To　insert　the　constructed　TGF-beta(1)　epitope　gene　into　the　el　loop　of　C-terminus　of　truncated　hepatitis　B　core　antigen　to　increase　TGF-beta(1)　antigenicity　in　its　prokaryotic　expression　system　and　to　identify　immunity　of　the　expressed　recombinant　protein　in　order　to　exploit　the　possibility　for　obtaining　anti-TGF-beta(1)　vaccine.The　TGF-beta(1)　encoding　epitope　gene　(the　mature　TGF-beta(1)　from　78-109　amino　acid　residues,　TGF-beta(1)(32))　was　amplified　by　polymerase　chain　reaction　from　the　recombinant　pGEM-7z/　TGF-beta(1)(32)　vector.　The　HBcAg　gene　fragments　(encoding　HBcAg　from　1-71　and　89-144　amino　acid　residues)　were　amplified　from　PYTA1-HBcAg　vector.　The　recombinant　vector　pGEMEX-1　was　used　to　insert　HBcAg1-71,　TGF-beta(1)(32)　and　HBcAg89-144　into　restrictive　endonuclease　enzyme　and　ligated　with　T(4)　ligase.　The　fusion　gene　fragments　HBcAg1-71-TGF-beta(1)(32)-　HBcAg89-144　were　recloned　to　pET28a(+)　and　the　DNA　sequence　was　confirmed　by　the　dideoxy　chain　termination　method.　The　recombinant　vector　pET28a　(+)/CTC　was　transformed　and　expressed　in　E.　coli　BL21　(DE3)　under　induction　of　IPTG.　After　purification　with　Ni(+2)-NTA　agarose　resins,　the　antigenicity　of　purified　protein　was　detected　by　ELISA　and　Western　blot　and　visualized　under　electron　microscope.Enzyme　digestion　analysis　and　sequencing　showed　that　TGF-beta(1)　epitope　gene　was　inserted　into　the　el　loop　of　C-terminus　of　truncated　hepatitis　B　core　antigen.　SDS-PAGE　analysis　showed　that　relative　molecular　mass　(Mr)　of　the　expressed　product　by　pET28a　(+)/CTC　was　Mr　24,600.　The　output　of　the　target　recombinant　protein　was　approximately　34.8%　of　the　total　bacterial　protein,　mainly　presented　in　the　form　of　inclusion　body.　Western　blotting　and　ELISA　demonstrated　that　the　fusion　protein　could　combine　with　anti-TGF-beta(1)　polyclonal　IgG　but　not　with　anti-HBcAg.　The　purity　of　protein　was　about　90%　and　the　protein　was　in　the　form　of　self-assembling　particles　visualized　under　electron　microscope.　This　fusion　protein　had　good　anti-TGF-beta(1)　antigenicity　and　could　be　used　as　anti-TGF-beta(1)　vaccine.A　recombinant　prokaryotic　expression　system　with　high　expression　efficiency　of　the　target　TGF-beta(1)　epitope　gene　was　successfully　established.　The　fusion　protein　is　in　the　form　of　self-assembling　particles　and　HBcAg　can　increase　the　antigenicity　of　TGF-beta(1).　The　expressed　TGF-beta(1)　epitope　gene　shows　good　immunogenicity　and　antigenicity.