RESUMO
The present study aimed to determine the intracellular localization of Cpn0425 in Chlamydophila pneumoniae-infected cells. The recombinant plasmid pGEX-6p/Cpn0425 was transformed into E.coli Bl21 cells to express the fusion protein. Following purification with glutathione S-transferase (GST) resin chromatography, the Cpn0425 fusion protein was used to induce immunity in mice to develop monoclonal and polyclonal antibodies, which were subsequently used to localize the endogenous Cpn0425 protein by indirect immunofluorescence assay (IFA). ELISA was used to determine the immunogenicity of the Cpn0425 plasmid protein by recognizing the pool sera of patients infected with Chlamydia trachomatis and the pool sera of mice immunized with the Cpn0425 fusion protein. The Cpn0425 gene was expressed as the GST-Cpn0425 fusion protein in E. coli and its antibody was prepared by immunizing mice with the fusion protein. An anti-GST-Cpn0425 antibody was used to localize the protein in cells infected with Chlamydophila pneumoniae AR-39 using an IFA. The anti-GST-CT058 antibody detected an inclusion signal in the IFA. Cpn0425 protein strongly reacted with antiserum. Although Cpn0425 protein is not a secreted protein, it has good immunogenicity. Therefore, this protein may be useful for developing vaccines against Chlamydophila pneumoniae infection.