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 ~۸۵% of young adults aged ۱۲–۲۵ years. Regarding the critical role of Propionibacterium acnes in the pathogenesis of acne and current therapeutic failures, developing efficient acne vaccines are appreciated. The purpose of this study was to design a chimeric protein from CAMP and sialidase parts of Propionibacterium acnes and evaluating its immunogenicity in a mice model as an acne vaccine candidate.Materials and Methods: CAMP-Sialidase recombinant gene expression was carried out through cloning in the vector pET۲۸a and transferring to E.coli BL۲۱DE۳. The protein was purified using the Ni-NTA column and its concentration was measured. The recombinant protein was injected in test and control mice groups. Then, antibody titration and challenge tests were made to determine the immunogenicity.Results: After successful expression and purification, the protein band was observed at a molecular weight of ۶۵ kDa. Western blotting confirmed the purified protein. The results of serum ELISA indicated the IgG titer was ۱:۲۰۴۸۰۰ and ۱:۱۶۰۰ against the recombinant protein and inactivated P. acne, respectively. Although there was no change in test mice, inflammation happened in ۵۰% of the control group.Conclusions: The current study demonstrated that the CAMP-Sialidase recombinant protein can appropriately induce humoral antibodies. However, more evaluations need to introduce it as an acne vaccine candidate.

کلیدواژه ها:

Acne ، Propionibacterium acnes ، CAMP-Sialidase Recombinant Protein ، Vaccine