Evidence map›Paper›PMID 35587428›Full record

ArticleEmerging microbes & infections2022

ACE2 decoy receptor generated by high-throughput saturation mutagenesis efficiently neutralizes SARS-CoV-2 and its prevalent variants.

Bolun Wang, Junxuan Zhao, Shuo Liu, Jingyuan Feng, Yufeng Luo, Xinyu He, Yanmin Wang, Feixiang Ge, Junyi Wang, Buqing Ye and 4 more

Abstract read
In one paragraph

Article in Emerging microbes & infections, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

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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

14 authors.

Bolun WangDepartment of Biomedical Engineering, Peking University, Beijing, People's Republic of China.
Junxuan ZhaoDepartment of Biomedical Engineering, Peking University, Beijing, People's Republic of China.
Shuo LiuDivision of HIV/AIDS and Sex-transmitted Virus Vaccines, Institute for Biological Product Control, National Institutes for Food and Drug Control (NIFDC), Beijing, People's Republic of China.
Jingyuan FengCollege of Chemistry, University of California Berkeley, Berkeley, CA, USA.
Yufeng LuoDepartment of Biomedical Engineering, Peking University, Beijing, People's Republic of China.
Xinyu HeDepartment of Biomedical Engineering, Peking University, Beijing, People's Republic of China.
Yanmin WangDepartment of Biomedical Engineering, Peking University, Beijing, People's Republic of China.
Feixiang GeDepartment of Biomedical Engineering, Peking University, Beijing, People's Republic of China.
Junyi WangDepartment of Biomedical Engineering, Peking University, Beijing, People's Republic of China.
Buqing YeDepartment of Biomedical Engineering, Peking University, Beijing, People's Republic of China.
Weijin HuangDivision of HIV/AIDS and Sex-transmitted Virus Vaccines, Institute for Biological Product Control, National Institutes for Food and Drug Control (NIFDC), Beijing, People's Republic of China.
Xiaochen BoInstitute of Health Service and Transfusion Medicine, Beijing, People's Republic of China.
Youchun WangDivision of HIV/AIDS and Sex-transmitted Virus Vaccines, Institute for Biological Product Control, National Institutes for Food and Drug Control (NIFDC), Beijing, People's Republic of China.ORCID 0000-0001-9769-5141
Jianzhong Jeff XiDepartment of Biomedical Engineering, Peking University, Beijing, People's Republic of China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The recent global pandemic was a spillover from the SARS-CoV-2 virus. Viral entry involves the receptor binding domain (RBD) of the viral spike protein interacting with the protease domain (PD) of the cellular receptor, ACE2. We hereby present a comprehensive mutational landscape of the effects of ACE2-PD point mutations on RBD-ACE2 binding using a saturation mutagenesis approach based on microarray-based oligo synthesis and a single-cell screening assay. We observed that changes in glycosylation sites and directly interacting sites of ACE2-PD significantly influenced ACE2-RBD binding. We further engineered an ACE2 decoy receptor with critical point mutations, D30I, L79W, T92N, N322V, and K475F, named C4-1. C4-1 shows a 200-fold increase in neutralization for the SARS-CoV-2 D614G pseudotyped virus compared to wild-type soluble ACE2 and a sevenfold increase in binding affinity to wild-type spike compared to the C-terminal Ig-Fc fused wild-type soluble ACE2. Moreover, C4-1 efficiently neutralized prevalent variants, especially the omicron variant (EC

Indexed as

COVID-19SARS-CoV-2Angiotensin-Converting Enzyme 2COVID-19 SerotherapyHumansImmunization, PassiveMutagenesisProtein BindingSpike Glycoprotein, CoronavirusAngiotensin-Converting Enzyme 2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2decoy receptorhigh-throughput screeningprotein engineeringSARS-CoV-2

Identifiers

PMID35587428
PMCPMC9176695

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Registered trials

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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.