ArticleJournal of virology2008
A filovirus-unique region of Ebola virus nucleoprotein confers aberrant migration and mediates its incorporation into virions.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 38 citations in OpenAlex.
- Assembly and transport of filovirus nucleocapsids.PLoS pathogens · 2022Review
- The two-stage interaction of Ebola virus VP40 with nucleoprotein results in a switch from viral RNA synthesis to virion assembly/budding.Protein & cell · 2022Article
- Article
- Global phosphoproteomic analysis of Ebola virions reveals a novel role for VP35 phosphorylation-dependent regulation of genome transcription.Cellular and molecular life sciences : CMLS · 2020Article
- Identification of RUVBL1 and RUVBL2 as Novel Cellular Interactors of the Ebola Virus Nucleoprotein.Viruses · 2019Article
- Generation and Characterization of Anti-Filovirus Nucleoprotein Monoclonal Antibodies.Viruses · 2019Article
- Article
- Crystal Structure of the Marburg Virus Nucleoprotein Core Domain Chaperoned by a VP35 Peptide Reveals a Conserved Drug Target for Filovirus.Journal of virology · 2017Article
- Ebola Virus Does Not Induce Stress Granule Formation during Infection and Sequesters Stress Granule Proteins within Viral Inclusions.Journal of virology · 2016Article
- Molecular architecture of the nucleoprotein C-terminal domain from the Ebola and Marburg viruses.Acta crystallographica. Section D, Structural biology · 2016Article
- Mammalian Bcnt/Cfdp1, a potential epigenetic factor characterized by an acidic stretch in the disordered N-terminal and Ser250 phosphorylation in the conserved C-terminal regions.Bioscience reports · 2015Article
- An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions.Cell reports · 2015Article
- Development of RNA aptamers targeting Ebola virus VP35.Biochemistry · 2013Article
- Article
- Article
- dsRNA binding characterization of full length recombinant wild type and mutants Zaire ebolavirus VP35.Antiviral research · 2012Article
- Productive replication of Ebola virus is regulated by the c-Abl1 tyrosine kinase.Science translational medicine · 2012Article
- Non-retroviral fossils in vertebrate genomes.Viruses · 2011Review
- Unexpected inheritance: multiple integrations of ancient bornavirus and ebolavirus/marburgvirus sequences in vertebrate genomes.PLoS pathogens · 2010Article
- Viral and host proteins that modulate filovirus budding.Future virology · 2010Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
The Ebola virus nucleoprotein (NP) is an essential component of the nucleocapsid, required for filovirus particle formation and replication. Together with virion protein 35 (VP35) and VP24, this gene product gives rise to the filamentous nucleocapsid within transfected cells. Ebola virus NP migrates aberrantly, with an apparent molecular mass of 115 kDa, although it is predicted to encode an approximately 85-kDa protein. In this report, we show that two domains of this protein determine this aberrant migration and that this region mediates its incorporation into virions. These regions, amino acids 439 to 492 and amino acids 589 to 739, alter the mobility of Ebola virus NP by sodium dodecyl sulfate-polyacrylamide gel electrophoresis by 5 and 15 kDa, respectively, and confer similar effects on a heterologous protein, LacZ, in a position-independent fashion. Furthermore, when coexpressed with VP40, VP35, and VP24, this region mediated incorporation of NP into released viruslike particles. When fused to chimeric paramyxovirus NPs derived from measles or respiratory syncytial virus, this domain directed these proteins into the viruslike particle. The COOH-terminal NP domain comprises a conserved highly acidic region of NP with predicted disorder, distinguishing Ebola virus NPs from paramyxovirus NPs. The acidic character of this domain is likely responsible for its aberrant biochemical properties. These findings demonstrate that this region is essential for the assembly of the filamentous nucleocapsids that give rise to filoviruses.
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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.