Production and Purification of CAMP-Sialidase Chimer Protein as a Vaccine Candidate for Acne and Its Immunization in the Animal Model

Introduction: acne vulgaris affects ~85% of young adults aged 12-25 years. regarding the critical role of propionibacterium acnes in the pathogenesis of acne and current therapeutic failures, developing efficient acne vaccines are appreciated. accordingly, designing a chimeric protein from camp and sialidase parts of propionibacterium acnes and evaluating its immunogenicity in mice model as an acne vaccine candidate was aimed in this study.materials and methods: camp-sialidase recombinant gene expression was carried out through cloning in the vector pet28a and transferring to e. coli bl21de3. the protein was purified using ni-nta column and its concentration was measured. the recombinant protein was injected in test and control mice groups. then, antibody titration and challenge test were made to determine the immunogenicity.results: after successful expression and purification, the protein band was observed at a molecular weight of 65 kda. western blotting confirmed the purified protein. the results of serum elisa indicated the igg titer was 1:204800 and 1:1600 against the recombinant protein and inactivated p. acne, respectively. although there was no change in test mice, inflammation happened in 50% of the control group.conclusions: the current study demonstrated that the camp-sialidase recombinant protein can appropriately induce humoral antibody. however, more evaluations need to introduce it as an acne vaccine candidate.