Evidence map›Paper›PMID 33080267›Full record

ArticleInternational journal of biological macromolecules2020

Designed variants of ACE2-Fc that decouple anti-SARS-CoV-2 activities from unwanted cardiovascular effects.

Pan Liu, Xinfang Xie, Li Gao, Jing Jin

Open access · greenAbstract read
In one paragraph

Article in International journal of biological macromolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.5field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  9. Review
  10. Human gene therapy · 2022
    Article
  11. Article
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  14. Review
  15. Article
  16. Article
  17. Reply to Liu et al.: Specific mutations matter in specificity and catalysis in ACE2.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. His345 mutant of angiotensin-converting enzyme 2 (ACE2) remains enzymatically active against angiotensin II.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
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

4 authors at 2 institutions in 2 countries.

Pan LiuFeinberg Cardiovascular and Renal Research Institute, Department of Medicine-Nephrology and Hypertension, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Xinfang XieFeinberg Cardiovascular and Renal Research Institute, Department of Medicine-Nephrology and Hypertension, Northwestern University Feinberg School of Medicine, Chicago, IL, USA; Department of Nephrology, The First Affiliated Hospital of Medical College, Xi'an Jiaotong University, Xi'an, China.
Li GaoFeinberg Cardiovascular and Renal Research Institute, Department of Medicine-Nephrology and Hypertension, Northwestern University Feinberg School of Medicine, Chicago, IL, USA; Department of Nephrology, The First Affiliated Hospital of Medical College, Xi'an Jiaotong University, Xi'an, China.
Jing JinFeinberg Cardiovascular and Renal Research Institute, Department of Medicine-Nephrology and Hypertension, Northwestern University Feinberg School of Medicine, Chicago, IL, USA. Electronic address: jing.jin@northwestern.edu.
Northwestern University · USFirst Affiliated Hospital of Xi'an Jiaotong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Angiotensin-converting enzyme 2 (ACE2) is the entry receptor for SARS-CoV-2, and recombinant ACE2 decoys are being evaluated as new antiviral therapies. We designed and tested an antibody-like ACE2-Fc fusion protein, which has the benefit of long pharmacological half-life and the potential to facilitate immune clearance of the virus. Out of a concern that the intrinsic catalytic activity of ACE2 may unintentionally alter the balance of its hormonal substrates and cause adverse cardiovascular effects in treatment, we performed a mutagenesis screening for inactivating the enzyme. Three mutants, R273A, H378A and E402A, completely lost their enzymatic activity for either surrogate or physiological substrates. All of them remained capable of binding SARS-CoV-2 and could suppress the transduction of a pseudotyped virus in cell culture. This study established new ACE2-Fc candidates as antiviral treatment for SARS-CoV-2 without potentially harmful side effects from ACE2's catalytic actions toward its vasoactive substrates.

Indexed as

Angiotensin-Converting Enzyme 2COVID-19COVID-19 Drug TreatmentImmunoglobulin Fc FragmentsRecombinant Fusion ProteinsAmino Acid SubstitutionAnimalsCell LineFemaleHumansMiceMice, Inbred BALB CMutation, MissenseSARS-CoV-2ACE2 protein, humanAngiotensin-Converting Enzyme 2Immunoglobulin Fc FragmentsRecombinant Fusion ProteinsACE2-FcCOVID-19MutagenesisSARS-CoV-2

Identifiers

PMID33080267
PMCPMC7568492
OpenAlexW3092975157

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.