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In Vitro Evaluation of Immunogenicity of Recombinant OMP25 Protein Obtained from Endemic Brucella abortus Biovar 3 as Vaccine Candidate Molecule Against Animal Brucellosis.

BACKGROUND: Brucellosis is a zoonotic disease that causes serious economic losses due to factors such as miscarriages and decreased milk yield in animals. Existing live vaccines have some disadvantages, so effective vaccines need to be developed with new technological approaches.

OBJECTIVES: The primary objectives of this study were the expression and purification of recombinant Omp25 fusion protein from B. abortus and the evaluation of the effect of the Omp25 protein on cell viability and inflammatory response.

METHODS: The omp25 gene region was amplified by a polymerase chain reaction and cloned into a Pet102/D-TOPO expression vector. The protein expression was carried out using the procaryotic expression system. The recombinant Omp25 protein was purified with affinity chromatography followed by GPC (Gel Permeation Chromatography). The MTS assay and cytokine-release measurements were carried out to evaluate cell viability and inflammatory response, respectively.

RESULTS: It was determined that doses of the recombinant Omp25 protein doses greater than 0.1 μg/mL are toxic to RAW cells. Doses of 1 µg/mL and lower significantly increased inflammation due to nitric oxide (NO) levels. ELISA results show that IFN-γ was produced in stimulated RAW 264.7 cells at a dose that did not affect the viability (0.05 µg/mL). However, IL-12, which is known to have a dual role in the activation of macrophages, did not show a statistically significant difference at the same dose.

CONCLUSION: Studies of cell viability and Th1-related cytokine release suggest that Omp25 protein is a promising candidate molecule for vaccine development.

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