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The immunodominant and T-cell epitopes within the fimbrial subunit protein (fimbrilin) of Porphyromonas gingivalis strain 381 were analysed by multi-pin peptide synthesis technology. Six regions with immunodominant epitopes within a sequence of 337 amino acids that reacted with the serum of patients with adult periodontitis were detected. T cells from mice immunised with P. gingivaĭis fimbriae exhibited proliferative responses to P. gingivalis fimbriae or to six 10.mer synthetic peptides from the amino-acid sequence of the fimbrillin. Three synthetic peptides that contained the regions responsible for the immunodominant epitopes as well as those which coincided with a T-cell epitope of P. gingivalis fimbrial molecules—FP381(142–161), FP381(202–221) and FP381(216–243)—were selected and synthesised. When guinea-pigs were immunised with fimbriae or one of the three synthetic peptide segments and an adjuvant in Freund’s incomplete adjuvant, enhanced production of the antigen-specific IgG antibodies was induced in the serum of the animals. Furthermore, of the three synthetic peptides tested, FP381(202–221) produced the greatest protective immune response in guinea-pigs infected with P. gingivaĭis and this was more effective than the native fimbrial protein.
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