ArticleScientific reports2026
Immunoinformatics-guided design of a universal chimeric multi-epitope subunit vaccine against Marburg virus disease and Ravn virus co-infection.
Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- Toward a Vaccine Against Multidrug-Resistant Elizabethkingia anophelis: Comprehensive Immunoinformatics-Based Design of a Multi-Epitope Vaccine and mRNA Construct.Probiotics and antimicrobial proteins · 2026Article
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Authors and funding
6 authors.
Funding
Abstract
Marburg Virus Disease (MVD) is a life-threatening hemorrhagic fever, caused by two viruses-Marburg virus (MARV) and Ravn virus (RAVV)-that belong to the family Filoviridae. Due to its high mortality rate and the lack of licensed vaccines, MVD remains a major global health concern. In this study, a comprehensive immunoinformatics workflow was used to design a universal chimeric multi-epitope subunit vaccine targeting conserved antigenic regions of both viruses to reduce MVD-related mortality. Antigenicity analysis identified glycoproteins (GP) of MARV and RAVV as the most immunogenic viral proteins, and multiple sequence alignment revealed conserved regions suitable for epitope selection. Three highly conserved, antigenic, non-allergenic, and non-toxic CTL, HTL, and B-cell epitopes from each virus were incorporated into the final vaccine construct. The designed vaccine exhibited high antigenicity, non-allergenicity, solubility, and acceptable physicochemical properties. Structural modeling generated a high-quality 3D structure, and molecular docking revealed stable binding to human TLR4 with a docking score of − 229.46 kcal/mol, supported by multiple hydrogen bonds and non-bonded interactions, suggesting robust immune activation potential. Codon optimization produced a CAI value of 0.96 and 52.2% GC content, indicating efficient expression in E. coli K-12, further validated through in silico cloning. Immune simulations showed robust primary and secondary immune responses, including high levels of IgM, IgG, IFN-γ, IL-2, and strong memory cell formation. Molecular dynamics simulation analyses confirmed the stability (RMSD), compactness (Rg), and consistent hydrogen-bonding interactions between the designed vaccine and TLR4. Overall, the computational analyses indicate that the proposed chimeric multi-epitope vaccine is stable, highly immunogenic, and capable of eliciting protective immune responses, providing a strong basis for subsequent in vitro and in vivo validation.
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