ArticleJournal of virology2007
Role of the transmembrane domain of marburg virus surface protein GP in assembly of the viral envelope.
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 25 papers.
What it found
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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
25 citing papers in PubMed.
- Marburg virus glycoprotein mRNA vaccine is more protective than a virus-like particle-forming mRNA vaccine.The Journal of clinical investigation · 2025Article
- Article
- Filovirus Antiviral Activity of Cationic Amphiphilic Drugs Is Associated with Lipophilicity and Ability To Induce Phospholipidosis.Antimicrobial agents and chemotherapy · 2020Article
- A live-cell imaging system for visualizing the transport of Marburg virus nucleocapsid-like structures.Virology journal · 2019Article
- Ebola virus proteins NP, VP35, and VP24 are essential and sufficient to mediate nucleocapsid transport.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Functional Characterization of Adaptive Mutations during the West African Ebola Virus Outbreak.Journal of virology · 2017Article
- Marburg Virus Reverse Genetics Systems.Viruses · 2016Review
- Chimeric Filoviruses for Identification and Characterization of Monoclonal Antibodies.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
- Conformational plasticity of the Ebola virus matrix protein.Protein science : a publication of the Protein Society · 2014Review
- The clinically approved drugs amiodarone, dronedarone and verapamil inhibit filovirus cell entry.The Journal of antimicrobial chemotherapy · 2014Article
- Review
- Article
- Morphogenesis of pestiviruses: new insights from ultrastructural studies of strain Giraffe-1.Journal of virology · 2014Article
- Review
- Forty-five years of Marburg virus research.Viruses · 2012Review
- Uncovering viral protein-protein interactions and their role in arenavirus life cycle.Viruses · 2012Review
- Genus-specific recruitment of filovirus ribonucleoprotein complexes into budding particles.The Journal of general virology · 2011Article
- Cryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells.PLoS biology · 2011Article
- Characterization of filovirus protein-protein interactions in mammalian cells using bimolecular complementation.The Journal of infectious diseases · 2011Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major protein constituents of the filoviral envelope are the matrix protein VP40 and the surface transmembrane protein GP. While VP40 is recruited to the sites of budding via the late retrograde endosomal transport route, GP is suggested to be transported via the classical secretory pathway involving the endoplasmic reticulum, Golgi apparatus, and trans-Golgi network until it reaches the plasma membrane where most filoviral budding takes place. Since both transport routes target the plasma membrane, it was thought that GP and VP40 join there to form the viral envelope. However, it was recently shown that, upon coexpression of both proteins, GP is partially recruited into peripheral VP40-enriched multivesicular bodies, which contained markers of the late endosome. Accumulation of GP and VP40 in this compartment was presumed to play an important role in the formation of the filoviral envelope. Using a domain-swapping approach, we were able to show that the transmembrane domain of GP was essential and sufficient for (i) partial recruitment of chimeric glycoproteins into VP40-enriched multivesicular bodies and (ii) incorporation into virus-like particles (VLPs) that were released upon expression of VP40. Only those chimeric glycoproteins which were targeted to VP40-enriched endosomal multivesicular bodies were subsequently recruited into VLPs. These data show that the transmembrane domain of GP is critical for the mixing of VP40 and GP in multivesicular bodies and incorporation of GP into the viral envelope. Results further suggest that trapping of GP in the VP40-enriched late endosomal compartment is important for the formation of the viral envelope.
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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.