Evidence map›Paper›PMID 35108220›Full record

ArticleThe Journal of clinical investigation2022

Ultrapotent neutralizing antibodies against SARS-CoV-2 with a high degree of mutation resistance.

Jia Zou, Li Li, Peiyi Zheng, Wenhua Liang, Siyi Hu, Shuaixiang Zhou, Yanqun Wang, Jincun Zhao, Daopeng Yuan, Lu Liu and 24 more

Open access · goldAbstract read
In one paragraph

Article in The Journal of clinical investigation, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
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  5. Article
  6. SARS-CoV-2 and gastrointestinal diseases.Frontiers in microbiology · 2023
    Review
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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

34 authors at 7 institutions in 1 country.

Jia ZouGuangzhou Laboratory, Guangzhou International Biotech Island, Guangzhou, China.
Li LiInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Peiyi ZhengHefei National Laboratory for Physical Sciences at Microscale, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Basic Medical Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.
Wenhua LiangGuangzhou Laboratory, Guangzhou International Biotech Island, Guangzhou, China.
Siyi HuInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Shuaixiang ZhouInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Yanqun WangGuangzhou Laboratory, Guangzhou International Biotech Island, Guangzhou, China.
Jincun ZhaoGuangzhou Laboratory, Guangzhou International Biotech Island, Guangzhou, China.
Daopeng YuanInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Lu LiuInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Dongdong WuInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Mengqiu XuInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Fangfang ZhangInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Mengzhu ZhuInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Zhihai WuInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Xiaochao CaoInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Meng NiInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Xiaomin LingInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Yue WuInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Zhihui KuangInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Moyan HuInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Jianfeng LiInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Xue LiInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Xiling GuoJiangsu Provincial Center for Disease Control and Prevention, Nanjing, China.
Tianmin XuDepartment of Infectious Diseases, The Third People's Hospital of Changzhou, Changzhou, China.
Haiping JiangDepartment of Medical Oncology, First Affiliated Hospital, College of Medicine, Zhejiang University, Hangzhou, Zhejiang Province, China.
Changshou GaoInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Michael YuInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Junjian LiuInnovent Biologics (Suzhou) Co., Ltd., Suzhou, Jiangsu, China.
Nanshan ZhongGuangzhou Laboratory, Guangzhou International Biotech Island, Guangzhou, China.
Jianfeng ZhouDepartment of Hematology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Jian-An HuangDepartment of Pulmonary and Critical Care Medicine, The First Affiliated Hospital of Soochow University, Suzhou, China.
Tengchuan JinHefei National Laboratory for Physical Sciences at Microscale, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Basic Medical Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.
Jianxing HeGuangzhou Laboratory, Guangzhou International Biotech Island, Guangzhou, China.
Guangzhou Experimental Station · CNUniversity of Science and Technology of China · CNChangzhou Third People's Hospital · CNJiangsu Provincial Center for Disease Control and Prevention · CNSoochow University · CNTongji Hospital · CNZhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many SARS-CoV-2 neutralizing antibodies (nAbs) lose potency against variants of concern. In this study, we developed 2 strategies to produce mutation-resistant antibodies. First, a yeast library expressing mutant receptor binding domains (RBDs) of the spike protein was utilized to screen for potent nAbs that are least susceptible to viral escape. Among the candidate antibodies, P5-22 displayed ultrahigh potency for virus neutralization as well as an outstanding mutation resistance profile. Additionally, P14-44 and P15-16 were recognized as mutation-resistant antibodies with broad betacoronavirus neutralization properties. P15-16 has only 1 binding hotspot, which is K378 in the RBD of SARS-CoV-2. The crystal structure of the P5-22, P14-44, and RBD ternary complex clarified the unique mechanisms that underlie the excellent mutation resistance profiles of these antibodies. Secondly, polymeric IgG enhanced antibody avidity by eliminating P5-22's only hotspot, residue F486 in the RBD, thereby potently blocking cell entry by mutant viruses. Structural and functional analyses of antibodies screened using both potency assays and the yeast RBD library revealed rare, ultrapotent, mutation-resistant nAbs against SARS-CoV-2.

Indexed as

AnimalsAntibodies, NeutralizingAntibodies, ViralAntibody AffinityBinding SitesB-LymphocytesBroadly Neutralizing AntibodiesCloning, MolecularCOVID-19COVID-19 SerotherapyDisease Models, AnimalHumansImmunization, PassiveImmunoglobulin GIn Vitro TechniquesLungAntibodies, NeutralizingAntibodies, ViralBroadly Neutralizing AntibodiesImmunoglobulin Gpolymeric IgGReceptors, VirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2COVID-19Drug screensDrug therapyPharmacology

Identifiers

PMID35108220
PMCPMC8843702
OpenAlexW4210765438

What OpenQuestion holds

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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.