Evidence map›Paper›PMID 36109569›Full record

ArticleScientific reports2022

Isolation of a human SARS-CoV-2 neutralizing antibody from a synthetic phage library and its conversion to fluorescent biosensors.

Haimei Li, Bo Zhu, Baowei Li, Limei Chen, Xuerao Ning, Hang Dong, Jingru Liang, Xueying Yang, Jinhua Dong, Hiroshi Ueda

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

8 citing papers in PubMed, 11 citations in OpenAlex.

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  7. VSensors (Basel, Switzerland) · 2023
    Article
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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

10 authors at 4 institutions in 2 countries.

Haimei Li *Weifang Key Laboratory for Antibodies Medicine, School of Life Science and Technology, Weifang Medical University, Weifang, China.
Bo Zhu *Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.
Baowei LiWeifang Key Laboratory for Antibodies Medicine, School of Life Science and Technology, Weifang Medical University, Weifang, China.
Limei ChenWeifang Key Laboratory for Antibodies Medicine, School of Life Science and Technology, Weifang Medical University, Weifang, China.
Xuerao NingLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.
Hang DongSchool of Basic Medical Sciences, Peking University, Beijing, China.
Jingru LiangWeifang Key Laboratory for Antibodies Medicine, School of Life Science and Technology, Weifang Medical University, Weifang, China.
Xueying YangWeifang Key Laboratory for Antibodies Medicine, School of Life Science and Technology, Weifang Medical University, Weifang, China.
Jinhua DongWeifang Key Laboratory for Antibodies Medicine, School of Life Science and Technology, Weifang Medical University, Weifang, China. dongjh@wfmc.edu.cn.
Hiroshi UedaLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan. ueda@res.titech.ac.jp.
Weifang Medical University · CNLife Science Institute · JPPeking University · CNTokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Since late 2019, the outbreak of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and the resultant spread of COVID-19 have given rise to a worldwide health crisis that is posing great challenges to public health and clinical treatment, in addition to serving as a formidable threat to the global economy. To obtain an effective tool to prevent and diagnose viral infections, we attempted to obtain human antibody fragments that can effectively neutralize viral infection and be utilized for rapid virus detection. To this end, several human monoclonal antibodies were isolated by bio-panning a phage-displayed human antibody library, Tomlinson I. The selected clones were demonstrated to bind to the S1 domain of the spike glycoprotein of SARS-CoV-2. Moreover, clone A7 in Fab and IgG formats were found to effectively neutralize the binding of S protein to angiotensin-converting enzyme 2 in the low nM range. In addition, this clone was successfully converted to quench-based fluorescent immunosensors (Quenchbodies) that allowed antigen detection within a few minutes, with the help of a handy fluorometer.

Indexed as

BacteriophagesBiosensing TechniquesCOVID-19Angiotensin-Converting Enzyme 2Antibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralHumansImmunoassayImmunoglobulin FragmentsImmunoglobulin GMembrane GlycoproteinsPeptide LibrarySARS-CoV-2Spike Glycoprotein, CoronavirusViral Envelope ProteinsAngiotensin-Converting Enzyme 2Antibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralImmunoglobulin FragmentsImmunoglobulin GMembrane GlycoproteinsPeptide LibrarySpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Viral Envelope Proteins

Identifiers

PMID36109569
PMCPMC9476436
OpenAlexW4295926719

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.