Background:　On　May　7,　2022,　WHO　reported　a　new　monkeypox　case.　By　May　2023　over　80,000　cases　had　been　reported　worldwide　outside　previously　endemic　nations.　(This　primarily　affected　the　men　who　have　sex　with　men　(MSM)　community　in　rich　nations).　The　present　research　aims　to　develop　a　multi-epitope　vaccine　for　the　monkeypox　virus　(MPXV)　using　structural　and　cell　surface　proteins.Methods:　The　first　part　of　the　research　involved　retrieving　protein　sequences.　The　Immune　Epitope　Database　(IEDB)　was　then　used　to　analyze　the　B　and　T　lymphocyte　epitopes.　After　analyzing　the　sensitizing　properties,　toxicity,　antigenicity,　and　molecular　binding,　appropriate　linkers　were　utilized　to　connect　selected　epitopes　to　adjuvants,　and　the　structure　of　the　vaccine　was　formulated.　Algorithms　from　the　field　of　immunoinformatics　predicted　the　secondary　and　tertiary　structures　of　vaccines.　The　physical,　chemical,　and　structural　properties　were　refined　and　validated　to　achieve　maximum　stability.　Molecular　docking　and　molecular　dynamic　simulations　were　subsequently　employed　to　assess　the　vaccine＇s　efficacy.　Afterward,　the　ability　of　the　vaccine　to　interact　with　toll-like　receptors　3　and　4　(TLR3　and　TLR4)　was　evaluated.　Finally,　the　optimized　sequence　was　then　introduced　into　the　Escherichia　coli　(E.　coli)　PET30A　+　vector.Results:　An　immunoinformatics　evaluation　suggested　that　such　a　vaccine　might　be　safe　revealed　that　this　vaccine　is　safe,　hydrophilic,　temperature-　and　condition-stable,　and　can　stimulate　innate　immunity　by　binding　to　TLR3　and　TLR4.Conclusion:　Our　findings　suggest　that　the　first　step　in　MPXV　pathogenesis　is　structural　and　cell　surface　epitopes.　In　this　study,　the　most　effective　and　promising　epitopes　were　selected　and　designed　through　precision　servers.　Furthermore,　through　the　utilization　of　multi-epitope　structures　and　a　combination　of　two　established　adjuvants,　this　research　has　the　potential　to　be　a　landmark　in　developing　an　antiviral　vaccine　against　MPXV.　However,　additional　in　vitro　and　in　vivo　tests　are　required　to　confirm　these　results.