Evidence map›Paper›PMID 36552031›Full record

ArticleBiomedicines2022

Development and Characterization of Phage-Display-Derived Novel Human Monoclonal Antibodies against the Receptor Binding Domain of SARS-CoV-2.

Ji Woong Kim, Sung Won Min, Jichul Lee, Ha Gyeong Shin, Hye Lim Choi, Ha Rim Yang, Ji Hyun Lee, Yea Bin Cho, Hyunbo Shim, Sukmook Lee

Abstract read
In one paragraph

Article in Biomedicines, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Unlocking the potential ofFrontiers in bioinformatics · 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

10 authors.

Ji Woong KimDepartment of Chemistry, Kookmin University, Seoul 02707, Republic of Korea.ORCID 0000-0002-1589-2449
Sung Won MinResearch Center, SG Medical, Seoul 05548, Republic of Korea.
Jichul LeeResearch Center, SG Medical, Seoul 05548, Republic of Korea.
Ha Gyeong ShinDepartment of Biopharmaceutical Chemistry, Kookmin University, Seoul 02707, Republic of Korea.
Hye Lim ChoiDepartment of Biopharmaceutical Chemistry, Kookmin University, Seoul 02707, Republic of Korea.
Ha Rim YangDepartment of Biopharmaceutical Chemistry, Kookmin University, Seoul 02707, Republic of Korea.
Ji Hyun LeeDepartment of Biopharmaceutical Chemistry, Kookmin University, Seoul 02707, Republic of Korea.
Yea Bin ChoDepartment of Chemistry, Kookmin University, Seoul 02707, Republic of Korea.
Hyunbo ShimDepartment of Life Sciences, Ewha Womans University, Seoul 03760, Republic of Korea.ORCID 0000-0001-8415-3976
Sukmook LeeDepartment of Chemistry, Kookmin University, Seoul 02707, Republic of Korea.

Funding

Korea Health Industry Development Institute HI22C1234National Research Foundation of Korea NRF-2019M3E5D5065844National Research Foundation of Korea NRF-2020M3A9I2107093
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has resulted in an ongoing global pandemic crisis, caused by the life-threatening illness coronavirus disease 2019 (COVID-19). Thus, the rapid development of monoclonal antibodies (mAbs) to cope with COVID-19 is urgently necessary. In this study, we used phage display to develop four human mAbs specific to the receptor-binding domain (RBD) of SARS-CoV-2. Our intensive in vitro functional analyses demonstrated that K102.1, an anti-SARS-CoV-2 RBD-specific mAb, exerted potent neutralizing activity against pseudoviral and live viral infection and the interaction between SARS-CoV-2 RBD and human angiotensin-converting enzyme 2. Monotherapy with K102.1 also revealed the therapeutic potential against SARS-CoV-2 infection in vivo. Further, this study developed a sandwich enzyme-linked immunosorbent assay with a non-competing mAb pair, K102.1 and K102.2, that accurately detected the RBDs of SARS-CoV-2 wild-type and variants with high sensitivity in the picomolar range. These findings suggest that the phage-display-based mAb selection from an established antibody library may be an effective strategy for the rapid development of mAbs against the constantly evolving SARS-CoV-2.

Indexed as

human antibodyneutralizationsandwich ELISASARS-CoV-2

Identifiers

PMID36552031
PMCPMC9775448

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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.