Evidence map›Paper›PMID 42467734›Full record

ArticlePLoS neglected tropical diseases2026

Ephrin B2 and Ephrin B3 are receptors for a novel putative henipavirus with zoonotic potential.

Guimin Dai, Shuang Yao, Wenjie Chen, Jinge Zhang, Xiaoyu Du, Yan Zhao, Zhenming Jin, Guigen Zhang

Abstract read
In one paragraph

Article in PLoS neglected tropical diseases, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Guimin DaiInstitute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, China.
Shuang YaoDepartment of Otolaryngology Head and Neck Surgery, Beijing Tongren Hospital, Capital Medical University, Beijing, China.
Wenjie ChenInstitute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, China.
Jinge ZhangHunan Research Center of the Basic Discipline for Cell Signaling, College of Biology, Hunan University, Changsha, China.
Xiaoyu DuHunan Research Center of the Basic Discipline for Cell Signaling, College of Biology, Hunan University, Changsha, China.
Yan ZhaoDepartment of Otolaryngology Head and Neck Surgery, Beijing Tongren Hospital, Capital Medical University, Beijing, China.
Zhenming JinHunan Research Center of the Basic Discipline for Cell Signaling, College of Biology, Hunan University, Changsha, China.
Guigen ZhangInstitute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, China.ORCID https://orcid.org/0000-0002-3336-6768

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Next-generation sequencing has accelerated the discovery of novel putative viruses in wildlife reservoirs, while identifying those with zoonotic potential remains challenging. In this study, we report the identification and characterization of Ailong virus, a novel putative henipavirus from previous bat metagenomes in China that utilizes human ephrin B2 (EFNB2) and EFNB3 as functional receptors. Using an integrated approach combining phylogenetic analysis, pseudotyped virus entry assays, antibody blockade assays, and structural modeling, we demonstrate that Ailong virus glycoprotein binds human EFNB2 and EFNB3 with high specificity, mediating pseudovirus entry into both human neuronal and respiratory epithelial cells. Structural analysis revealed the Ailong virus glycoprotein-EFNB2 interface closely resembling that of Nipah virus (NiV), with conservation of all critical receptor-binding residues. Moreover, AiV encodes an exceptionally large phosphoprotein, 1,033 amino acids in length, which is larger than any other known phosphoprotein in the subfamily Paramyxoviridae. Given its receptor usage, structural similarities to NiV, and efficient entry in human airway epithelia, Ailong virus is believed to pose a spillover risk.

Indexed as

Ephrin-B2Ephrin-B3HenipavirusReceptors, VirusAnimalsCell LineChinaChiropteraHumansModels, MolecularPhylogenyProtein BindingVirus InternalizationEphrin-B2Ephrin-B3Receptors, Virus

Identifiers

PMID42467734
PMCPMC13421762

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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.