ArticleJournal of virology2005
Interactions between rubella virus capsid and host protein p32 are important for virus replication.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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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
34 citing papers in PubMed, 60 citations in OpenAlex.
- Review
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- Leaked Mitochondrial C1QBP Inhibits Activation of the DNA Sensor cGAS.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- SLE: Novel Postulates for Therapeutic Options.Frontiers in immunology · 2020Review
- 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
- Activation of the Mitochondrial Apoptotic Signaling Platform during Rubella Virus Infection.Viruses · 2015Article
- Role of Host Cell p32 in Herpes Simplex Virus 1 De-Envelopment during Viral Nuclear Egress.Journal of virology · 2015Article
- Phosphorylation and membrane association of the Rubella virus capsid protein is important for its anti-apoptotic function.Cellular microbiology · 2014Article
- Antiapoptotic activity of Coxiella burnetii effector protein AnkG is controlled by p32-dependent trafficking.Infection and immunity · 2014Article
- Exploration of panviral proteome: high-throughput cloning and functional implications in virus-host interactions.Theranostics · 2014Article
- Mechanisms of MAVS regulation at the mitochondrial membrane.Journal of molecular biology · 2013Review
- Activity increase in respiratory chain complexes by rubella virus with marginal induction of oxidative stress.Journal of virology · 2013Article
- Virus factories: biogenesis and structural design.Cellular microbiology · 2013Review
- The West Nile virus capsid protein blocks apoptosis through a phosphatidylinositol 3-kinase-dependent mechanism.Journal of virology · 2013Article
- Article
- Binding of cellular p32 protein to the rubella virus P150 replicase protein via PxxPxR motifs.The Journal of general virology · 2012Article
- Rubella virus-like replicon particles: analysis of encapsidation determinants and non-structural roles of capsid protein in early post-entry replication.The Journal of general virology · 2012Article
- The capsid-binding nucleolar helicase DDX56 is important for infectivity of West Nile virus.Journal of virology · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The distribution and morphology of mitochondria are dramatically affected during infection with rubella virus (RV). Expression of the capsid, in the absence of other viral proteins, was found to induce both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of RV-infected cells. We previously identified p32, a host cell mitochondrial matrix protein, as a capsid-binding protein. Here, we show that two clusters of arginine residues within capsid are required for stable binding to p32. Mutagenic ablation of the p32-binding site in capsid resulted in decreased mitochondrial clustering, indicating that interactions with this cellular protein are required for capsid-dependent reorganization of mitochondria. Recombinant viruses encoding arginine-to-alanine mutations in the p32-binding region of capsid exhibited altered plaque morphology and replicated to lower titers. Further analysis indicated that disruption of stable interactions between capsid and p32 was associated with decreased production of subgenomic RNA and, consequently, infected cells produced significantly lower amounts of viral structural proteins under these conditions. Together, these results suggest that capsid-p32 interactions are important for nonstructural functions of capsid that include regulation of virus RNA replication and reorganization of mitochondria during infection.
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