Sojar H T, Lee J Y, Genco R J
Department of Oral Biology, School of Dental Medicine, State University of New York at Buffalo 14214, USA.
Biochem Biophys Res Commun. 1995 Nov 22;216(3):785-92. doi: 10.1006/bbrc.1995.2690.
P. gingivalis fimbriae play an important role in attachment of bacteria to various salivary components as well as to host cells and matrix proteins including fibronectin. In the present study, we investigated the binding domain of P. gingivalis fimbriae to fibronectin using synthetic peptides. A series of 20 mer fimbrillin peptides were used. Binding of fibronectin to purified fimbriae and synthetic peptides was assayed using polyclonal fibronectin antibodies as well as iodinated fibronectin. Purified fimbriae and peptide 126-146 (RMAFTEIKVQMSAAYDNIYTF) showed high levels of binding to fibronectin, while peptide 318-337(HLNVQCTVAEWVLVGQNATW) showed low but statistically significant binding. Our results suggest V-Q-X-X-X-A or V-X-X-X A common domain/domains present in both peptides might be involved in protein-protein interaction between P. gingivalis fimbriae and fibronectin.
牙龈卟啉单胞菌菌毛在细菌与各种唾液成分以及宿主细胞和包括纤连蛋白在内的基质蛋白的附着过程中发挥着重要作用。在本研究中，我们使用合成肽研究了牙龈卟啉单胞菌菌毛与纤连蛋白的结合结构域。使用了一系列20个氨基酸残基的菌毛蛋白肽。使用多克隆纤连蛋白抗体以及碘化纤连蛋白测定纤连蛋白与纯化菌毛和合成肽的结合。纯化的菌毛和肽126 - 146（RMAFTEIKVQMSAAYDNIYTF）显示出与纤连蛋白的高水平结合，而肽318 - 337（HLNVQCTVAEWVLVGQNATW）显示出低但具有统计学意义的结合。我们的结果表明，两种肽中存在的共同结构域V - Q - X - X - X - A或V - X - X - X A可能参与牙龈卟啉单胞菌菌毛与纤连蛋白之间的蛋白质 - 蛋白质相互作用。
