Porphyromonas gingivalis fimbriae mediate coaggregation with Streptococcus oralis through specific domains
Porphyromonas gingivalis fimbriae mediate coaggregation with Streptococcus oralis through specific domains
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DOI：
10.1177/00220345970760040601
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发表时间：
1997-04-01
影响因子：
7.6
通讯作者：
Shizukuishi, S
中科院分区：
文献类型：
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作者：
Amano, A;Fujiwara, T;Shizukuishi, S
菌毛是牙龈卟啉单胞菌细胞表面的主要粘附成分。在这项研究中，我们评估了菌毛与口腔链球菌共聚集的作用。从牙龈假单胞菌中纯化的菌毛在50 μ g/mL的浓度下竞争性地抑制了100%的共聚集。另一方面，从牙龈假单胞菌中分离的相同数量的脂多糖仅被菌毛水平的25%所抑制。牙龈卟啉卟啉灭活突变体未能表现出明显的共聚集活性。将菌毛加入到各种链球菌菌株的溶液中，在浓度为10至30 μ g/mL时，菌毛会自聚集。λ -精氨酸（20 ~ 40 mM/L）可抑制菌毛诱导的自聚集。碘化菌毛与固定在硝化纤维素膜上的口腔葡萄球菌细胞发生反应，细胞在100℃加热后结合能力减弱。重组纤维蛋白（r- film，对应原生纤维蛋白1 ~ 337个残基）对牙龈卟啉卟啉的共聚集也有100%的抑制作用。缺乏c端51个残基的r-Fim变体（残基1 ~ 286）与r-Fim一样具有抑制作用。然而，没有c -末端72个残基的变体（残基1至265）失去了77%的抑制活性。这些结果表明，残基266 ~ 286包含一个与牙龈卟啉单胞菌和口腔卟啉单胞菌共聚集有关的结构域。研究了266 ~ 286、266 ~ 337和287 ~ 337三个残基对应的多肽的抑制作用。在1.5 nmol/mL的浓度下，266 ~ 286和266 ~ 337肽的抑制率分别为96%和100%。肽287 ~ 337也有显著的抑制作用，但抑制程度略低于肽266 ~ 286。牙龈假单胞菌菌毛似乎与链球菌共聚集，可能是通过后者的粘附蛋白分子参与的，并且菌毛在c端残基266至337处具有与口腔链球菌相互作用的几个结构域。
Fimbriae are major adhesive components on the cell surface of Porphyromonas gingivalis. In this study, we evaluated the role of fimbriae in coaggregation with Streptococcus oralis. Fimbriae purified from P. gingivalis competitively inhibited the coaggregation by 100% at a concentration of 50 mu g/mL. On the other hand, the same amount of lipopolysaccharide isolated from P. gingivalis was inhibited by only 25% of the level of the fimbriae. A fimA-inactivated mutant of P. gingivalis failed to show distinct coaggregation activity. Fimbriae added to a solution of various strains of streptococci caused their self-aggregation at a concentration of 10 to 30 mu g/mL. The self-aggregation induced by fimbriae was inhibited by lambda-arginine (20 to 40 mM/L). Iodinated fimbriae reacted with S. oralis cells immobilized on the nitrocellulose membrane, and 100 degrees C heating of the cells diminished the binding abilities. Recombinant fimbrillin (r-Fim, corresponding to whole residues 1 to 337 of native fimbrillin) of P. gingivalis also showed 100% inhibition of the coaggregation. The r-Fim variant (residues 1 to 286) lacking the C-terminal 51 residues was as inhibitory as r-Fim. However, the variant (residues 1 to 265) without the C-terminal 72 residues lost 77% of the inhibitory activity. These findings suggested that residues 266 to 286 contain a domain involved in the coaggregation of P. gingivalis with S. oralis. Inhibition by three polypeptides corresponding to residues 266 to 286, 266 to 337, and 287 to 337 was studied. Peptides 266 to 286 and 266 to 337 inhibited by 96 and 100%, respectively, at a concentration of 1.5 nmol/mL. Peptide 287 to 337 also showed a significant inhibitory effect but to a slightly lesser extent than that of peptide 266 to 286. P. gingivalis fimbriae appear to be involved in coaggregation with streptococci, probably through an adhesive protein molecule(s) of the latter, and the fimbriae possess several domains in the C-terminal residues 266 to 337 for interaction with S. oralis.