Abstract: 【Objective】 To study the protein expression effect and immunogenicity of recombinant plasmids of rabies virus G gene, Echinococcus granulosus EgM123 gene and EGFP gene in eukaryotic cells in the hope of constructing the recombinant rabies SRV9 virus vaccine strain with EgM123 gene by reverse geneticstechnology,which can save EgM123 gene recombinant rabies by reverse genetics, it also provides the research basis for the development of rabies and hydatid disease combined gene recombinant vaccine. 【Methods】 In this study, we successfully constructed the recombinant plasmid(3033bp) of G gene of rabies virus carrying EGFP enhanced green fluorescent protein EgM123 gene of Echinococcus granulosus and transfected it into BHK-21 cells by liposome transfection. The fusion protein was expressed in BHK-21 cells and observed by fluorescence microscopy, SDS-PAGE polyacrylamide gel electrophoresis. The fluorescent protein expression, molecular weight and immunogenicity of the fusion protein were identified by Western blotting test. 【Results】 The results of recombinant plasmid transfection showed that the recombinant plasmid transfection was effective, the expression of green fluorescent protein could be seen in 48 hours after transfection, and SDS-PAGE polyacrylamide gel electrophoresis showed that the recombinant plasmid was expressed in BHK-21 cells with fusion protein with molecular weight of about 120KDa; Western Blotting results showed that the protein gel transferred PVDF membrane was incubated with rabies virus G protein monoclonal antibody, EgM123 polyclonal antibody and GFP monoclonal antibody respectively, and antigen antibody binding bands were seen at 120KDa. 【Conclusion】 The fusion protein is successfully expressed in eukaryotic cells with EGFP labeled recombinant egm123 gene of rabies virus, and the recombinant plasmid has immunogenicity.