Gene Center, Virology, LMU München, Munich, Germany; German Center for Infection Research, Munich Partner Site, Munich, Germany.
Johannes BuchnerDepartment of Chemistry, Technical University of Munich, Garching, Germany.
Carsten BrockmeyerFormycon AG, Martinsried/Planegg, Germany. Electronic address: carsten.brockmeyer@formycon.com.
Ulrike ProtzerInstitute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany; German Center for Infection Research, Munich Partner Site, Munich, Germany. Electronic address: protzer@tum.de.
Helmholtz Zentrum München · DEMorphoSys (Germany) · DEGerman Center for Infection Research · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SARS-CoV-2 enters host cells after binding through its spike glycoprotein to the angiotensin-converting enzyme 2 (ACE2) receptor. Soluble ACE2 ectodomains bind and neutralize the virus, yet their short in vivo half-live limits their therapeutic use. This limitation can be overcome by fusing the fragment crystallizable (Fc) part of human immunoglobulin G (IgG) to the ACE2 ectodomain, but this bears the risk of Fc-receptor activation and antibody-dependent cellular cytotoxicity. Here, we describe optimized ACE2-IgG4-Fc fusion constructs that avoid Fc-receptor activation, preserve the desired ACE2 enzymatic activity and show promising pharmaceutical properties. The engineered ACE2-IgG4-Fc fusion proteins neutralize the original SARS-CoV, pandemic SARS-CoV-2 as well as the rapidly spreading SARS-CoV-2 alpha, beta and delta variants of concern. Importantly, these variants of concern are inhibited at picomolar concentrations proving that ACE2-IgG4 maintains - in contrast to therapeutic antibodies - its full antiviral potential. Thus, ACE2-IgG4-Fc fusion proteins are promising candidate anti-antivirals to combat the current and future pandemics.

Indexed as

Angiotensin-Converting Enzyme 2COVID-19 Drug TreatmentImmunoglobulin GAntiviral AgentsHumansProtein BindingSARS-CoV-2Virus InternalizationAngiotensin-Converting Enzyme 2Antiviral AgentsImmunoglobulin GAntiviral drugAntiviral therapyCOVID-19Entry inhibitorReceptor trap

Identifiers

PMID34774603
PMCPMC8579703
OpenAlexW3162695165

What OpenQuestion holds

Textmetadata
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.