Consumption of contaminated water and foods by Salmonella Typhi cause the most common enteric disease known as Typhoid fever in both humans and animals. Despite the existence of various vaccines but infectious diseases remain a major cause of mortality worldwide. Nowadays, in-silico tools design a reliable and stable vaccine to combat such infections. Data based on microorganism genomes can help to predict the epitopes that can interact with the host immune system. However, mapping epitopes in immunogenic proteins is critical in peptide vaccine development. The study aimed to design and evaluate a multi-epitope vaccine based on the outer-membrane proteins of Salmonella Typhi. B-cells and T-cells epitopes were predicted. Predicted epitopes were connected by AAY, KK, and GPGPG linkers. Heparin-Binding Hemagglutinin Adhesin (HBHA) has been attached to the N-terminal of the final vaccine as a potent immune adjuvant. Epitope’s antigenicity, allergenicity, immunogenicity, and physicochemical characteristics were defined using in-silico tools. Molecular docking of vaccine-TLR4 was done. The RMSD of all atoms in the ligand-receptor complex gradually increases over time, and it continues until 20 ns. The RMSD graph of all atoms means that the ligand-receptor complex mostly remained stable, and the RMSD value converged within ~0.1 nm. ∆G of vaccine-TLR4 is -3.91×104 Kcal mol-1 with 1.93 RMSD. The results indicated protein was stable and non-allergen and Z-scores of multi-epitope vaccines are within the range of native proteins with similar sizes. In conclusion, the multi-epitope vaccine base on outer membrane proteins of the Salmonella Typhi bacterium might be considered to combat typhoid fever.