ArticleJournal of virology2007
Borna disease virus matrix protein is an integral component of the viral ribonucleoprotein complex that does not interfere with polymerase activity.
Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 38 citations in OpenAlex.
- Antagonistic activity against innate immunity determines virulence in mammalian bornaviruses.Npj viruses · 2025Article
- Negative and ambisense RNA virus ribonucleocapsids: more than protective armor.Microbiology and molecular biology reviews : MMBR · 2023Review
- Review
- Avian Bornavirus Research-A Comprehensive Review.Viruses · 2022Review
- The Borna Disease Virus 2 (BoDV-2) Nucleoprotein Is a Conspecific Protein That Enhances BoDV-1 RNA-Dependent RNA Polymerase Activity.Journal of virology · 2021Article
- Optimal Expression of the Envelope Glycoprotein of Orthobornaviruses Determines the Production of Mature Virus Particles.Journal of virology · 2021Article
- Divergent bornaviruses from Australian carpet pythons with neurological disease date the origin of extant Bornaviridae prior to the end-Cretaceous extinction.PLoS pathogens · 2018Article
- Dual function of the nuclear export signal of the Borna disease virus nucleoprotein in nuclear export activity and binding to viral phosphoprotein.Virology journal · 2017Article
- Borna Disease Virus Assembles Porous Cage-like Viral Factories in the Nucleus.The Journal of biological chemistry · 2016Article
- Inhibition of Borna disease virus replication by an endogenous bornavirus-like element in the ground squirrel genome.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Comprehensive analysis of endogenous bornavirus-like elements in eukaryote genomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Review
- Review
- Article
- Crystal structure of the Borna disease virus matrix protein (BDV-M) reveals ssRNA binding properties.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have recently shown that the matrix protein M of Borna disease virus (BDV) copurifies with the affinity-purified nucleoprotein (N) from BDV-infected cells, suggesting that M is an integral component of the viral ribonucleoprotein complex (RNP). However, further studies were hampered by the lack of appropriate tools. Here we generated an M-specific rabbit polyclonal antiserum to investigate the intracellular distribution of M as well as its colocalization with other viral proteins in BDV-infected cells. Immunofluorescence analysis revealed that M is located both in the cytoplasm and in nuclear punctate structures typical for BDV infection. Colocalization studies indicated an association of M with nucleocapsid proteins in these nuclear punctate structures. In situ hybridization analysis revealed that M also colocalizes with the viral genome, implying that M associates directly with viral RNPs. Biochemical studies demonstrated that M binds specifically to the phosphoprotein P but not to N. Binding of M to P involves the N terminus of P and is independent of the ability of P to oligomerize. Surprisingly, despite P-M complex formation, BDV polymerase activity was not inhibited but rather slightly elevated by M, as revealed in a minireplicon assay. Thus, unlike M proteins of other negative-strand RNA viruses, BDV-M seems to be an integral component of the RNPs without interfering with the viral polymerase activity. We propose that this unique feature of BDV-M is a prerequisite for the establishment of BDV persistence.
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