ArticleJournal of virology2016
Crystal Structure of Marburg Virus VP40 Reveals a Broad, Basic Patch for Matrix Assembly and a Requirement of the N-Terminal Domain for Immunosuppression.
Article in Journal of virology, 2016. 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, 45 citations in OpenAlex.
- A short history of Auto-Rickshaw.Acta crystallographica. Section D, Structural biology · 2026Review
- AI-Driven Discovery and BSL-4 Validation of Cross-Filovirus Ebola-Marburg Inhibitors and their Synergistic Combinations.bioRxiv : the preprint server for biology · 2026Article
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- Marburg virus exploits the Rab11-mediated endocytic pathway in viral-particle production.Microbiology spectrum · 2024Article
- Phosphatidylserine clustering by the Ebola virus matrix protein is a critical step in viral budding.EMBO reports · 2022Article
- Negative-sense RNA viruses: An underexplored platform for examining virus-host lipid interactions.Molecular biology of the cell · 2021Review
- Lipid-protein interactions in virus assembly and budding from the host cell plasma membrane.Biochemical Society transactions · 2021Review
- Compound FC-10696 Inhibits Egress of Marburg Virus.Antimicrobial agents and chemotherapy · 2021Article
- Article
- Article
- Article
- Review
- Recent advances in marburgvirus research.F1000Research · 2019Review
- DNA-launched RNA replicon vaccines induce potent anti-Ebolavirus immune responses that can be further improved by a recombinant MVA boost.Scientific reports · 2018Article
- A cationic, C-terminal patch and structural rearrangements in Ebola virus matrix VP40 protein control its interactions with phosphatidylserine.The Journal of biological chemistry · 2018Article
- Deep-sequencing of Marburg virus genome during sequential mouse passaging and cell-culture adaptation reveals extensive changes over time.Scientific reports · 2017Article
- Plasma membrane association facilitates conformational changes in the Marburg virus protein VP40 dimer.RSC advances · 2017Article
- Detection of lipid-induced structural changes of the Marburg virus matrix protein VP40 using hydrogen/deuterium exchange-mass spectrometry.The Journal of biological chemistry · 2017Article
- Unveiling a Drift Resistant Cryptotope withinFrontiers in immunology · 2017Article
- Oligomeric viral proteins: small in size, large in presence.Critical reviews in biochemistry and molecular biology · 2016Review
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
unlabelledMarburg virus (MARV), a member of the filovirus family, causes severe hemorrhagic fever with up to 90% lethality. MARV matrix protein VP40 is essential for assembly and release of newly copied viruses and also suppresses immune signaling in the infected cell. Here we report the crystal structure of MARV VP40. We found that MARV VP40 forms a dimer in solution, mediated by N-terminal domains, and that formation of this dimer is essential for budding of virus-like particles. We also found the N-terminal domain to be necessary and sufficient for immune antagonism. The C-terminal domains of MARV VP40 are dispensable for immunosuppression but are required for virus assembly. The C-terminal domains are only 16% identical to those of Ebola virus, differ in structure from those of Ebola virus, and form a distinct broad and flat cationic surface that likely interacts with the cell membrane during virus assembly. IMPORTANCE: Marburg virus, a cousin of Ebola virus, causes severe hemorrhagic fever, with up to 90% lethality seen in recent outbreaks. Molecular structures and visual images of the proteins of Marburg virus are essential for the development of antiviral drugs. One key protein in the Marburg virus life cycle is VP40, which both assembles the virus and suppresses the immune system. Here we provide the molecular structure of Marburg virus VP40, illustrate differences from VP40 of Ebola virus, and reveal surfaces by which Marburg VP40 assembles progeny and suppresses immune function.
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