ReviewAntonie van Leeuwenhoek2025
In silico analysis of VP2 protein from infectious bursal disease virus isolate UPM1432/2019: structural dynamics and epitope prediction.
Review in Antonie van Leeuwenhoek, 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.
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Who cites it
1 citing paper in PubMed.
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Infectious Bursal Disease Virus (IBDV) remains a significant threat to global poultry health due to its immunosuppressive effects and high mutation rate, which challenge existing vaccine strategies. This study presents a comprehensive computational analysis of the VP2 protein from Malaysian IBDV isolate UPM1432/2019 to elucidate its structural stability and antigenic potential. Phylogenetic analysis revealed evolutionary divergence among VP2 sequences, while physicochemical profiling demonstrated the protein's high thermostability (aliphatic index: 98.77) and cellular stability (instability index: 17.55). Molecular dynamics simulations at 20 °C, 40 °C, 60 °C, and 80 °C showed progressive destabilization at elevated temperatures, indicated by increased RMSD, reduced hydrogen bonding, and higher solvent accessibility. Epitope prediction identified twelve linear and seven conformational B-cell epitopes, with several conserved, surface-exposed regions demonstrating high antigenicity. The most immunodominant conformational epitope (L168-E181) achieved a high ElliPro score of 0.903, indicating strong immune recognition potential. These findings highlight structurally stable and immunoreactive domains within VP2, offering valuable insights for the development of next-generation, thermostable epitope-based vaccines for effective IBDV control.
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Registered trials
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