Evidence map›Paper›PMID 30936489›Full record

ArticleNature microbiology2019

Neutralization mechanism of human monoclonal antibodies against Rift Valley fever virus.

Qihui Wang, Tong Ma, Yan Wu, Zhihai Chen, Hui Zeng, Zhou Tong, Feng Gao, Jianxun Qi, Zhennan Zhao, Yan Chai and 17 more

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Nature microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

49 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  7. Cryo-EM structure of the Rift Valley fever virus envelope protein in complex with a potent neutralization antibody.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  12. Review
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  14. Review
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  16. Bispecific antibodies targeting two glycoproteins on SFTSV exhibit synergistic neutralization and protection in a mouse model.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Humoral immunity to phlebovirus infection.Annals of the New York Academy of Sciences · 2023
    Review
  19. Article
  20. Article
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

27 authors at 8 institutions in 4 countries.

Qihui Wang *CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0003-3768-0401
Tong Ma *CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0001-5358-6023
Yan Wu *Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen, China.
Zhihai Chen *Center of Infectious Disease, Beijing Ditan Hospital, Capital Medical University, Beijing, China.ORCID http://orcid.org/0000-0001-6481-4781
Hui ZengBeijing Key Laboratory of Emerging Infectious Diseases, Institute of Infectious Diseases, Beijing Ditan Hospital, Capital Medical University, Beijing, China.
Zhou TongCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
Feng GaoInstitute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
Jianxun QiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
Zhennan ZhaoCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-7500-1222
Yan ChaiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
Huabing YangCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0003-0987-994X
Gary WongDépartement de Microbiologie-Infectiologie et d'Immunologie, Université Laval, Quebec, Quebec, Canada.
Yuhai BiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-5595-363X
Lili WuCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-6749-1727
Rui ShiCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0001-8469-8730
Mi YangCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0001-6842-2769
Jian SongCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0003-2004-9250
Haihai JiangCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-1895-3040
Zhiqiang AnTexas Therapeutics Institute, Brown Foundation Institute of Molecular Medicine, University of Texas Health Science Center at Houston, Houston, TX, USA.
Junzhi WangKey Laboratory of the Ministry of Health for Research on Quality and Standardization of Biotech Products, National Institutes for Food and Drug Control, Beijing, China.
Tilahun D YilmaInternational Laboratory of Molecular Biology for Tropical Disease Agents, School of Veterinary Medicine, University of California, Davis, Davis, CA, USA.
Yi ShiShenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen, China.ORCID http://orcid.org/0000-0002-3053-2687
William J LiuNational Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing, China.
Mifang LiangNational Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing, China.
Chuan QinKey Laboratory of Human Diseases Comparative Medicine, Ministry of Health, Institute of Medical Laboratory Animal Science, Chinese Academy of Medical Sciences, Beijing, China.
George F GaoShenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen, China. gaof@im.ac.cn.ORCID http://orcid.org/0000-0002-3869-615X
Jinghua YanCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China. yanjh@im.ac.cn.ORCID http://orcid.org/0000-0003-0502-3829
Chinese Academy of Sciences · CNAnhui University · CNCapital Medical University · CNChinese Center For Disease Control and Prevention · CNBrown Foundation · USChinese Academy of Medical Sciences & Peking Union Medical College · CNNational Institutes for Food and Drug Control · CNUniversity of California, Davis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rift Valley fever virus (RVFV) is a mosquito-borne pathogen that causes substantial morbidity and mortality in livestock and humans. To date, there are no licensed human vaccines or therapeutics available. Here, we report the isolation of monoclonal antibodies from a convalescent patient, targeting the RVFV envelope proteins Gn and Gc. The Gn-specific monoclonal antibodies exhibited much higher neutralizing activities in vitro and protection efficacies in mice against RVFV infection, compared to the Gc-specific monoclonal antibodies. The Gn monoclonal antibodies were found to interfere with soluble Gn binding to cells and prevent infection by blocking the attachment of virions to host cells. Structural analysis of Gn complexed with four Gn-specific monoclonal antibodies resulted in the definition of three antigenic patches (A, B and C) on Gn domain I. Both patches A and B are major neutralizing epitopes. Our results highlight the potential of antibody-based therapeutics and provide a structure-based rationale for designing vaccines against RVFV.

Indexed as

AnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralChlorocebus aethiopsCrystallography, X-RayEpitopesFemaleHumansMice, Inbred BALB CNeutralization TestsProtein DomainsRift Valley FeverRift Valley fever virusVero CellsViral Envelope ProteinsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesViral Envelope Proteins

Identifiers

PMID30936489
OpenAlexW2932902987

What OpenQuestion holds

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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.