ArticleScientific reports2021
Marek's disease virus Meq oncoprotein interacts with chicken HDAC 1 and 2 and mediates their degradation via proteasome dependent pathway.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- Pathogenicity analysis and control strategies to combat avian diseases: mechanisms of increased virulence of Marek's disease virus and the development of vaccines against poultry red mites.The Journal of veterinary medical science · 2025Review
- The emergence of a highly pathogenic marek's disease virus featuring newly identified mutations in Meq oncogene in Southern China.Virology journal · 2025Article
- Coronavirus M protein impairs cilium during early infection by enhancing the AurA-HDAC6 axis.PLoS pathogens · 2025Article
- Marek's Disease Virus (MDV) Meq Oncoprotein Plays Distinct Roles in Tumor Incidence, Distribution, and Size.Viruses · 2025Article
- Review
- Characterization of a Very Short Meq Protein Isoform in a Marek's Disease Virus Strain in Japan.Veterinary sciences · 2024Article
- Integrated Analysis of MicroRNA and mRNA Expression Profiles in the Fat Bodies of MbMNPV-InfectedViruses · 2022Article
- Porcine Deltacoronavirus Infection Cleaves HDAC2 to Attenuate Its Antiviral Activity.Journal of virology · 2022Article
- Role of gga-miR-29b-3p in suppressing the proliferation, invasion and migration of MSB1 Marek's disease tumor cells by the targeting of theAnnals of translational medicine · 2022Article
- Marek's Disease Virus Virulence Genes Encode Circular RNAs.Journal of virology · 2022Article
- A Review on the Marek's Disease Outbreak and Its Virulence-RelatedAnimals : an open access journal from MDPI · 2022Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Marek's disease virus (MDV) encodes a basic-leucine zipper (BZIP) protein, Meq, which is considered the major MDV oncoprotein. It has been reported that the oncogenicity of Meq is associated with its interaction with C-terminal binding protein 1 (CtBP), which is also an interaction partner of Epstein-Barr virus encoded EBNA3A and EBNA3C oncoproteins. Since both EBNA3C and CtBP interact with histone deacetylase 1 (HDAC1) and HDAC2, we examined whether Meq shares this interaction with chicken HDAC1 (chHDAC1) and chHDAC2. Using confocal microscopy analysis, we show that Meq co-localizes with chHDAC1 and chHDAC2 in the nuclei of MDV lymphoblastoid tumor cells. In addition, immunoprecipitation assays demonstrate that Meq interacts with chHDAC1 and chHDAC2 in transfected cells and MDV lymphoblastoid tumor cells. Using deletion mutants, interaction domains were mapped to the N-terminal dimerization domain of chHDAC1 and chHDAC2, and the BZIP domain of Meq. Our results further demonstrate that this interaction mediates the degradation of chHDAC1 and chHDAC2 via the proteasome dependent pathway. In addition, our results show that Meq also induces the reduction of global ubiquitinated proteins through a proteasome dependent pathway. In conclusion, our results provide evidence that Meq interacts with chHDAC1 and chHDAC2, and induces their proteasome dependent degradation.
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