Chemotaxis of human monocytes by synthetic peptides that mimic segments of Porphyromonas gingivalis fimbrial protein.

Porphyromonas gingivalis strain 381 fimbriae and their synthetic peptide segments were assessed for migration-stimulating activity on human peripheral blood monocytes by multiwell chemotaxis assay. P. gingivalis 381 fimbrial protein was found to markedly enhance migration of human monocytes. The observed increase in monocyte migration occurred mainly directed toward a positive stimulus (chemotaxis). Furthermore, lipopolysaccharides extracted from P. gingivalis 381 were shown to induce chemotaxis and chemokinesis. It was also revealed that the migration of monocytes was increased by specific synthetic peptide segments, FP381(61-80) and FP381(171-185), that correspond to GKTLAEVKALTTELTAENQE and DANYLTGSLTTFNGA, respectively, based on the amino acid sequence of the fimbrial subunit protein proposed by Dickinson et al., and the migration stimulation was ascribed to chemotaxis. Furthermore, within the amino acid sequences, the LTXXLTXXN sequence may play an important role in binding the organisms to monocytes and macrophages and in the induction of migration-stimulating activity.