ArticleTraffic (Copenhagen, Denmark)2023
Henipaviruses and lyssaviruses target nucleolar treacle protein and regulate ribosomal RNA synthesis.
Article in Traffic (Copenhagen, Denmark), 2023. 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, 14 citations in OpenAlex.
- Importin Alpha Is Implicated in the Nuclear Import of Novel Duck Reovirus Protein p18.Viruses · 2026Article
- Nucleolar targeting of lyssavirus P-protein is isoform- and phylogroup-specific.The Journal of general virology · 2026Article
- Analysis of the Porcine Reproductive and Respiratory Syndrome Virus Nucleocapsid Interactome.Journal of proteome research · 2025Article
- Conformational dynamics, RNA binding, and phase separation regulate the multifunctionality of rabies virus P protein.Nature communications · 2025Article
- The intracellular virus-host interface of henipaviruses.Journal of virology · 2025Review
- Article
- Sub-Nucleolar Trafficking of Hendra Virus Matrix Protein Is Regulated by Ubiquitination.Viruses · 2025Article
- Deciphering Immune Modulation in Chickens Co-Infected with ALV-J and CIAV: A Transcriptomic Approach.Microorganisms · 2024Article
- Henipavirus Matrix Protein Employs a Non-Classical Nuclear Localization Signal Binding Mechanism.Viruses · 2023Article
- Structural insights into the multifunctionality of rabies virus P3 protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Henipaviruses and lyssaviruses target nucleolar treacle protein and regulate ribosomal RNA synthesis.Traffic (Copenhagen, Denmark) · 2023Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nucleolus is a common target of viruses and viral proteins, but for many viruses the functional outcomes and significance of this targeting remains unresolved. Recently, the first intranucleolar function of a protein of a cytoplasmically-replicating negative-sense RNA virus (NSV) was identified, with the finding that the matrix (M) protein of Hendra virus (HeV) (genus Henipavirus, family Paramyxoviridae) interacts with Treacle protein within nucleolar subcompartments and mimics a cellular mechanism of the nucleolar DNA-damage response (DDR) to suppress ribosomal RNA (rRNA) synthesis. Whether other viruses utilise this mechanism has not been examined. We report that sub-nucleolar Treacle targeting and modulation is conserved between M proteins of multiple Henipaviruses, including Nipah virus and other potentially zoonotic viruses. Furthermore, this function is also evident for P3 protein of rabies virus, the prototype virus of a different RNA virus family (Rhabdoviridae), with Treacle depletion in cells also found to impact virus production. These data indicate that unrelated proteins of viruses from different families have independently developed nucleolar/Treacle targeting function, but that modulation of Treacle has distinct effects on infection. Thus, subversion of Treacle may be an important process in infection by diverse NSVs, and so could provide novel targets for antiviral approaches with broad specificity.
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