Evidence map›Paper›PMID 31341055›Full record

ArticleJournal of virology2019

Porcine Reproductive and Respiratory Syndrome Virus E Protein Degrades Porcine Cholesterol 25-Hydroxylase via the Ubiquitin-Proteasome Pathway.

Wenting Ke, Liurong Fang, Ran Tao, Yang Li, Huiyuan Jing, Dang Wang, Shaobo Xiao

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.7field-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

25 citing papers in PubMed, 34 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

7 authors at 1 institution in 1 country.

Wenting KeState Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China.
Liurong FangState Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China fanglr@mail.hzau.edu.cn vet@mail.hzau.edu.cn.ORCID 0000-0003-1406-6409
Ran TaoState Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China.
Yang LiState Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China.
Huiyuan JingState Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China.
Dang WangState Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China.
Shaobo XiaoState Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China fanglr@mail.hzau.edu.cn vet@mail.hzau.edu.cn.ORCID 0000-0003-0023-9188
Huazhong Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Porcine reproductive and respiratory syndrome is one of the most important infectious diseases affecting the global pig industry. Previous studies from our group and other groups showed that cholesterol 25-hydroxylase (CH25H), a multitransmembrane endoplasmic reticulum-associated enzyme, catalyzes the production of 25-hydroxycholesterol (25HC) and inhibits porcine reproductive and respiratory syndrome virus (PRRSV) replication. However, PRRSV infection also actively decreases porcine CH25H (pCH25H) expression, through unidentified mechanisms. In this study, we found that the ubiquitin-proteasome pathway plays a major role in pCH25H degradation during PRRSV infection and that the PRRSV-encoded envelope (E) protein interacts with pCH25H. PRRSV E protein degraded pCH25H via ubiquitination, and the ubiquitination site was at pCH25H Lys28. Interestingly, PRRSV E protein appeared to specifically degrade pCH25H but not human CH25H, likely because of a Lys28Arg substitution in the human orthologue. As expected, ubiquitin-mediated degradation by E protein attenuated the antiviral effect of pCH25H by downregulating 25HC production. In addition, we found that knockdown of pCH25H decreased E protein-induced inflammatory cytokine expression and that pCH25H overexpression had the opposite effect. These findings suggested that regulation of pCH25H expression was associated with E protein-induced inflammatory responses. Taken together, our results and those of previous studies of the anti-PRRSV effects of CH25H highlight the complex interplay between PRRSV and pCH25H.

Indexed as

Amino Acid SequenceAnimalsGene Expression Regulation, ViralGene Knockdown TechniquesHost-Pathogen InteractionsPorcine Reproductive and Respiratory SyndromePorcine respiratory and reproductive syndrome virusProteasome Endopeptidase ComplexProtein BindingSignal TransductionSteroid HydroxylasesSwineUbiquitinUbiquitinationViral Envelope Proteinscholesterol 25-hydroxylaseProteasome Endopeptidase ComplexSteroid HydroxylasesUbiquitinViral Envelope ProteinsCH25Hcholesterol 25-hydroxylaseE proteinporcine reproductive and respiratory syndrome virusPRRSVubiquitin-proteasome pathway

Identifiers

PMID31341055
PMCPMC6798101
OpenAlexW2963782350

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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.