Evidence map›Paper›PMID 38041113›Full record

ArticleVirology journal2023

Development of a neutralization monoclonal antibody with a broad neutralizing effect against SARS-CoV-2 variants.

Hae Li Ko, Deuk-Ki Lee, Younghyeon Kim, Hui Jeong Jang, Youn Woo Lee, Ho-Young Lee, Sang-Hyuk Seok, Jun Won Park, Jin-Kyung Limb, Da In On and 7 more

Open access · goldAbstract read
In one paragraph

Article in Virology journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 28% 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

4 citing papers in PubMed, 1 synthesis or guideline pooled it, 4 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. 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

17 authors at 6 institutions in 3 countries.

Hae Li Ko *Division of Research Program, Scripps Korea Antibody Institute, Chuncheon, 24341, Republic of Korea.
Deuk-Ki Lee *Division of Research Program, Scripps Korea Antibody Institute, Chuncheon, 24341, Republic of Korea.
Younghyeon KimDivision of Research Program, Scripps Korea Antibody Institute, Chuncheon, 24341, Republic of Korea.
Hui Jeong JangDepartment of Nuclear Medicine, Seoul National University Bundang Hospital, Seongnam-si, Gyeonggi-do, 13620, South Korea.
Youn Woo LeeDepartment of Nuclear Medicine, Seoul National University Bundang Hospital, Seongnam-si, Gyeonggi-do, 13620, South Korea.
Ho-Young LeeDepartment of Nuclear Medicine, Seoul National University Bundang Hospital, Seongnam-si, Gyeonggi-do, 13620, South Korea.
Sang-Hyuk SeokDivision of Biomedical Convergence, College of Biomedical Science, Kangwon National University, Chuncheon-si, Gangwon-do, 24341, South Korea.
Jun Won ParkDivision of Biomedical Convergence, College of Biomedical Science, Kangwon National University, Chuncheon-si, Gangwon-do, 24341, South Korea.
Jin-Kyung LimbKorea Mouse Phenotyping Center (KMPC), Seoul National University, Seoul, 08826, South Korea.
Da In OnKorea Mouse Phenotyping Center (KMPC), Seoul National University, Seoul, 08826, South Korea.
Jun-Won YunLaboratory of Veterinary Toxicology, College of Veterinary Medicine, Seoul National University, Seoul, 08826, South Korea.
Kwang-Soo LyooCollege of Veterinary Medicine, Jeonbuk National University, Iksan, 54596, Republic of Korea.
Daesub SongDepartment of Veterinary Medicine Virology Laboratory, College of Veterinary Medicine and Research Institute for Veterinary Science, Seoul National University, Seoul, 08826, Republic of Korea.
Minjoo YeomDepartment of Veterinary Medicine Virology Laboratory, College of Veterinary Medicine and Research Institute for Veterinary Science, Seoul National University, Seoul, 08826, Republic of Korea.
Hanbyeul LeeDepartment of Veterinary Medicine Virology Laboratory, College of Veterinary Medicine and Research Institute for Veterinary Science, Seoul National University, Seoul, 08826, Republic of Korea.
Je Kyung SeongKorea Mouse Phenotyping Center (KMPC), Seoul National University, Seoul, 08826, South Korea. sunmouse@snu.ac.kr.
Sungjin LeeDivision of Research Program, Scripps Korea Antibody Institute, Chuncheon, 24341, Republic of Korea. sjlee@skai.or.kr.
Seoul National University · KRScripps Korea Antibody Institute · KRSeoul National University Bundang Hospital · KRKangwon National University · KRJeonbuk National University · KRNational University College · PR

Funding

National Research Foundation of Korea NRF-2014M3A9D5A01075128National Research Foundation of Korea NRF-2021R1F1A1055906Science and Industrial Technology in Gwangwon-do 2022-DD-UP-0287
6 · The paper itself

Abstract

backgroundThe emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants has challenged the effectiveness of current therapeutic regimens. Here, we aimed to develop a potent SARS-CoV-2 antibody with broad neutralizing effect by screening a scFv library with the spike protein receptor-binding domain (RBD) via phage display.

methodsSKAI-DS84 was identified through phage display, and we performed pseudovirus neutralization assays, authentic virus neutralization assays, and in vivo neutralization efficacy evaluations. Furthermore, surface plasmon resonance (SPR) analysis was conducted to assess the physical characteristics of the antibody, including binding kinetics and measure its affinity for variant RBDs.

resultsThe selected clones were converted to human IgG, and among them, SKAI-DS84 was selected for further analyses based on its binding affinity with the variant RBDs. Using pseudoviruses, we confirmed that SKAI-DS84 was strongly neutralizing against wild-type, B.1.617.2, B.1.1.529, and subvariants of SARS-CoV-2. We also tested the neutralizing effect of SKAI-DS84 on authentic viruses, in vivo and observed a reduction in viral replication and improved lung pathology. We performed binding and epitope mapping experiments to understand the mechanisms underlying neutralization and identified quaternary epitopes formed by the interaction between RBDs as the target of SKAI-DS84.

conclusionsWe identified, produced, and tested the neutralizing effect of SKAI-DS84 antibody. Our results highlight that SKAI-DS84 could be a potential neutralizing antibody against SARS-CoV-2 and its variants.

Indexed as

COVID-19SARS-CoV-2Antibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralHumansNeutralization TestsReceptors, VirusSpike Glycoprotein, CoronavirusAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralReceptors, VirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2AntibodyCOVID-19Human angiotensin-converting enzyme 2Quaternary epitopes of RBDSevere acute respiratory syndrome coronavirus 2Single-chain fragment variableVariant of concern

Identifiers

PMID38041113
PMCPMC10693169
OpenAlexW4389222273

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.