ArticleJournal of virology2004
Multivesicular bodies as a platform for formation of the Marburg virus envelope.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 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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Who cites it
64 citing papers in PubMed, 116 citations in OpenAlex.
- IQGAP1 and IQGAP3 are critical host factors for Marburg virus replication, nucleocapsid transport, and cell-to-cell spread.Cellular and molecular life sciences : CMLS · 2026Article
- To be or not to be phosphorylated: understanding the role of Ebola virus nucleoprotein in the dynamic interplay with the transcriptional activator VP30 and the host phosphatase PP2A-B56.Emerging microbes & infections · 2025Article
- Molecular insights into nucleocapsid assembly and transport in Marburg and Ebola viruses.mBio · 2025Article
- Marburg virus glycoprotein mRNA vaccine is more protective than a virus-like particle-forming mRNA vaccine.The Journal of clinical investigation · 2025Article
- Immunogenicity of differentially glycosylated Marburg virus glycoproteins expressed in mammalian and insect cells.Virology journal · 2025Article
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- Marburg virus exploits the Rab11-mediated endocytic pathway in viral-particle production.Microbiology spectrum · 2024Article
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- Bombyx mori Nucleopolyhedrovirus Hijacks Multivesicular Body as an Alternative Envelopment Platform for Budded Virus Egress.Journal of virology · 2023Article
- Self-amplifying RNA vaccine protects mice against lethal Ebola virus infection.Molecular therapy : the journal of the American Society of Gene Therapy · 2023Article
- Role of VP30 Phosphorylation in Ebola Virus Nucleocapsid Assembly and Transport.Journal of virology · 2022Article
- Compound FC-10696 Inhibits Egress of Marburg Virus.Antimicrobial agents and chemotherapy · 2021Article
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- A live-cell imaging system for visualizing the transport of Marburg virus nucleocapsid-like structures.Virology journal · 2019Article
- Serum Deprivation of Mesenchymal Stem Cells Improves Exosome Activity and Alters Lipid and Protein Composition.iScience · 2019Article
- Marburg virus regulates the IRE1/XBP1-dependent unfolded protein response to ensure efficient viral replication.Emerging microbes & infections · 2019Article
- Filoviruses: Ecology, Molecular Biology, and Evolution.Advances in virus research · 2018Review
- Dissecting the Subcellular Localization, Intracellular Trafficking, Interactions, Membrane Association, and Topology of Citrus Leprosis Virus C Proteins.Frontiers in plant science · 2018Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Marburg virus (MARV) envelope consists of a lipid membrane and two major proteins, the matrix protein VP40 and the glycoprotein GP. Both proteins use different intracellular transport pathways: GP utilizes the exocytotic pathway, while VP40 is transported through the retrograde late endosomal pathway. It is currently unknown where the proteins combine to form the viral envelope. In the present study, we identified the intracellular site where the two major envelope proteins of MARV come together as peripheral multivesicular bodies (MVBs). Upon coexpression with VP40, GP is redistributed from the trans-Golgi network into the VP40-containing MVBs. Ultrastructural analysis of MVBs suggested that they provide the platform for the formation of membrane structures that bud as virus-like particles from the cell surface. The virus-like particles contain both VP40 and GP. Single expression of GP also resulted in the release of particles, which are round or pleomorphic. Single expression of VP40 led to the release of filamentous structures that closely resemble viral particles and contain traces of endosomal marker proteins. This finding indicated a central role of VP40 in the formation of the filamentous structure of MARV particles, which is similar to the role of the related Ebola virusVP40. In MARV-infected cells, VP40 and GP are colocalized in peripheral MVBs as well. Moreover, intracellular budding of progeny virions into MVBs was frequently detected. Taken together, these results demonstrate an intracellular intersection between GP and VP40 pathways and suggest a crucial role of the late endosomal compartment for the formation of the viral envelope.
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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.