ArticleViruses2014
A loop region in the N-terminal domain of Ebola virus VP40 is important in viral assembly, budding, and egress.
Article in Viruses, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 41 citations in OpenAlex.
- Ebola Virus Matrix Protein VP40 Single Mutations G198R and G201R Significantly Enhance Plasma Membrane Localization.The journal of physical chemistry. B · 2024Article
- Identification of Prospective Ebola Virus VP35 and VP40 Protein Inhibitors from Myxobacterial Natural Products.Biomolecules · 2024Article
- High-resolution comparative atomic structures of two Giardiavirus prototypes infecting G. duodenalis parasite.PLoS pathogens · 2024Article
- Minor changes in electrostatics robustly increase VP40 membrane binding, assembly, and budding of Ebola virus matrix protein derived virus-like particles.bioRxiv : the preprint server for biology · 2024Article
- Research progress on the mechanism of exosome-mediated virus infection.Frontiers in cellular and infection microbiology · 2024Review
- Elucidating Residue-Level Determinants Affecting Dimerization of Ebola Virus Matrix Protein Using High-Throughput Site Saturation Mutagenesis and Biophysical Approaches.The journal of physical chemistry. B · 2023Article
- Cheminformatics-Based Study Identifies Potential Ebola VP40 Inhibitors.International journal of molecular sciences · 2023Article
- Ebola virus protein VP40 stimulates IL-12- and IL-18-dependent activation of human natural killer cells.JCI insight · 2022Article
- Mechanisms of phosphatidylserine influence on viral production: A computational model of Ebola virus matrix protein assembly.The Journal of biological chemistry · 2022Article
- Structural and Functional Aspects of Ebola Virus Proteins.Pathogens (Basel, Switzerland) · 2021Review
- A Conserved Tryptophan in the Ebola Virus Matrix Protein C-Terminal Domain Is Required for Efficient Virus-Like Particle Formation.Pathogens (Basel, Switzerland) · 2020Article
- Using enhanced number and brightness to measure protein oligomerization dynamics in live cells.Nature protocols · 2019Article
- Review
- 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
- Curcumin and Natural Derivatives Inhibit Ebola Viral Proteins: AnPharmacognosy research · 2017Article
- Interdomain salt-bridges in the Ebola virus protein VP40 and their role in domain association and plasma membrane localization.Protein science : a publication of the Protein Society · 2016Article
- The Ebola Virus matrix protein, VP40, requires phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) for extensive oligomerization at the plasma membrane and viral egress.Scientific reports · 2016Article
- Ebolavirus comparative genomics.FEMS microbiology reviews · 2015Review
- Host Cell Plasma Membrane Phosphatidylserine Regulates the Assembly and Budding of Ebola Virus.Journal of virology · 2015Article
- The multifunctional Ebola virus VP40 matrix protein is a promising therapeutic target.Future virology · 2015Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Ebola virus (EBOV) causes viral hemorrhagic fever in humans and can have clinical fatality rates of ~60%. The EBOV genome consists of negative sense RNA that encodes seven proteins including viral protein 40 (VP40). VP40 is the major Ebola virus matrix protein and regulates assembly and egress of infectious Ebola virus particles. It is well established that VP40 assembles on the inner leaflet of the plasma membrane of human cells to regulate viral budding where VP40 can produce virus like particles (VLPs) without other Ebola virus proteins present. The mechanistic details, however, of VP40 lipid-interactions and protein-protein interactions that are important for viral release remain to be elucidated. Here, we mutated a loop region in the N-terminal domain of VP40 (Lys127, Thr129, and Asn130) and find that mutations (K127A, T129A, and N130A) in this loop region reduce plasma membrane localization of VP40. Additionally, using total internal reflection fluorescence microscopy and number and brightness analysis we demonstrate these mutations greatly reduce VP40 oligomerization. Lastly, VLP assays demonstrate these mutations significantly reduce VLP release from cells. Taken together, these studies identify an important loop region in VP40 that may be essential to viral egress.
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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 Socratic graph.