Evidence map›Paper›PMID 38830098›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2024

Bispecific antibodies targeting two glycoproteins on SFTSV exhibit synergistic neutralization and protection in a mouse model.

Zhen Chang, Dan Gao, Liying Liao, Junqing Sun, Gen Zhang, Xue Zhang, Feiran Wang, Chunrui Li, Babayemi Olawale Oladejo, Shihua Li and 8 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 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

18 authors.

Zhen Chang *Department of Pathogen Microbiology, School of Basic Medical Sciences, Capital Medical University, Beijing 100069, China.
Dan Gao *Department of Pathogen Microbiology, School of Basic Medical Sciences, Capital Medical University, Beijing 100069, China.
Liying Liao *Department of Pathogen Microbiology, School of Basic Medical Sciences, Capital Medical University, Beijing 100069, China.ORCID 0009-0003-4150-9233
Junqing Sun *Chinese Academy of Sciences Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Gen ZhangChinese Academy of Sciences Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Xue ZhangDepartment of Pathogen Microbiology, School of Basic Medical Sciences, Capital Medical University, Beijing 100069, China.
Feiran WangChinese Academy of Sciences Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Chunrui LiChinese Academy of Sciences Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Babayemi Olawale OladejoChinese Academy of Sciences Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.ORCID 0000-0002-3284-8781
Shihua LiChinese Academy of Sciences Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Yan ChaiChinese Academy of Sciences Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Yongfei HuCollege of Veterinary Medicine, China Agricultural University, Beijing 100193, China.
Xuancheng LuNational Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Chinese Center for Disease Control and Prevention, Beijing 102206, China.ORCID 0000-0002-0452-0834
Haixia XiaoLaboratory of Protein Engineering and Vaccines, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.ORCID 0000-0003-0032-5430
Jianxun QiChinese Academy of Sciences Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.ORCID 0000-0002-9358-4732
Zhihai ChenCenter of Infectious Disease, Beijing Ditan Hospital, Capital Medical University, Beijing 100015, China.
Feng GaoLaboratory of Protein Engineering and Vaccines, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.ORCID 0000-0002-0670-010X
Yan WuDepartment of Pathogen Microbiology, School of Basic Medical Sciences, Capital Medical University, Beijing 100069, China.ORCID 0000-0003-2734-0673

Funding

MOST | National Key Research and Development Program of China (NKPs) 2020YFA0907104MOST | National Key Research and Development Program of China (NKPs) 2022YFC2303402MOST | National Natural Science Foundation of China (NSFC) 32090014MOST | National Natural Science Foundation of China (NSFC) 82022042
6 · The paper itself

Abstract

Severe fever with thrombocytopenia syndrome (SFTS) is an emerging infectious disease with a high fatality rate of up to 30% caused by SFTS virus (SFTSV). However, no specific vaccine or antiviral therapy has been approved for clinical use. To develop an effective treatment, we isolated a panel of human monoclonal antibodies (mAbs). SF5 and SF83 are two neutralizing mAbs that recognize two viral glycoproteins (Gn and Gc), respectively. We found that their epitopes are closely located, and we then engineered them as several bispecific antibodies (bsAbs). Neutralization and animal experiments indicated that bsAbs display more potent protective effects than the parental mAbs, and the cryoelectron microscopy structure of a bsAb3 Fab-Gn-Gc complex elucidated the mechanism of protection. In vivo virus passage in the presence of antibodies indicated that two bsAbs resulted in less selective pressure and could efficiently bind to all single parental mAb-escape mutants. Furthermore, epitope analysis of the protective mAbs against SFTSV and RVFV indicated that they are all located on the Gn subdomain I, where may be the hot spots in the phleboviruses. Collectively, these data provide potential therapeutic agents and molecular basis for the rational design of vaccines against SFTSV infection.

Indexed as

Antibodies, BispecificAntibodies, NeutralizingAntibodies, ViralPhlebovirusAnimalsAntibodies, MonoclonalDisease Models, AnimalEpitopesGlycoproteinsHumansMiceSevere Fever with Thrombocytopenia SyndromeAntibodies, BispecificAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesGlycoproteinsbispecific antibodybunyavirusglycoproteinsSFTSVstructural basis

Identifiers

PMID38830098
PMCPMC11181109

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.