To reveal the main immunogenic domain of the glycoprotein of spring viremia of carp virus (SVCV), the glycoprotein encoding gene was truncated and expressed, and the immunogenicity of the truncated glycoprotein was analyzed using a rabbit polyclonal antibody produced in response to the recombination protein. The transmembrane, antigenic and hydrophilic domains of SVCV were analyzed by SOSUI and DNAStar 6.0 software. The predicted main immunogenic domain was amplified by reverse transcription polymerase chain reaction and cloned into a prokaryotic expression plasmid. The truncated glycoprotein was expressed in BL21 cells. After purification and refolding, the protein was used to produce antiserum in rabbits. The antiserum titer was tested by an enzyme-linked immunosorbent assay and the immunogenicity of the protein was tested by immunoblotting and indirect immunofluorescence assay (IFA). The results showed that the truncated glycoprotein gene was 1339 bp encoding a 439 aa peptide (from 29 to 467aa of the full-length glycoprotein) with a predicted molecular weight of 49.6 kD. The antiserum titer against the recombinant glycoprotein was 1:64000. Immunoblotting and IFA results demonstrated that the antiserum reacted immunologically with the natural glycoprotein on the surface of SVCV-HN. There was no difference in immunogenicity between the truncated glycoprotein produced in this study and the natural glycoprotein of SVCV. Therefore, the truncated glycoprotein of SVCV had good immunogenicity and could be used in immunological diagnosis and genetic engineering vaccine development of SVCV.