| Co-Investigator(Kenkyū-buntansha) |
TANAKA Takaharu Suntory Ltd., Health Care Div., Director, ヘルスケア事業部, 部長
KAWABATA Shigetada Osaka University Faculty of Dentistry, Associate Professor, 歯学部, 助教授 (50273694)
木村 重信 大阪大学, 歯学部, 助教授 (10177917)
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| Budget Amount *help |
¥11,400,000 (Direct Cost: ¥11,400,000)
Fiscal Year 1998: ¥4,600,000 (Direct Cost: ¥4,600,000)
Fiscal Year 1997: ¥6,800,000 (Direct Cost: ¥6,800,000)
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| Research Abstract |
Porphyromonas gingivalis, a Gram-negative anaerobe, is known to be involved in the pathogenesis of periodontitis. P.gingivalis fimbriae are thought to play an important role in the colonization and invasion to periodontal tissues. We analyzed the interactions of P.gingivalis fimbriae with human extracellar matrix proteins (i. e., fibronectin, laminin, collagen), hemoglobin, fibrinogen and salivary components (i.e., proline-rich protein [PRP], proline-rich glycoprotein [PRG] and statherin) based on surface plasmon resonance (SPR) spectroscopy using a biomolecular interaction analyzing system (BlAcore). Fimbriae were observed to have high affinity with all the human proteins we used. Arginine-specific protease from P.gingivalis can expose the C-terminal Arg residue in the matrix proteins, and results in enhanced fimbria-mediated binding of this organism. We examined the binding of fimbriae to some synthetic dipeptides by using affinity column chromatography. Only Gly-Arg ligand was obser
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ved to have affinity with fimbriae. In addition, we analyzed the interaction of fimbriae and immobilized fibronectins (intact or partially degraded fibronectin by the protease). BlAcore profiles demonstrated an enhanced interaction between fimbriae and protease-degraded fibronectin. This enhancement was inhibited by the addition of L-Arg, or oligopeptides including bradykinin containing the Arg residue at the C-terminus, suggesting that the P.gingivalis fimbriae may potentially have an ability to bind tightly to the C-terminal Arg residue. The peptide PRP-C, which is corresponding to the C-terminal segment composed of 21 amino acid residues of PRP, and a potent inhibitor of PRP-fimbriae interaction, dramatically inhibited the fimbrial association to the salivery proteins and collagen, and was less inhibitory against fibronectin and laminin on BlAcore. These observations suggested that P.gin givalis fimbriae interact diversly with the host proteins by different mechanisms, which eventually promotes the bacterial adherence to the oral cavity. Less
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