Evidence map›Paper›PMID 32477319›Full record

ArticleFrontiers in immunology2020

Herpes Simplex Virus 1 UL2 Inhibits the TNF-α-Mediated NF-κB Activity by Interacting With p65/p50.

Mingsheng Cai, Zongmin Liao, Xingmei Zou, Zuo Xu, Yuanfang Wang, Tong Li, Yiwen Li, Xiaowen Ou, Yangxi Deng, Yingjie Guo and 2 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

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  17. Ikzf2 Regulates the Development of ICOSFrontiers in immunology · 2021
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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

12 authors at 2 institutions in 1 country.

Mingsheng CaiGuangdong Provincial Key Laboratory of Allergy and Clinical Immunology, The Second Affiliated Hospital of Guangzhou Medical University, Sino-French Hoffmann Institute, School of Basic Medical Science, Guangzhou Medical University, Guangzhou, China.
Zongmin LiaoGuangdong Provincial Key Laboratory of Allergy and Clinical Immunology, The Second Affiliated Hospital of Guangzhou Medical University, Sino-French Hoffmann Institute, School of Basic Medical Science, Guangzhou Medical University, Guangzhou, China.
Xingmei ZouGuangdong Provincial Key Laboratory of Allergy and Clinical Immunology, The Second Affiliated Hospital of Guangzhou Medical University, Sino-French Hoffmann Institute, School of Basic Medical Science, Guangzhou Medical University, Guangzhou, China.
Zuo XuGuangdong Provincial Key Laboratory of Allergy and Clinical Immunology, The Second Affiliated Hospital of Guangzhou Medical University, Sino-French Hoffmann Institute, School of Basic Medical Science, Guangzhou Medical University, Guangzhou, China.
Yuanfang WangGuangdong Provincial Key Laboratory of Allergy and Clinical Immunology, The Second Affiliated Hospital of Guangzhou Medical University, Sino-French Hoffmann Institute, School of Basic Medical Science, Guangzhou Medical University, Guangzhou, China.
Tong LiGuangdong Provincial Key Laboratory of Allergy and Clinical Immunology, The Second Affiliated Hospital of Guangzhou Medical University, Sino-French Hoffmann Institute, School of Basic Medical Science, Guangzhou Medical University, Guangzhou, China.
Yiwen LiGuangdong Provincial Key Laboratory of Allergy and Clinical Immunology, The Second Affiliated Hospital of Guangzhou Medical University, Sino-French Hoffmann Institute, School of Basic Medical Science, Guangzhou Medical University, Guangzhou, China.
Xiaowen OuGuangdong Provincial Key Laboratory of Allergy and Clinical Immunology, The Second Affiliated Hospital of Guangzhou Medical University, Sino-French Hoffmann Institute, School of Basic Medical Science, Guangzhou Medical University, Guangzhou, China.
Yangxi DengGuangdong Provincial Key Laboratory of Allergy and Clinical Immunology, The Second Affiliated Hospital of Guangzhou Medical University, Sino-French Hoffmann Institute, School of Basic Medical Science, Guangzhou Medical University, Guangzhou, China.
Yingjie GuoGuangdong Provincial Key Laboratory of Allergy and Clinical Immunology, The Second Affiliated Hospital of Guangzhou Medical University, Sino-French Hoffmann Institute, School of Basic Medical Science, Guangzhou Medical University, Guangzhou, China.
Tao PengState Key Laboratory of Respiratory Diseases, Sino-French Hoffmann Institute, Guangzhou Medical University, Guangzhou, China.
Meili LiGuangdong Provincial Key Laboratory of Allergy and Clinical Immunology, The Second Affiliated Hospital of Guangzhou Medical University, Sino-French Hoffmann Institute, School of Basic Medical Science, Guangzhou Medical University, Guangzhou, China.
Guangzhou Medical University · CNSecond Affiliated Hospital of Guangzhou Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herpes simplex virus 1 (HSV-1) is a large double-stranded DNA virus that encodes at least 80 viral proteins, many of which are involved in the virus-host interaction and are beneficial to the viral survival and reproduction. However, the biological functions of some HSV-1-encoded proteins are not fully understood. Nuclear factor κB (NF-κB) activation is the major antiviral innate response, which can be triggered by various signals induced by cellular receptors from different pathways. Here, we demonstrated that HSV-1 UL2 protein could antagonize the tumor necrosis factor α (TNF-α)-mediated NF-κB activation. Co-immunoprecipitation assays showed that UL2 could interact with the NF-κB subunits p65 and p50, which also revealed the region of amino acids 9 to 17 of UL2 could suppress the NF-κB activation and interact with p65 and p50, and UL2 bound to the immunoglobulin-like plexin transcription factor functional domain of p65. However, UL2 did not affect the formation of p65/p50 dimerization and their nuclear localizations. Yet, UL2 was demonstrated to inhibit the NF-κB activity by attenuating TNF-α-induced p65 phosphorylation at Ser536 and therefore decreasing the expression of downstream inflammatory chemokine interleukin 8. Taken together, the attenuation of NF-κB activation by UL2 may contribute to the escape of host's antiviral innate immunity for HSV-1 during its infection.

Indexed as

HEK293 CellsHeLa CellsHerpes SimplexHerpesvirus 1, HumanHost-Pathogen InteractionsHumansImmune EvasionNF-kappa BTumor Necrosis Factor-alphaUracil-DNA GlycosidaseViral ProteinsNF-kappa BTumor Necrosis Factor-alphaUL2 protein, HSV-1Uracil-DNA GlycosidaseViral ProteinsHSV-1IL-8innate immunityNF-κBUL2

Identifiers

PMID32477319
PMCPMC7237644
OpenAlexW3025861112

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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.