Evidence map›Paper›PMID 37464367›Full record

ArticleVirology journal2023

Histone deacetylase III interactions with BK polyomavirus large tumor antigen may affect protein stability.

Yueh-Han Hsu, Chun-Nun Chao, Hsin-Yi Huang, Pei-Wen Zhao, Pang-Hung Hsu, Cheng-Huang Shen, San-Yuan Chen, Chiung-Yao Fang

Open access · goldAbstract read
In one paragraph

Article in Virology journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 32% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Wnt3a Facilitates SARS-CoV-2 Pseudovirus Entry into Cells.International journal of molecular sciences · 2023
    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

8 authors at 4 institutions in 1 country.

Yueh-Han HsuDivision of Nephrology, Department of Internal Medicine, Ditmanson Medical Foundation Chia-Yi Christian Hospital, Chia-Yi, Taiwan.
Chun-Nun ChaoDepartment of Pediatrics, Ditmanson Medical Foundation Chia-Yi Christian Hospital, Chia-Yi, Taiwan.
Hsin-Yi HuangDepartment of Medical Research, Ditmanson Medical Foundation Chia-Yi Christian Hospital, Chia-Yi, Taiwan.
Pei-Wen ZhaoDepartment of Medical Research, Ditmanson Medical Foundation Chia-Yi Christian Hospital, Chia-Yi, Taiwan.
Pang-Hung HsuDepartment of Bioscience and Biotechnology, National Taiwan Ocean University, Keelung, Taiwan.
Cheng-Huang ShenDepartment of Urology, Ditmanson Medical Foundation Chiayi Christian Hospital, Chia-Yi, Taiwan.
San-Yuan Chen *Department of Chinese Medicine, Ditmanson Medical Foundation Chia-Yi Christian Hospital, Chia-Yi, Taiwan. 02157@cych.org.tw.
Chiung-Yao Fang *Department of Medical Research, Ditmanson Medical Foundation Chia-Yi Christian Hospital, Chia-Yi, Taiwan. fcyo@ms72.hinet.net.
Chia-Yi Christian Hospital · TWChia Nan University of Pharmacy and Science · TWMin-Hwei College of Health Care Management · TWNational Taiwan Ocean University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHuman polyomavirus BK (BKPyV) causes associated nephropathy and contributes to urinary tract cancer development in renal transplant recipients. Large tumor antigen (LT) is an early protein essential in the polyomavirus life cycle. Protein acetylation plays a critical role in regulating protein stability, so this study investigated the acetylation of the BKPyV LT protein.

methodsThe BKPyV LT nucleotide was synthesized, and the protein was expressed by transfection into permissive cells. The BKPyV LT protein was immunoprecipitated and subjected to LC-MS/MS analysis to determine the acetylation residues. The relative lysine was then mutated to arginine in the LT nucleotide and BKPyV genome to analyze the role of LT lysine acetylation in the BKPyV life cycle.

resultsBKPyV LT acetylation sites were identified at Lys3 and Lys230 by mass spectrometry. HDAC3 and HDAC8 and their deacetylation activity are required for BKPyV LT expression. In addition, mutations of Lys3 and Lys230 to arginine increased LT expression, and the interaction of HDAC3 and LT was confirmed by coimmunoprecipitation.

conclusionsHDAC3 is a newly identified protein that interacts with BKPyV LT, and LT acetylation plays a vital role in the BKPyV life cycle.

Indexed as

BK VirusKidney TransplantationPolyomavirusPolyomavirus InfectionsTumor Virus InfectionsAntigens, NeoplasmChromatography, LiquidHistone DeacetylasesHumansLysineProtein StabilityRepressor ProteinsTandem Mass SpectrometryAntigens, NeoplasmHDAC8 protein, humanHistone DeacetylasesLysineRepressor ProteinsAcetylationBKPyVHDAC3Large T antigenProtein stability

Identifiers

PMID37464367
PMCPMC10354968
OpenAlexW4384665116

What OpenQuestion holds

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LicenceCC BY
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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.