Evidence map›Paper›PMID 33235207›Full record

ArticleNature communications2020

Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses.

Chao Su, Lili Wu, Yan Chai, Jianxun Qi, Shuguang Tan, George F Gao, Hao Song, Jinghua Yan

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

33 citing papers in PubMed, 46 citations in OpenAlex.

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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

8 authors at 3 institutions in 2 countries.

Chao SuCollege of Veterinary Medicine, China Agricultural University, Beijing, 100193, China.ORCID 0000-0002-5824-7968
Lili WuCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Yan ChaiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Jianxun QiUniversity of Chinese Academy of Sciences, Beijing, 100049, China.
Shuguang TanCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
George F GaoCollege of Veterinary Medicine, China Agricultural University, Beijing, 100193, China. gaof@im.ac.cn.ORCID 0000-0002-3869-615X
Hao SongResearch Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing, 100101, China. songhao@im.ac.cn.ORCID 0000-0002-2811-0370
Jinghua YanCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. yanjh@im.ac.cn.ORCID 0000-0003-0502-3829
Chinese Academy of Sciences · CNChina Agricultural University · CNComputer Network Information Center · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human γ-herpesviruses Kaposi sarcoma associated herpesvirus (KSHV) and Epstein-Barr virus (EBV) are associated with many human malignancies. Viral glycoprotein H (gH) and glycoprotein L (gL) are crucial for the cell tropism by binding to specific receptors. Recently, EphA2 was identified as the specific entry receptor for both KSHV and EBV. Here, we characterized the crystal structures of KSHV gHgL or EBV gHgL in complex with the ligand binding domain (LBD) of EphA2. Both KSHV and EBV gHgL bind to the channel and peripheral regions of LBD primarily using gL. Extensive interactions with more contacts contribute to the higher affinity of KSHV gHgL to LBD than that of EBV gHgL. These binding characteristics were verified using cell-based fusion assays with mutations in key EphA2 residues. Our experiments suggest that multiple animal γ-herpesviruses could use EphA2 as an entry receptor, implying a potential threat to human health.

Indexed as

Crystallography, X-RayGammaherpesvirinaeHerpesvirus 4, HumanHerpesvirus 8, HumanHost Microbial InteractionsMembrane GlycoproteinsMolecular ChaperonesProtein BindingReceptor, EphA2Viral Envelope ProteinsViral ProteinsVirus Internalizationglycoprotein L, Human herpesvirus 4Membrane GlycoproteinsMolecular ChaperonesReceptor, EphA2Viral Envelope ProteinsViral Proteins

Identifiers

PMID33235207
PMCPMC7687889
OpenAlexW3109985685

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.