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<p>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&#xa0;°C, 40&#xa0;°C, 60&#xa0;°C, and 80&#xa0;°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.</p>

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In silico analysis of VP2 protein from infectious bursal disease virus isolate UPM1432/2019: structural dynamics and epitope prediction

  • 期刊论文

  • 发表日期：

    2025年12月5日

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  • Ali Youssif Mansour,
  • Abdul Rahman Omar,
  • Mohd Hair Bejo,
  • Noorjahan Banu Alitheen,
  • Nurulfiza Mat Isa

摘要

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.