Abstract

Introduction: Approximately 85% of young individuals between the ages of 12 and 25 have acne vulgaris. It is important to create effective acne vaccines due to Propionibacterium acnes' crucial involvement in the aetiology of acne and existing treatment failures. As a result, the goal of this work was to create a chimeric protein from the CAMP and sialidase portions of Propionibacterium acnes and assess its immunogenicity in a mouse model as a potential acne vaccine candidate.

Literature Review: The pET28a vector was used to clone the CAMP-sialidase recombinant gene and transfer it to the E. coli BL21DE3 strain. Utilizing a Ni-NTA column, the protein was purified, and its concentration was assessed. Both the test and control mouse groups received injections of the recombinant protein. To ascertain immunogenicity, antibody titration and challenge tests were conducted.

Discussion: The protein was successfully expressed and purified, and a band with a molecular weight of 65 kDa was seen. The isolated protein was verified by western blotting. The serum ELISA findings showed that the IgG titer against the recombinant protein and inactivated P. acne was 1:204800 and 1:1600, respectively. Although test mice showed no change, 50% of the control group had inflammation.

Conclusion: The recent work shown that the recombinant CAMP-Sialidase protein may effectively produce humoral antibodies. It still need additional testing before it can be considered a contender for an acne vaccination.

Keywords: Acne; Propionibacterium acnes; CAMP-Sialidase; Recombinant protein; Acne vaccine