Proteomic peptide scan of porphyromonas gingivalis fima type ii for searching potential b-cell epitopes.

Abstract

PURPOSE To identify potential antigenic targets for Porphyromonas gingivalis vaccine development. MATERIALS AND METHODS In the present study, we analyzed the Porphyromonas gingivalis, fimA type II primary amino acid sequence and characterized the similarity to the human proteome at the pentapeptide level. RESULTS We found that exact peptide-peptide profiling of the fimbrial antigen versus the human proteome shows that only 19 out of 344 fimA type II pentapeptides are uniquely owned by the bacterial protein. CONCLUSIONS The concept that protein immunogenicity is allocated in rare peptide sequences and the search the Porphyromonas gingivalis fimA type II sequence for peptides unique to the bacterial protein and absent in the human host, might be used in new therapeutical approaches as a significant adjunct to current periodontal therapies.