Evidence map›Paper›PMID 28060938›Full record

ArticlePLoS pathogens2017

EV71 3D Protein Binds with NLRP3 and Enhances the Assembly of Inflammasome Complex.

Wenbiao Wang, Feng Xiao, Pin Wan, Pan Pan, Yecheng Zhang, Fang Liu, Kailang Wu, Yingle Liu, Jianguo Wu

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

78 citing papers in PubMed, 115 citations in OpenAlex.

  1. Review
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  4. The Neglected Role of GSDMD C-Terminal in Counteracting Type I Interferon Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Wenbiao WangState Key Laboratory of Virology and College of Life Sciences, Wuhan University, Wuhan, China.
Feng XiaoState Key Laboratory of Virology and College of Life Sciences, Wuhan University, Wuhan, China.
Pin WanState Key Laboratory of Virology and College of Life Sciences, Wuhan University, Wuhan, China.
Pan PanState Key Laboratory of Virology and College of Life Sciences, Wuhan University, Wuhan, China.
Yecheng ZhangState Key Laboratory of Virology and College of Life Sciences, Wuhan University, Wuhan, China.
Fang LiuState Key Laboratory of Virology and College of Life Sciences, Wuhan University, Wuhan, China.ORCID 0000-0003-0972-9968
Kailang WuState Key Laboratory of Virology and College of Life Sciences, Wuhan University, Wuhan, China.
Yingle LiuState Key Laboratory of Virology and College of Life Sciences, Wuhan University, Wuhan, China.
Jianguo WuState Key Laboratory of Virology and College of Life Sciences, Wuhan University, Wuhan, China.
Wuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of NLRP3 inflammasome is important for effective host defense against invading pathogen. Together with apoptosis-associated speck-like protein containing CARD domain (ASC), NLRP3 induces the cleavage of caspase-1 to facilitate the maturation of interleukin-1beta (IL-1β), an important pro-inflammatory cytokine. IL-1β subsequently plays critical roles in inflammatory responses by activating immune cells and inducing many secondary pro-inflammatory cytokines. Although the role of NLRP3 inflammasome in immune response is well defined, the mechanism underlying its assembly modulated by pathogen infection remains largely unknown. Here, we identified a novel mechanism by which enterovirus 71 (EV71) facilitates the assembly of NLRP3 inflammasome. Our results show that EV71 induces production and secretion of IL-1β in macrophages and peripheral blood mononuclear cells (PBMCs) through activation of NLRP3 inflammasome. EV71 replication and protein synthesis are required for NLRP3-mediated activation of IL-1β. Interestingly, EV71 3D protein, a RNA-dependent RNA polymerase (RdRp) was found to stimulate the activation of NLRP3 inflammasome, the cleavage of pro-caspase-1, and the release of IL-1β through direct binding to NLRP3. More importantly, 3D interacts with NLRP3 to facilitate the assembly of inflammasome complex by forming a 3D-NLRP3-ASC ring-like structure, resulting in the activation of IL-1β. These findings demonstrate a new role of 3D as an important player in the activation of inflammatory response, and identify a novel mechanism underlying the modulation of inflammasome assembly and function induced by pathogen invasion.

Indexed as

CARD Signaling Adaptor ProteinsCaspase 1Cell Line, TumorCytoskeletal ProteinsEnterovirus A, HumanEnterovirus InfectionsEnzyme ActivationHEK293 CellsHumansInflammasomesInterleukin-1betaLeukocytes, MononuclearMacrophagesNLR Family, Pyrin Domain-Containing 3 ProteinProtein BindingRNA-Dependent RNA PolymeraseCARD Signaling Adaptor ProteinsCaspase 1Cytoskeletal ProteinsIL1B protein, humanInflammasomesInterleukin-1betaNLR Family, Pyrin Domain-Containing 3 ProteinNLRP3 protein, humanPYCARD protein, humanRNA-Dependent RNA PolymeraseViral Nonstructural Proteins

Identifiers

PMID28060938
PMCPMC5245909
OpenAlexW2567835140

What OpenQuestion holds

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LicenceCC BY
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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.