ArticleJournal of virology2002
VP40, the matrix protein of Marburg virus, is associated with membranes of the late endosomal compartment.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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
53 citing papers in PubMed, 103 citations in OpenAlex.
- Article
- Transcription- and Replication-Competent Virus-like Particle Systems for Marburg Virus.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Marburg virus exploits the Rab11-mediated endocytic pathway in viral-particle production.Microbiology spectrum · 2024Article
- Article
- WWOX-Mediated Degradation of AMOTp130 Negatively Affects Egress of Filovirus VP40 Virus-Like Particles.Journal of virology · 2022Article
- Multiple RNA virus matrix proteins interact with SLD5 to manipulate host cell cycle.The Journal of general virology · 2021Article
- Compound FC-10696 Inhibits Egress of Marburg Virus.Antimicrobial agents and chemotherapy · 2021Article
- New Perspectives on the Biogenesis of Viral Inclusion Bodies in Negative-Sense RNA Virus Infections.Cells · 2021Review
- Angiomotin Counteracts the Negative Regulatory Effect of Host WWOX on Viral PPxY-Mediated Egress.Journal of virology · 2021Article
- Impact of Měnglà Virus Proteins on Human and Bat Innate Immune Pathways.Journal of virology · 2020Article
- Article
- Review
- Ebola Virus VP40 Modulates Cell Cycle and Biogenesis of Extracellular Vesicles.The Journal of infectious diseases · 2018Article
- Dissecting the Subcellular Localization, Intracellular Trafficking, Interactions, Membrane Association, and Topology of Citrus Leprosis Virus C Proteins.Frontiers in plant science · 2018Article
- Ubiquitin Ligase WWP1 Interacts with Ebola Virus VP40 To Regulate Egress.Journal of virology · 2017Article
- Article
- Crystal Structure of Marburg Virus VP40 Reveals a Broad, Basic Patch for Matrix Assembly and a Requirement of the N-Terminal Domain for Immunosuppression.Journal of virology · 2016Article
- A Single Amino Acid Change in the Marburg Virus Matrix Protein VP40 Provides a Replicative Advantage in a Species-Specific Manner.Journal of virology · 2016Article
- Investigation of the Lipid Binding Properties of the Marburg Virus Matrix Protein VP40.Journal of virology · 2015Article
- Small-molecule probes targeting the viral PPxY-host Nedd4 interface block egress of a broad range of RNA viruses.Journal of virology · 2014Article
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
Localization of VP40 in Marburg virus (MBGV)-infected cells was studied by using immunofluorescence and immunoelectron microscopic analysis. VP40 was detected in association with nucleocapsid structures, present in viral inclusions and at sites of virus budding. Additionally, VP40 was identified in the foci of virus-induced membrane proliferation and in intracellular membrane clusters which had the appearance of multivesicular bodies (MVBs). VP40-containing MVBs were free of nucleocapsids. When analyzed by immunogold labeling, the concentration of VP40 in MVBs was six times higher than in nucleocapsid structures. Biochemical studies showed that recombinant VP40 represented a peripheral membrane protein that was stably associated with membranes by hydrophobic interaction. Recombinant VP40 was also found in association with membranes of MVBs and in filopodia- or lamellipodia-like protrusions at the cell surface. Antibodies against marker proteins of various cellular compartments showed that VP40-positive membranes contained Lamp-1 and the transferrin receptor, confirming that they belong to the late endosomal compartment. VP40-positive membranes were also associated with actin. Western blot analysis of purified MBGV structural proteins demonstrated trace amounts of actin, Lamp-1, and Rab11 (markers of recycling endosomes), while markers for other cellular compartments were absent. Our data indicate that MBGV VP40 was able to interact with membranes of late endosomes in the course of viral infection. This capability was independent of other MBGV proteins.
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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.