ArticleJournal of virus eradication2025
Development of a novel bivalent vaccine candidate against hepatitis A virus and rotavirus using reverse vaccinology and immunoinformatics.
Article in Journal of virus eradication, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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.
- Atomic force microscopy at the forefront: unveiling foodborne viruses with biophysical tools.Npj viruses · 2025Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The hepatitis A virus (HAV) and rotavirus are mainly transmitted through fecal-oral and person-to-person contact, and cause severe gastrointestinal complications and liver disease. This work used reverse vaccinology and immunoinformatic methods to create a novel bivalent vaccine against rotavirus and HAV. The amino acid sequences of HAV-rotavirus proteins (VP1 and VP8∗) were retrieved from the GenBank database. Various computational approaches were employed to predict highly conserved regions and the most immunogenic B-cell and T-cell epitopes of VP8 and VP1 of rotavirus and HAV proteins in both humans and BALB/c. Moreover, the predicted fusion protein was analyzed regarding primary and secondary structures and homology validation. In this study, we used two highly conserved peptide sequences of VP8 and VP1 of rotavirus and HAV that induce T and B cell immunogenicity. According to T-cell epitope prediction, this area comprises 2713 antigenic peptides for HLA class II and 30 HLA class I antigenic peptides, both of which are virtually entirely conserved in the Iranian population. In this study, validation as well as analysis of the secondary and three-dimensional structure of the VP8∗-rotavirus + AAY + HAV-VP1 fusion protein, with the aim of designing a multi-epitope vaccine with different receptors. TLR 3, 4 high immunogenic binding ability with immunological properties and interaction between multi-epitope target and TLR were predicted, and it is expected that the target fusion protein has stable antigenic potency and compatible half-life. The above is suggested as a universal vaccination program.
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