Evidence map›Paper›PMID 40548980›Full record

ArticleCellular and molecular life sciences : CMLS2025

THAP11-mediated K48- and K63-linked ubiquitination is essential for the degradation of porcine reproductive and respiratory syndrome virus nonstructural protein 1β.

Binghua Chen, Yongsheng Xie, Zhan He, Yongjie Chen, Jiecong Yan, Fangfang Li, Yunyan Luo, Yanfei Pan, Min Liu, Chunhe Guo

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Article
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

10 authors.

Binghua Chen *Guangdong Laboratory for Lingnan Modern Agriculture, State Key Laboratory for Animal Disease Control and Prevention, Key Laboratory of Zoonosis Prevention and Control of Guangdong Province, College of Veterinary Medicine, South China Agricultural University, Guangzhou, Guangdong, PR China.
Yongsheng Xie *College of Life Science and Resources and Environment, Yichun University, Yichun, 336000, Jiangxi, China.
Zhan He *Guangdong Laboratory for Lingnan Modern Agriculture, State Key Laboratory for Animal Disease Control and Prevention, Key Laboratory of Zoonosis Prevention and Control of Guangdong Province, College of Veterinary Medicine, South China Agricultural University, Guangzhou, Guangdong, PR China.
Yongjie ChenGuangdong Laboratory for Lingnan Modern Agriculture, State Key Laboratory for Animal Disease Control and Prevention, Key Laboratory of Zoonosis Prevention and Control of Guangdong Province, College of Veterinary Medicine, South China Agricultural University, Guangzhou, Guangdong, PR China.
Jiecong YanGuangdong Laboratory for Lingnan Modern Agriculture, State Key Laboratory for Animal Disease Control and Prevention, Key Laboratory of Zoonosis Prevention and Control of Guangdong Province, College of Veterinary Medicine, South China Agricultural University, Guangzhou, Guangdong, PR China.
Fangfang LiGuangdong Laboratory for Lingnan Modern Agriculture, State Key Laboratory for Animal Disease Control and Prevention, Key Laboratory of Zoonosis Prevention and Control of Guangdong Province, College of Veterinary Medicine, South China Agricultural University, Guangzhou, Guangdong, PR China.
Yunyan LuoGuangdong Laboratory for Lingnan Modern Agriculture, State Key Laboratory for Animal Disease Control and Prevention, Key Laboratory of Zoonosis Prevention and Control of Guangdong Province, College of Veterinary Medicine, South China Agricultural University, Guangzhou, Guangdong, PR China.
Yanfei PanGuangdong Laboratory for Lingnan Modern Agriculture, State Key Laboratory for Animal Disease Control and Prevention, Key Laboratory of Zoonosis Prevention and Control of Guangdong Province, College of Veterinary Medicine, South China Agricultural University, Guangzhou, Guangdong, PR China.
Min LiuGuangdong Laboratory for Lingnan Modern Agriculture, State Key Laboratory for Animal Disease Control and Prevention, Key Laboratory of Zoonosis Prevention and Control of Guangdong Province, College of Veterinary Medicine, South China Agricultural University, Guangzhou, Guangdong, PR China.
Chunhe GuoGuangdong Laboratory for Lingnan Modern Agriculture, State Key Laboratory for Animal Disease Control and Prevention, Key Laboratory of Zoonosis Prevention and Control of Guangdong Province, College of Veterinary Medicine, South China Agricultural University, Guangzhou, Guangdong, PR China. guochunh@mail.sysu.edu.cn.ORCID http://orcid.org/0000-0002-7859-1985

Funding

Basic and Applied Basic Research Foundation of Guangdong Province 2024A1515012991National Key Research and Development Program of China 2023YFD1801500
6 · The paper itself

Abstract

Porcine reproductive and respiratory syndrome virus (PRRSV) is a highly infectious pathogen in the global pig industry that causes significant economic losses. Owing to its rapid mutation, effective antiviral treatments or vaccines are still lacking. Therefore, it is essential to identify potential host factors that interact with PRRSV-encoded proteins. In this study, a porcine alveolar macrophage cDNA library was used to identify host proteins that interact with PRRSV nonstructural protein 1β (Nsp1β) via a yeast two-hybrid system. A total of 34 potential host factors were identified, with Thanatos-associated protein 11 (THAP11) strongly interacting with Nsp1β. These interactions were further analyzed via Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analyses. Co-localization of Nsp1β with THAP11, poly(rC)-binding protein 1 (PCBP1), thioredoxin-interacting protein (TXNIP), and cathepsin D (CTSD) was observed, and co-IP assays confirmed the Nsp1β-THAP11 interaction. The overexpression of THAP11 reduced PRRSV N protein accumulation, indicating an antiviral effect, whereas the silencing of THAP11 increased PRRSV replication. Furthermore, THAP11 promoted the degradation of Nsp1β by increasing K48- and K63-linked ubiquitination, thereby restricting PRRSV replication. These findings suggest that THAP11 exerts an antiviral effect by interacting with and degrading Nsp1β via the ubiquitin-proteasome system, providing insights for future PRRSV defence strategies.

Indexed as

DNA-Binding ProteinsPorcine respiratory and reproductive syndrome virusUbiquitinationViral Nonstructural ProteinsAnimalsCell LineHost-Pathogen InteractionsMacrophages, AlveolarPorcine Reproductive and Respiratory SyndromeProteolysisSwineDNA-Binding ProteinsViral Nonstructural ProteinsNsp1βPRRSVTHAP11Virus-host interactionsYeast two-hybrid screening

Identifiers

PMID40548980
PMCPMC12185814

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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.