Evidence map›Paper›PMID 28750047›Full record

ArticlePLoS pathogens2017

Human cytomegalovirus IE1 downregulates Hes1 in neural progenitor cells as a potential E3 ubiquitin ligase.

Xi-Juan Liu, Bo Yang, Sheng-Nan Huang, Cong-Cong Wu, Xiao-Jun Li, Shuang Cheng, Xuan Jiang, Fei Hu, Ying-Zi Ming, Michael Nevels and 6 more

Open 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. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

36 citing papers in PubMed, 62 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

16 authors at 7 institutions in 4 countries.

Xi-Juan LiuState Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology (CEBSIT), Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.
Bo YangState Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology (CEBSIT), Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.
Sheng-Nan HuangState Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology (CEBSIT), Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.
Cong-Cong WuState Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology (CEBSIT), Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.
Xiao-Jun LiState Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology (CEBSIT), Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.ORCID http://orcid.org/0000-0002-0207-8018
Shuang ChengState Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology (CEBSIT), Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.ORCID http://orcid.org/0000-0001-9255-0453
Xuan JiangState Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology (CEBSIT), Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.
Fei HuWuhan Brain Hospital, Ministry of Transportation, Wuhan, Hubei, China.
Ying-Zi MingThe Third Xiangya Hospital, South Central University, Changsha, Hunan, China.
Michael NevelsSchool of Biology, Biomedical Sciences Research Complex, University of St Andrews, St Andrews, Fife, United Kingdom.
William J BrittDepartment of Pediatrics, University of Alabama School of Medicine, Birmingham, Alabama, United States of America.
Simon RaynerState Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology (CEBSIT), Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.ORCID http://orcid.org/0000-0001-8703-9140
Qiyi TangDepartment of Microbiology, Howard University College of Medicine, Howard University, Washington DC, United States of America.
Wen-Bo ZengState Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology (CEBSIT), Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.
Fei ZhaoState Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology (CEBSIT), Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.
Min-Hua LuoState Key Laboratory of Virology, CAS Center for Excellence in Brain Science and Intelligence Technology (CEBSIT), Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.ORCID http://orcid.org/0000-0001-9352-0643
Chinese Academy of Sciences · CNCentral South University · CNHoward University · USMinistry of Transport · CNOslo University Hospital · NOUniversity of Alabama at Birmingham · USUniversity of St Andrews · GB

Funding

PROTEOMICS CORE FACILITYG12MD007597 · NIMHD · HOWARD UNIVERSITY · PI SOUTHERLAND, WILLIAM M. · 2012 to 2018
$14.8M
NIMHD NIH HHS G12 MD007597
6 · The paper itself

Abstract

Congenital human cytomegalovirus (HCMV) infection is the leading cause of neurological disabilities in children worldwide, but the mechanisms underlying these disorders are far from well-defined. HCMV infection has been shown to dysregulate the Notch signaling pathway in human neural progenitor cells (NPCs). As an important downstream effector of Notch signaling, the transcriptional regulator Hairy and Enhancer of Split 1 (Hes1) is essential for governing NPC fate and fetal brain development. In the present study, we report that HCMV infection downregulates Hes1 protein levels in infected NPCs. The HCMV 72-kDa immediate-early 1 protein (IE1) is involved in Hes1 degradation by assembling a ubiquitination complex and promoting Hes1 ubiquitination as a potential E3 ubiquitin ligase, followed by proteasomal degradation of Hes1. Sp100A, an important component of PML nuclear bodies, is identified to be another target of IE1-mediated ubiquitination. A C-terminal acidic region in IE1, spanning amino acids 451 to 475, is required for IE1/Hes1 physical interaction and IE1-mediated Hes1 ubiquitination, but is dispensable for IE1/Sp100A interaction and ubiquitination. Our study suggests a novel mechanism linking downregulation of Hes1 protein to neurodevelopmental disorders caused by HCMV infection. Our findings also complement the current knowledge of herpesviruses by identifying IE1 as the first potential HCMV-encoded E3 ubiquitin ligase.

Indexed as

CytomegalovirusCytomegalovirus InfectionsDown-RegulationHost-Pathogen InteractionsHumansImmediate-Early ProteinsNeural Stem CellsProtein BindingProteolysisTranscription Factor HES-1UbiquitinationUbiquitin-Protein LigasesHES1 protein, humanIE1 protein, cytomegalovirusImmediate-Early ProteinsTranscription Factor HES-1Ubiquitin-Protein Ligases

Identifiers

PMID28750047
PMCPMC5549770
OpenAlexW2739755407

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.