Evidence map›Paper›PMID 17581998›Full record

ArticleJournal of virology2007

The ORF3 protein of porcine circovirus type 2 interacts with porcine ubiquitin E3 ligase Pirh2 and facilitates p53 expression in viral infection.

Jue Liu, Yu Zhu, Isabelle Chen, Jennifer Lau, Fang He, Adeline Lau, Zhilong Wang, Anbu K Karuppannan, Jimmy Kwang

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 88 citations in OpenAlex.

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  13. Apoptosis Triggered by ORF3 Proteins of theFrontiers in cellular and infection microbiology · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Mouse models of porcine circovirus 2 infection.Animal models and experimental medicine · 2018
    Review
  18. Review
  19. Article
  20. 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

9 authors at 2 institutions in 1 country.

Jue LiuAnimal Health Biotechnology Group, Temasek Life Sciences Laboratory, National University of Singapore, 1 Research Link, Singapore.
Yu Zhu
Isabelle Chen
Jennifer Lau
Fang He
Adeline Lau
Zhilong Wang
Anbu K Karuppannan
Jimmy Kwang
Temasek Life Sciences Laboratory · SGNational University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Porcine circovirus type 2 (PCV2) is the primary causative agent of an emerging swine disease, postweaning multisystemic wasting syndrome. We previously showed that a newly identified protein, ORF3, plays a major role in virus-induced apoptosis and is involved in viral pathogenesis in vitro and in vivo. To characterize the role of the ORF3 protein in modulation of cellular function, a yeast two-hybrid system was used to screen a porcine cDNA library to find its interacting partner. We have isolated and characterized pPirh2 (for "porcine p53-induced RING-H2"), an E3 ubiquitin ligase, which specifically interacts with the ORF3 protein of PCV2. This interaction was further confirmed when the ORF3 protein coimmunoprecipitated with and colocalized to pPirh2 in PK15 cells. The ORF3 protein has been found to interact with the p53 binding domain of pPirh2 in yeast cells. Expression of the protein results in less pPirh2 expression in PCV2-infected cells. Furthermore, increases in p53 expression were observed in PCV2-infected and ORF3 (alone)-transfected cells. Phosphorylation of p53 at Ser-46, which is related to p53-induced apoptosis, was also time-dependently activated in PCV-infected and ORF3-transfected cells. Taken together, our results show that the PCV2 ORF3 protein specifically interacts with pPirh2 and inhibits its stabilization; this may lead to increasing p53 expression, resulting in apoptosis.

Indexed as

AnimalsBinding SitesCell LineCircovirusDNA, ComplementaryGene LibraryImmunoprecipitationMolecular Sequence DataPhosphorylationProtein BindingProtein Processing, Post-TranslationalSequence Analysis, DNASwineTumor Suppressor Protein p53Two-Hybrid System TechniquesUbiquitin-Protein LigasesDNA, ComplementaryTumor Suppressor Protein p53Ubiquitin-Protein LigasesViral Proteins

Identifiers

PMID17581998
PMCPMC1951394
OpenAlexW2105495738

What OpenQuestion holds

Textmetadata
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.