A Lucchese1, A Guida2, G Capone3, G Donnarumma4, L Laino1, M Petruzzi5, R Serpico1, F Silvestre6, M Gargari7. 1. Multidisciplinary Department of Medical-Surgical and Odontostomatological Specialties, Second University of Naples SUN, Naples, Italy. 2. Postgraduate School in Oral Surgery, Department of Neurosciences, Reproductive and Odontostomatological Sciences, University of Naples "Federico II", Naples, Italy. 3. Department of Biosciences, Biotechnologies and Pharmacological Sciences, University of Bari, Bari, Italy. 4. Department of Experimental Medicine, Section of Microbiology and Clinical Microbiology, Second University of Naples, Naples, Italy. 5. Interdisciplinary Department of Medicine (DIM) - Section of Dentistry, University "Aldo Moro" of Bari, Bari, Italy. 6. Departimento de Estomatologia, University of Valencia, Valencia, Spain. 7. Department of Clinical Sciences And Translational Medicine, University of Rome "Tor Vergata", Rome, Italy; Department of dentistry "Fra G.B. Orsenigo - Ospedale San Pietro F.B.F.", Rome, Italy.
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.
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.
Entities:
Keywords:
bacterial versus human peptide overlap; low-similarity peptides; peptide vaccine; periodontitis
Authors: Reinhard Dummer; Abraham Mittelman; Francesco P Fanizzi; Guglielmo Lucchese; Jörg Willers; Darja Kanduc Journal: Int J Cancer Date: 2004-09-20 Impact factor: 7.396