Human immunology · 2026
A wide proteome analysis to engineer an efficient epitope based vaccine against Salmonella typhi: An immunoinformatic study.
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Beiranvand Mahsa, Shams Nemat, Jaydari Amin, Nazifi Narges, Khademi Peyman
Аннотация
BACKGROUND: Typhoid fever, a potentially fatal disease caused by Salmonella enterica serovar Typhi, requires effective vaccines. This study aimed to design a recombinant subunit vaccine using the most immunogenic proteins from the Salmonella Typhi proteome.
METHODS: Initially, the most antigenic proteins were selected to predict linear T-cell, B-cell, and IFN-γ epitopes. A recombinant construct incorporating these epitopes, peptide linkers, and a molecular adjuvant was designed. Comprehensive evaluation assessed physicochemical properties, solubility, secondary/tertiary structure, antigenicity, and immune stimulation potential. Molecular docking and dynamics simulations investigated binding to the TLR4/MD2 receptor complex.
RESULTS: Seven proteins from 4322 were chosen for epitope prediction, yielding a 655-amino acid construct. Physicochemical analysis showed 40.31 % hydrophobic amino acids, an aliphatic index of 53.66, GRAVY index of -0.712, and instability index of 22.34. Structural composition was 53.53 % alpha-helix, 8.85 % extended strand, and 40.61 % random coil. Immune simulations demonstrated significant enhancement of primary/secondary humoral and cellular immune responses. The vaccine construct effectively bound the TLR4/MD2 receptor via significant hydrogen bonding (affinity: -1019.1 kcal/mol). Molecular dynamics simulations confirmed the stability of this interaction over 200 ns, demonstrating that both the vaccine candidate and receptor remained structurally stable throughout the simulation period.
CONCLUSION: Typhoid vaccine candidate shows immunogenic properties, robust immune responses and stable TLR4/MD2 receptor binding.
METHODS: Initially, the most antigenic proteins were selected to predict linear T-cell, B-cell, and IFN-γ epitopes. A recombinant construct incorporating these epitopes, peptide linkers, and a molecular adjuvant was designed. Comprehensive evaluation assessed physicochemical properties, solubility, secondary/tertiary structure, antigenicity, and immune stimulation potential. Molecular docking and dynamics simulations investigated binding to the TLR4/MD2 receptor complex.
RESULTS: Seven proteins from 4322 were chosen for epitope prediction, yielding a 655-amino acid construct. Physicochemical analysis showed 40.31 % hydrophobic amino acids, an aliphatic index of 53.66, GRAVY index of -0.712, and instability index of 22.34. Structural composition was 53.53 % alpha-helix, 8.85 % extended strand, and 40.61 % random coil. Immune simulations demonstrated significant enhancement of primary/secondary humoral and cellular immune responses. The vaccine construct effectively bound the TLR4/MD2 receptor via significant hydrogen bonding (affinity: -1019.1 kcal/mol). Molecular dynamics simulations confirmed the stability of this interaction over 200 ns, demonstrating that both the vaccine candidate and receptor remained structurally stable throughout the simulation period.
CONCLUSION: Typhoid vaccine candidate shows immunogenic properties, robust immune responses and stable TLR4/MD2 receptor binding.
Предметные рубрики MeSH
Salmonella typhiImmunoinformaticsTyphoid FeverProteomeHumansEpitopes, B-LymphocyteToll-Like Receptor 4Typhoid-Paratyphoid VaccinesMolecular Docking SimulationMolecular Dynamics SimulationProtein Subunit VaccinesEpitopes, T-LymphocyteAntigens, BacterialVaccines, SubunitLymphocyte Antigen 96Bacterial ProteinsProteomicsEpitopes