FIBRONECTIN-BINDING DOMAIN OF P-GINGIVALIS FIMBRIAE

P. gingivalis fimbriae play an important role in attachment of bacteri a to various salivary components as well as to host cells and matrix p roteins including fibronectin. In the present study, we investigated t he binding domain of P. gingivalis fimbriae to fibronectin using synth etic peptides. A series of 20 mer fimbrillin peptides were used. Bindi ng of fibronectin to purified fimbriae and synthetic peptides was assa yed using polyclonal fibronectin antibodies as well as iodinated fibro nectin. Purified fimbriae and peptide 126-146 (RMAFTEIKVQMSAAYDNIYTF) showed high levels of binding to fibronectin, while peptide 318-337(HL NVQCTVAEWVLVGQNATW) showed low but statistically significant binding. Our results suggest V-Q-X-X-X-A or V-X-X-X A common domain/domains pre sent in both peptides might be involved in protein-protein interaction between P. gingivalis fimbriae and fibronectin. (C) 1995 Academic Pre ss, Inc.