Open AccessSpecific interactions between Porphyromonas gingivalis fimbriae and human extracellular matrix proteins
Author(s) -
Nakamura Takayuki,
Amano Atsuo,
Nakagawa Ichiro,
Hamada Shigeyuki
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13630.x
Subject(s) - fimbria , vitronectin , porphyromonas gingivalis , fibronectin , laminin , chemistry , extracellular matrix , thrombospondin , surface plasmon resonance , bacterial adhesin , pilus , microbiology and biotechnology , biochemistry , biophysics , biology , matrix metalloproteinase , escherichia coli , bacteria , metalloproteinase , materials science , genetics , nanoparticle , gene , nanotechnology
The interactions of the extracellular matrix (ECM) proteins (laminin, elastin, fibronectin, type I collagen, thrombospondin and vitronectin) with the fimbriae of Porphyromonas gingivalis were analyzed based on surface plasmon resonance (SPR) spectroscopy using a biomolecular interaction analyzing system (BIAcore). The BIAcore profiles demonstrated that fimbriae specifically bound to all of the ECM proteins with significant association constants ( K a ). Vitronectin showed the highest affinity to fimbriae ( K a =3.79×10 6 M −1 ), while the affinity of laminin was lowest ( K a =2.15×10 6 M −1 ). A synthetic peptide which is a potent inhibitor of fimbrial binding to salivary proteins was not significantly effective on the fimbrial interactions with the ECM proteins. Using polystyrene microtiter plates revealed that P. gingivalis fimbriae bound markedly to immobilized fibronectin and type I collagen, while the interaction of fimbriae with the other ECM proteins was not clearly demonstrated. These results suggest that interactions between fimbriae and the ECM proteins occur with specific affinities which are not mediated by mechanisms identical to those of salivary proteins. It was also shown that SPR spectroscopy is a useful method to analyze these specific interactions.