ArticleJournal of virology2011
Sumoylation of the P protein at K254 plays an important role in growth of parainfluenza virus 5.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 15 citations in OpenAlex.
- Isolation, genome analysis and comparison of a novel parainfluenza virus 5 from a Siberian tiger (Frontiers in veterinary science · 2024Article
- Sumoylation of Human Parainfluenza Virus Type 3 Phosphoprotein Correlates with A Reduction in Viral Replication.Virologica Sinica · 2021Article
- Molecular detection and whole genome characterization of Canine Parainfluenza type 5 in Thailand.Scientific reports · 2021Article
- Duck PIAS2 Promotes H5N1 Avian Influenza Virus Replication Through Its SUMO E3 Ligase Activity.Frontiers in microbiology · 2020Article
- SUMO and Cytoplasmic RNA Viruses: From Enemies to Best Friends.Advances in experimental medicine and biology · 2020Review
- The switch between acute and persistent paramyxovirus infection caused by single amino acid substitutions in the RNA polymerase P subunit.PLoS pathogens · 2019Article
- Viral Interplay with the Host Sumoylation System.Advances in experimental medicine and biology · 2017Review
- Novel insights into human respiratory syncytial virus-host factor interactions through integrated proteomics and transcriptomics analysis.Expert review of anti-infective therapy · 2016Article
- Review
- A novel rabies vaccine based on a recombinant parainfluenza virus 5 expressing rabies virus glycoprotein.Journal of virology · 2013Article
- Rotavirus viroplasm proteins interact with the cellular SUMOylation system: implications for viroplasm-like structure formation.Journal of virology · 2013Article
- Sumoylation at the host-pathogen interface.Biomolecules · 2012Article
- Human pathogens and the host cell SUMOylation system.Journal of virology · 2012Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The P protein of parainfluenza virus 5 (PIV5) is an essential cofactor of the viral RNA-dependent RNA polymerase. Phosphorylation of the P protein can positively or negatively regulate viral gene expression, depending on the precise phosphorylation sites. Sumoylation, a process of adding small ubiquitin-like modifier (SUMO) to proteins posttranslationally, plays an important role in regulating protein function. In this study, we have found that the P protein of PIV5 was sumoylated with SUMO1 in both transfected and infected cells. The K254 residue of the P protein is within a consensus sumoylation motif. Mutation of the P protein at K254 to arginine (P-K254R) reduced PIV5 minigenome activity, as well as the sumoylation level of the P protein. Incorporation of K254R into a recombinant PIV5 (rPIV5-P-K254R) resulted in a virus that grew to a lower titer and had lower levels of viral RNA synthesis and protein expression than wild-type PIV5, suggesting that sumoylation of the P protein at K254 is important for PIV5 growth. Biochemical studies did not reveal any defect of P-K254R in its interactions with viral proteins NP and L or formation of homotetramers. We propose that sumoylation of the P protein at K254 regulates PIV5 gene expression through a host protein.
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