Evidence map›Paper›PMID 39239724›Full record

ArticleVirulence2024

ATP synthase subunit ATP5B interacts with TGEV Nsp2 and acts as a negative regulator of TGEV replication.

Yanan Wang, Aoying Sun, Yaru Guo, Lingxiang Xin, Yanping Jiang, Wen Cui, Jiaxuan Li, Yijing Li, Li Wang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virulence, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing 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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Yanan WangCollege of Veterinary Medicine, Northeast Agricultural University, Harbin, China.
Aoying SunCollege of Veterinary Medicine, Northeast Agricultural University, Harbin, China.
Yaru GuoCollege of Veterinary Medicine, Northeast Agricultural University, Harbin, China.
Lingxiang XinDivision of Viral Biologic Testing(I), China Institute of Veterinary Drug Control, Beijing, China.
Yanping JiangCollege of Veterinary Medicine, Northeast Agricultural University, Harbin, China.
Wen CuiCollege of Veterinary Medicine, Northeast Agricultural University, Harbin, China.
Jiaxuan LiCollege of Veterinary Medicine, Northeast Agricultural University, Harbin, China.
Yijing LiCollege of Veterinary Medicine, Northeast Agricultural University, Harbin, China.
Li WangCollege of Veterinary Medicine, Northeast Agricultural University, Harbin, China.ORCID 0000-0002-8682-0696

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coronavirus nonstructural protein 2 (Nsp2) is regarded as a virulence determinant and plays a critical role in virus replication, and innate immunity. Screening and identifying host cell proteins that interact with viral proteins is an effective way to reveal the functions of viral proteins. In this study, the host proteins that interacted with transmissible gastroenteritis virus (TGEV) Nsp2 were identified using immunoprecipitation combined with LC-MS/MS. 77 host cell proteins were identified as putative Nsp2 interaction host cell proteins and a protein-protein interaction (PPI) was constructed. The identified proteins were found to be associated with various subcellular locations and functional categories through Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analysis. It is hypothesized that the host cell proteins interacting with TGEV Nsp2 are mainly involved in the formation of the cytoplasmic translation initiation complex, mRNA binding, ribosomes, and proteasomes. Among these, the ATP5B, a core subunit of the mitochondrial ATP synthase was further studied. The Coimmunoprecipitation (Co-IP) and indirect immunofluorescence (IFA) results confirmed that TGEV Nsp2 interacted with ATP5B. Furthermore, the downregulation of ATP5B expression was found to promote TGEV replication, suggesting that ATP5B might function as a negative regulator of TGEV replication. Collectively, our results offer additional insights into the functions of Nsp2 and provide a novel antiviral target against TGEV.

Indexed as

Mitochondrial Proton-Translocating ATPasesTransmissible gastroenteritis virusViral Nonstructural ProteinsVirus ReplicationAnimalsCell LineGastroenteritis, Transmissible, of SwineHost-Pathogen InteractionsHumansImmunoprecipitationSwineTandem Mass SpectrometryMitochondrial Proton-Translocating ATPasesViral Nonstructural ProteinsATP synthaseGO and KEGG analysesimmunoprecipitationprotein-protein interactionTGEV

Identifiers

PMID39239724
PMCPMC11385163

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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.