CHEMOTAXIS OF HUMAN MONOCYTES BY SYNTHETIC PEPTIDES THAT MIMIC SEGMENTS OF PORPHYROMONAS-GINGIVALIS FIMBRIAL PROTEIN

Porphyromonas gingivalis strain 381 fimbriae and their synthetic pepti de segments were assessed for migration-stimulating activity on human peripheral blood monocytes by multiwell chemotaxis assay. P. gingivali s 381 fimbrial protein was found to markedly enhance migration of huma n monocytes. The observed increase in monocyte migration occurred main ly directed toward a positive stimulus (chemotaxis). Furthermore, lipo polysaccharides extracted from P. gingivalis 381 were shown to induce chemotaxis and chemokinesis. It was also revealed that the migration o f monocytes was increased by specific synthetic peptide segments, FP38 1(61-80) and FP381(171-185), that correspond to GKTLAEVKALTTELTAENQE a nd DANYLTGSLTTFNGA, respectively, based on the amino acid sequence of the fimbrial subunit protein proposed by Dickinson et al., and the mig ration stimulation was ascribed to chemotaxis. Furthermore, within the amino acid sequences, the LTXXLTXXN sequence may play an important ro le in binding the organisms to monocytes and macrophages and in the in duction of migration-stimulating activity.