Evidence map›Paper›PMID 35293796›Full record

ArticleMicrobiology spectrum2022

Neutralizing Monoclonal Antibodies Inhibit SARS-CoV-2 Infection through Blocking Membrane Fusion.

Chia-Jung Li, Tai-Ling Chao, Ting-Yu Chang, Chia-Chun Hsiao, De-Chao Lu, Yi-Wei Chiang, Guan-Chun Lai, Ya-Min Tsai, Jun-Tung Fang, Siman Ieong and 3 more

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.2field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 32 citations in OpenAlex.

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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

13 authors at 2 institutions in 1 country.

Chia-Jung Li *Department of Biochemical Science and Technology, College of Life Science, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.
Tai-Ling Chao *Department of Clinical Laboratory Sciences and Medical Biotechnology, College of Medicine, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.
Ting-Yu ChangDepartment of Biochemical Science and Technology, College of Life Science, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.
Chia-Chun HsiaoDepartment of Biochemical Science and Technology, College of Life Science, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.
De-Chao LuDepartment of Biochemical Science and Technology, College of Life Science, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.
Yi-Wei ChiangDepartment of Biochemical Science and Technology, College of Life Science, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.
Guan-Chun LaiDepartment of Biochemical Science and Technology, College of Life Science, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.
Ya-Min TsaiDepartment of Clinical Laboratory Sciences and Medical Biotechnology, College of Medicine, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.
Jun-Tung FangDepartment of Clinical Laboratory Sciences and Medical Biotechnology, College of Medicine, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.
Siman IeongDepartment of Clinical Laboratory Sciences and Medical Biotechnology, College of Medicine, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.
Jann-Tay WangDepartment of Internal Medicine, National Taiwan Universitygrid.19188.39 Hospital, Taipei, Taiwan.
Sui-Yuan ChangDepartment of Clinical Laboratory Sciences and Medical Biotechnology, College of Medicine, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.
Shih-Chung ChangDepartment of Biochemical Science and Technology, College of Life Science, National Taiwan Universitygrid.19188.39, Taipei, Taiwan.ORCID 0000-0002-5015-8178
National Taiwan University · TWNational Taiwan University Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most of SARS-CoV-2 neutralizing antibodies (nAbs) targeted the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein. However, mutations at RBD sequences found in the emerging SARS-CoV-2 variants greatly reduced the effectiveness of nAbs. Here we showed that four nAbs, S2-4D, S2-5D, S2-8D, and S2-4A, which recognized a conserved epitope in the S2 subunit of the S protein, can inhibit SARS-CoV-2 infection through blocking the S protein-mediated membrane fusion. Notably, these four nAbs exhibited broadly neutralizing activity against SARS-CoV-2 Alpha, Gamma, Delta, and Epsilon variants. Antisera collected from mice immunized with the identified epitope peptides of these four nAbs also exhibited potent virus neutralizing activity. Discovery of the S2-specific nAbs and their unique antigenic epitopes paves a new path for development of COVID-19 therapeutics and vaccines.

Indexed as

COVID-19SARS-CoV-2AnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesImmune SeraMembrane FusionMiceSpike Glycoprotein, CoronavirusAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesImmune SeraSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2membrane fusionneutralizing antibodiesS2 subunitSARS-CoV-2spike (S) protein

Identifiers

PMID35293796
PMCPMC9045258
OpenAlexW4221079027

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.