Proteomics Exploration of Helicobacter pylori to Design an Innovative Multi-Epitope mRNA Vaccine

Background: This study aimed to explore the virulence factors associated with Helicobacter pylori and develop a multi-epitope vaccine.
Materials & Methods: Several antigenic proteins derived from the H. pylori proteome were analyzed, including CagA, FlaA, FlaB, OipA, SabA, UreA, HSP, BabA, and FecA. B and T cell epitopes were predicted for HTL, CTL, and B cells. Predicted stability and immunological responses to the vaccine were assessed using molecular binding analysis, thermodynamic sketching, in silico expression assessments, and agent-based modeling.
Findings: This study identified and selected B-cell epitopes from eight H. pylori proteins using the ABCpred web server, resulting in 19 epitopes after filtering for allergenic, toxic, and homologous properties. Computationally, the epitopes from BabA, CagA, and FlaA showed favorable scores and no adverse characteristics. Additionally, 20 CTL epitopes and 17 HTL epitopes were selected based on their IC50 values and conservation within protein sequences. Molecular docking predicted that the epitope LSDGAAAGY had the highest binding affinity to the MHC allele HLA-A*01:01, achieving -643.6 kcal/moL, suggesting potential for vaccine development.
Conclusion: This computational study supports the strategic assembly of epitopes for multi-epitope vaccine design, providing in silico insights requiring experimental validation for future H. pylori interventions.