Evidence map›Paper›PMID 38773072›Full record

ArticleNature communications2024

A potent Henipavirus cross-neutralizing antibody reveals a dynamic fusion-triggering pattern of the G-tetramer.

Pengfei Fan, Mengmeng Sun, Xinghai Zhang, Huajun Zhang, Yujiao Liu, Yanfeng Yao, Ming Li, Ting Fang, Bingjie Sun, Zhengshan Chen and 16 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
–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, 1 synthesis or guideline pooled it.

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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

26 authors.

Pengfei Fan *Laboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China. fanpengfei93@163.com.ORCID http://orcid.org/0000-0002-7212-231X
Mengmeng Sun *Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.
Xinghai Zhang *State Key Laboratory of Virology, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, China.
Huajun ZhangState Key Laboratory of Virology, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, China.ORCID http://orcid.org/0000-0001-8161-3949
Yujiao LiuLaboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China.
Yanfeng YaoState Key Laboratory of Virology, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, China.ORCID http://orcid.org/0000-0002-6175-8590
Ming LiDivision of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.
Ting FangLaboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China.
Bingjie SunLaboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China.
Zhengshan ChenLaboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China.
Xiangyang ChiLaboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China.
Li ChenState Key Laboratory of Virology, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, China.ORCID http://orcid.org/0009-0005-6304-9738
Cheng PengState Key Laboratory of Virology, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, China.
Zhen ChenState Key Laboratory of Virology, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, China.
Guanying ZhangLaboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China.
Yi RenLaboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China.
Zixuan LiuLaboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China.
Yaohui LiLaboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China.
Jianmin LiLaboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China.
Entao LiDivision of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.
Wuxiang GuanState Key Laboratory of Virology, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, China.
Shanshan LiDivision of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.ORCID http://orcid.org/0000-0002-7041-5960
Rui GongState Key Laboratory of Virology, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, China. gongr@wh.iov.cn.ORCID http://orcid.org/0000-0001-9222-5642
Kaiming ZhangDivision of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China. kmzhang@ustc.edu.cn.ORCID http://orcid.org/0000-0003-0414-4776
Changming YuLaboratory of Advanced Biotechnology, Institute of Biotechnology, Beijing, China. yuchangming@126.com.ORCID http://orcid.org/0000-0002-0304-4477
Sandra ChiuDivision of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China. qiux@ustc.edu.cn.ORCID http://orcid.org/0000-0001-9034-5755

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Hendra and Nipah viruses (HNVs) are highly pathogenic pathogens without approved interventions for human use. In addition, the interaction pattern between the attachment (G) and fusion (F) glycoproteins required for virus entry remains unclear. Here, we isolate a panel of Macaca-derived G-specific antibodies that cross-neutralize HNVs via multiple mechanisms. The most potent antibody, 1E5, confers adequate protection against the Nipah virus challenge in female hamsters. Crystallography demonstrates that 1E5 has a highly similar binding pattern to the receptor. In cryo-electron microscopy studies, the tendency of 1E5 to bind to the upper or lower heads results in two distinct quaternary structures of G. Furthermore, we identify the extended outer loop β1S2-β1S3 of G and two pockets on the apical region of fusion (F) glycoprotein as the essential sites for G-F interactions. This work highlights promising drug candidates against HNVs and contributes deeper insights into the viruses.

Indexed as

Antibodies, NeutralizingAntibodies, ViralCryoelectron MicroscopyHenipavirus InfectionsViral Fusion ProteinsAnimalsCricetinaeCross ReactionsCrystallography, X-RayFemaleHendra VirusHenipavirusHumansMacacaMesocricetusNipah VirusAntibodies, NeutralizingAntibodies, Viralattachment protein GViral Envelope ProteinsViral Fusion Proteins

Identifiers

PMID38773072
PMCPMC11109247

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.