ArticleScientific reports2018
African swine fever virus encodes for an E2-ubiquitin conjugating enzyme that is mono- and di-ubiquitinated and required for viral replication cycle.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Multiple directed mutagenesis reduces enzymatic activity and antibody recognition of the African Swine Fever Virus E2 ubiquitin-conjugating protein (ASFV-pI215L).Emerging microbes & infections · 2026Article
- Comparative genomic analysis of pigs differing in survival following African swine fever virus infection.Veterinary research communications · 2026Article
- Exploiting Ubiquitination: African Swine Fever Virus-Mediated Recruitment of Host E3 Ligases During Viral Infection and Immune Regulation.Pathogens (Basel, Switzerland) · 2026Review
- Article
- Immunogenicity assessment and epitope mapping of the ASFV proteome by profiling serum antibodies with ASFV antigen phage libraries.Communications biology · 2026Article
- Insights and progress on epidemic characteristics, pathogenesis, and preventive measures of African swine fever virus: A review.Virulence · 2025Review
- Temperature and pH dynamics during carcass decomposition and implications for disease management.Scientific reports · 2025Article
- Exploring antiviral strategies to combat African swine fever.FEMS microbiology reviews · 2025Review
- Transcriptome profiles of organ tissues from pigs experimentally infected with African swine fever virus in early phase of infection.Emerging microbes & infections · 2024Article
- When ASFV Infection Meets the cGAS-STING Signaling Pathway.Transboundary and emerging diseases · 2024Review
- Active viral infection during blooms of a dinoflagellate indicates dinoflagellate-viral co-adaptation.Applied and environmental microbiology · 2023Article
- Novel Epitope Mapping of African Swine Fever Virus pI215L Protein Using Monoclonal Antibodies.Viruses · 2023Article
- Virologs, viral mimicry, and virocell metabolism: the expanding scale of cellular functions encoded in the complex genomes of giant viruses.FEMS microbiology reviews · 2023Article
- Article
- Review
- Pleiotropic Roles of a KEAP1-Associated Deubiquitinase, OTUD1.Antioxidants (Basel, Switzerland) · 2023Review
- Structure and function of African swine fever virus proteins: Current understanding.Frontiers in microbiology · 2023Review
- African Swine Fever Virus pI215L Inhibits Type I Interferon Signaling by Targeting Interferon Regulatory Factor 9 for Autophagic Degradation.Journal of virology · 2022Article
- African Swine Fever Virus: A Review.Life (Basel, Switzerland) · 2022Review
- African Swine Fever Virus EP364R and C129R Target Cyclic GMP-AMP To Inhibit the cGAS-STING Signaling Pathway.Journal of virology · 2022Article
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4 authors.
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Abstract
African swine fever virus is the etiological agent of a contagious and fatal acute haemorrhagic viral disease for which there are no vaccines or therapeutic options. The ASFV encodes for a putative E2 ubiquitin conjugating enzyme (ORF I215L) that shows sequence homology with eukaryotic counterparts. In the present study, we showed that pI215L acts as an E2-ubiquitin like enzyme in a large range of pH values and temperatures, after short incubation times. Further experiments revealed that pI215L is polyubiquitinated instead of multi-mono-ubiquitinated and Cys85 residue plays an essential role in the transthioesterification reaction. In infected cells, I215L gene is transcribed from 2 hours post infection and immunoblot analysis confirmed that pI215L is expressed from 4 hpi. Immunofluorescence studies revealed that pI215L is recruited to viral factories from 8 hpi and a diffuse distribution pattern throughout the nucleus and cytoplasm. siRNA studies suggested that pI215L plays a critical role in the transcription of late viral genes and viral DNA replication. Altogether, our results emphasize the potential use of this enzyme as target for drug and vaccine development against ASF.
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