Evidence map›Paper›PMID 36528147›Full record

ArticleInternational journal of biological macromolecules2023

Human antibody BD-218 has broad neutralizing activity against concerning variants of SARS-CoV-2.

Bo Wang, Hua Xu, Zi-Teng Liang, Tian-Ning Zhao, Xin Zhang, Tian-Bo Peng, You-Chun Wang, Xiao-Dong Su

Open access · greenAbstract read
In one paragraph

Article in International journal of biological macromolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

8 authors at 2 institutions in 1 country.

Bo WangState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, China.
Hua XuState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, China.
Zi-Teng LiangDivision of HIV/AIDS and Sex-transmitted Virus Vaccines, Institute for Biological Product Control, National Institutes for Food and Drug Control (NIFDC), WHO Collaborating Center for Standardization and Evaluation of Biologicals, Beijing, China.
Tian-Ning ZhaoState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, China.
Xin ZhangState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, China.
Tian-Bo PengState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, China.
You-Chun WangDivision of HIV/AIDS and Sex-transmitted Virus Vaccines, Institute for Biological Product Control, National Institutes for Food and Drug Control (NIFDC), WHO Collaborating Center for Standardization and Evaluation of Biologicals, Beijing, China.
Xiao-Dong SuState Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, China. Electronic address: xdsu@pku.edu.cn.
Peking University · CNNational Institutes for Food and Drug Control · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As SARS-CoV-2 variants of concern (VOC) reduce the effectiveness of existing anti-COVID therapeutics, it is increasingly critical to identify highly potent neutralizing antibodies (nAbs) that bind to conserved regions across multiple variants, especially beta, delta, and omicron variants. Using single-cell sequencing with biochemical methods and pseudo-typed virus neutralization experiments, here we report the characterization of a potent nAb BD-218, identified from an early screen of patients recovering from the original virus. We have determined the cryo-EM structure of the BD-218/spike protein complex to define its epitope in detail, which revealed that BD-218 interacts with a novel epitope on the receptor-binding domain (RBD) of the spike protein. We concluded that BD-218 is a highly effective and broadly active nAb against SARS-CoV-2 variants with promising potential for therapeutic development.

Indexed as

COVID-19SARS-CoV-2Antibodies, NeutralizingAntibodies, ViralEpitopesHumansSpike Glycoprotein, CoronavirusAntibodies, NeutralizingAntibodies, ViralEpitopesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Neutralizing antibodySARS-CoV-2

Identifiers

PMID36528147
PMCPMC9747686
OpenAlexW4311360725

What OpenQuestion holds

Textmetadata
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.