ArticlePLoS pathogens2011
The Rubella virus capsid is an anti-apoptotic protein that attenuates the pore-forming ability of Bax.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
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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.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- A self-amplifying RNA vector based on rubella virus for mRNA therapeutics and vaccine applications.Molecular therapy. Nucleic acids · 2026Article
- Mammalian innate antiviral defenses: beyond interferon.Journal of virology · 2025Review
- Exogenous Rubella Virus Capsid Proteins Enhance Virus Genome Replication.Pathogens (Basel, Switzerland) · 2022Article
- Article
- Hantavirus inhibits apoptosis by preventing mitochondrial membrane potential loss through up-regulation of the pro-survival factor BCL-2.PLoS pathogens · 2020Article
- Infectious vaccine-derived rubella viruses emerge, persist, and evolve in cutaneous granulomas of children with primary immunodeficiencies.PLoS pathogens · 2019Article
- Molecular aspects of the teratogenesis of rubella virus.Biological research · 2019Review
- Mitochondria Redistribution in Enterovirus A71 Infected Cells and Its Effect on Virus Replication.Virologica Sinica · 2019Article
- Article
- Nucleocapsid Interacts with NPM1 and Protects it from Proteolytic Cleavage, Enhancing Cell Survival, and is Involved in PEDV Growth.Scientific reports · 2017Article
- Activation of the Mitochondrial Apoptotic Signaling Platform during Rubella Virus Infection.Viruses · 2015Article
- Structural proteins of Kaposi's sarcoma-associated herpesvirus antagonize p53-mediated apoptosis.Oncogene · 2015Article
- Short self-interacting N-terminal region of rubella virus capsid protein is essential for cooperative actions of capsid and nonstructural p150 proteins.Journal of virology · 2014Article
- Phosphorylation and membrane association of the Rubella virus capsid protein is important for its anti-apoptotic function.Cellular microbiology · 2014Article
- Exploration of panviral proteome: high-throughput cloning and functional implications in virus-host interactions.Theranostics · 2014Article
- Rubella virus capsid protein structure and its role in virus assembly and infection.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Review
- Viruses as modulators of mitochondrial functions.Advances in virology · 2013Review
- Article
- The West Nile virus capsid protein blocks apoptosis through a phosphatidylinositol 3-kinase-dependent mechanism.Journal of virology · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Apoptosis is an important mechanism by which virus-infected cells are eliminated from the host. Accordingly, many viruses have evolved strategies to prevent or delay apoptosis in order to provide a window of opportunity in which virus replication, assembly and egress can take place. Interfering with apoptosis may also be important for establishment and/or maintenance of persistent infections. Whereas large DNA viruses have the luxury of encoding accessory proteins whose primary function is to undermine programmed cell death pathways, it is generally thought that most RNA viruses do not encode these types of proteins. Here we report that the multifunctional capsid protein of Rubella virus is a potent inhibitor of apoptosis. The main mechanism of action was specific for Bax as capsid bound Bax and prevented Bax-induced apoptosis but did not bind Bak nor inhibit Bak-induced apoptosis. Intriguingly, interaction with capsid protein resulted in activation of Bax in the absence of apoptotic stimuli, however, release of cytochrome c from mitochondria and concomitant activation of caspase 3 did not occur. Accordingly, we propose that binding of capsid to Bax induces the formation of hetero-oligomers that are incompetent for pore formation. Importantly, data from reverse genetic studies are consistent with a scenario in which the anti-apoptotic activity of capsid protein is important for virus replication. If so, this would be among the first demonstrations showing that blocking apoptosis is important for replication of an RNA virus. Finally, it is tempting to speculate that other slowly replicating RNA viruses employ similar mechanisms to avoid killing infected cells.
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Registered trials
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.