Evidence map›Paper›PMID 40164599›Full record

ArticleNature communications2025

Generation and characterization of neutralizing antibodies against M1R and B6R proteins of monkeypox virus.

Yuanyuan Qu, Wanbo Tai, Enhao Ma, Qiwei Jiang, Miao Fan, Wangcheng Xiao, Chongyu Tian, Yang Liu, Jianying Liu, Xinquan Wang and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

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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

12 authors.

Yuanyuan Qu *Institute of Infectious Diseases, Shenzhen Bay Laboratory, Shenzhen, Guangdong, 518132, China.
Wanbo Tai *Institute of Infectious Diseases, Shenzhen Bay Laboratory, Shenzhen, Guangdong, 518132, China.ORCID http://orcid.org/0000-0002-9864-8993
Enhao Ma *New Cornerstone Science Laboratory, Tsinghua University-Peking University Joint Center for Life Sciences, School of Basic Medical Sciences, Tsinghua University, Beijing, 100084, China.
Qiwei Jiang *Changchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences, State Key Laboratory of Pathogen and Biosecurity, Key Laboratory of Jilin Province for Zoonosis Prevention and Control, Changchun, China.
Miao FanKey Laboratory of Pathogen Infection Prevention and Control (MOE), State Key Laboratory of Respiratory Health and Multimorbidity, National Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, 102629, China.
Wangcheng XiaoInstitute of Infectious Diseases, Shenzhen Bay Laboratory, Shenzhen, Guangdong, 518132, China.
Chongyu TianInstitute of Infectious Diseases, Shenzhen Bay Laboratory, Shenzhen, Guangdong, 518132, China.
Yang LiuInstitute of Infectious Diseases, Shenzhen Bay Laboratory, Shenzhen, Guangdong, 518132, China.
Jianying LiuInstitute of Infectious Diseases, Shenzhen Bay Laboratory, Shenzhen, Guangdong, 518132, China.
Xinquan WangThe Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, Beijing, 100084, China.ORCID http://orcid.org/0000-0003-3136-8070
Jiwan GeKey Laboratory of Pathogen Infection Prevention and Control (MOE), State Key Laboratory of Respiratory Health and Multimorbidity, National Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, 102629, China. gejiwan@ipbcams.ac.cn.ORCID http://orcid.org/0000-0001-9366-1470
Gong ChengNew Cornerstone Science Laboratory, Tsinghua University-Peking University Joint Center for Life Sciences, School of Basic Medical Sciences, Tsinghua University, Beijing, 100084, China. gongcheng@mail.tsinghua.edu.cn.ORCID http://orcid.org/0000-0001-7447-5488

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The global outbreak of monkeypox virus (MPXV), combined with the termination of smallpox vaccination and the lack of specific antiviral treatments, raises increasing concerns. The surface proteins M1R and B6R of MPXV are crucial for virus transmission and serve as key targets for vaccine development. In this study, a panel of human antibodies targeting M1R and B6R is isolated from a human antibody library using phage display technology. Among these antibodies, A138 against M1R and B026 against B6R show the most potent broad-spectrum neutralizing activities against MPXV and Vaccinia virus (VACV). When used in combination, A138 and B026 exhibit complementary neutralizing activity against both viruses in vitro. X-ray crystallography reveales that A138 binds to the loop regions of M1R, similar to the vulnerable epitope of 7D11 on VACV L1R. By contrast, A129 targets a more cryptic epitope, primarily comprising the β-strands of M1R. Moreover, prophylactic and therapeutic administration of A138 or B026 alone provides partial protection, while combining these two antibodies results in enhanced protection against VACV in male C57BL/6 mice. This study demonstrates of a dual-targeting strategy using two different components of the virion for the prevention and treatment of MPXV infection.

Indexed as

Antibodies, NeutralizingAntibodies, ViralMonkeypox virusMpox, MonkeypoxViral Envelope ProteinsAnimalsCrystallography, X-RayEpitopesFemaleHumansMiceMice, Inbred BALB CVaccinia virusAntibodies, NeutralizingAntibodies, ViralEpitopesViral Envelope Proteins

Identifiers

PMID40164599
PMCPMC11958656

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Registered trials

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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.