Identification of a novel cytotoxic T lymphocyte epitope from CFP21, a secreted protein of Mycobacterium tuberculosis

CFP21 is a major secreted protein of Mycobacterium tuberculosis (Mtb) which is considered as a promising antigen for immunotherapy. To identify CFP21-derived HLA-A*0201 restricted epitopes, a series of native peptides and their analogues were predicted with prediction programs and synthesized. The native peptide, p134 (AVADHVAAV), and its analogues, p134-1Y2L and p134-1Y2L9L, showed potent binding affinity and stability to HLA-A*0201 molecule. In ELISPOT assay, the cytotoxic T lymphocytes (CTLs) induced by these peptides could release IFN-γ. In cytotoxicity assay, the CTLs induced by p134 and p134-1Y2L9L could specifically lyse peptide-loaded T2 cells. In these two assays, the native peptide, p134, showed the most potent activity. Our results indicated that p134 could be a novel epitope which could serve as a good candidate to develop peptide vaccines against M. tuberculosis.

Research highlights▶ A novel HLA-A*0201-restricted CTL epitope from CFP21, a secreted protein of M. tuberculosis, was identified. ▶ The native epitope, p134, showed potent activities in both ELISPOT and cytotoxicity assays. ▶ p134 could widely induce potent responses in PBMCs of HLA-A*02+ PPD+ individuals.