Evidence map›Paper›PMID 37626059›Full record

ArticleNature communications2023

Structural and functional insights into the modulation of T cell costimulation by monkeypox virus protein M2.

Shangyu Yang, Yong Wang, Feiyang Yu, Rao Cheng, Yiwei Zhang, Dan Zhou, Xuanxiu Ren, Zengqin Deng, Haiyan Zhao

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

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  11. Methods to Study Poxvirus Structures by Cryo-EM Imaging Modalities.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
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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

9 authors at 2 institutions in 1 country.

Shangyu Yang *State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, China.
Yong Wang *Center for Antiviral Research, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.
Feiyang Yu *State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, China.
Rao ChengState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, China.
Yiwei ZhangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, China.
Dan ZhouState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, China.
Xuanxiu RenState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, China.
Zengqin DengCenter for Antiviral Research, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China. dengzengqin@wh.iov.cn.ORCID http://orcid.org/0000-0002-5658-2068
Haiyan ZhaoState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, China. haiyzhao@whu.edu.cn.ORCID http://orcid.org/0000-0001-5123-5537
Wuhan University · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rapid spread of monkeypox in multiple countries has resulted in a global public health threat and has caused international concerns since May 2022. Poxvirus encoded M2 protein is a member of the poxvirus immune evasion family and plays roles in host immunomodulation via the regulation of innate immune response mediated by the NF-κB pathway and adaptive immune response mediated by B7 ligands. However, the interaction of monkeypox virus (MPXV) M2 with B7 ligands and structural insight into poxviral M2 function have remained elusive. Here we reveal that MPXV M2, co-existing as a hexamer and a heptamer, recognizes human B7.1 and B7.2 (hB7.1/2) with high avidities. The binding of oligomeric MPXV M2 interrupts the interactions of hB7.1/2 with CD28 and CTLA4 and subverts T cell activation mediated by B7.1/2 costimulatory signals. Cryo-EM structures of M2 in complex with hB7.1/2 show that M2 binds to the shallow concave face of hB7.1/2 and displays sterically competition with CD28 and CTLA4 for the binding to hB7.1/2. Our findings provide structural mechanisms of poxviral M2 function and immune evasion deployed by poxviruses.

Indexed as

Mpox, MonkeypoxPoxviridaeCD28 AntigensCTLA-4 AntigenHumansLigandsMonkeypox virusT-LymphocytesCD28 AntigensCTLA-4 AntigenLigands

Identifiers

PMID37626059
PMCPMC10457294
OpenAlexW4386167367

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.