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首页> 外文期刊>Infection and immunity >Synthetic peptides analogous to the fimbrillin sequence inhibit adherence of Porphyromonas gingivalis.
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Synthetic peptides analogous to the fimbrillin sequence inhibit adherence of Porphyromonas gingivalis.

机译：类似于纤毛蛋白序列的合成肽抑制牙龈卟啉单胞菌的粘附。

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摘要

Fimbriae are important in the adherence of many bacterial species to the surfaces they eventually colonize. Porphyromonas (Bacteroides) gingivalis fimbriae appear to mediate adherence to oral epithelial cells and the pellicle-coated tooth surface. The role and contribution of fimbriae in the binding of P. gingivalis to hydroxyapatite (HAP) coated with saliva as a model for the pellicle-coated tooth surface were investigated. 3H-labeled P. gingivalis or the radioiodinated purified fimbriae were incubated with 2 mg of HAP beads coated with whole human saliva (sHAP) and layered on 100% Percoll to separate unbound from sHAP-bound components. The radioactivity of the washed beads was a measure of the bound components. The binding of P. gingivalis 2561 (381) cells and that of purified fimbriae were concentration dependent and saturable at approximately 10(8) cells and 40 micrograms of fimbriae added, respectively. The addition of fimbriae inhibited binding of P. gingivalis to sHAP beads by 65%, while the 75-kDa protein, which is another major surface component of P. gingivalis 2561, did not show significant inhibition, suggesting that the fimbriae are important in adherence. Encapsulated and sparsely fimbriated P. gingivalis W50 did not bind to sHAP beads. On the basis of the predicted sequence of the fimbrillin, a structural subunit of fimbriae, a series of peptides were synthesized and used to localize the active fimbrillin domains involved in P. gingivalis adherence to sHAP beads. Peptides from the carboxyl-terminal one-third of the fimbrillin strongly inhibited P. gingivalis binding to sHAP beads. Active residues within the sequence of inhibitory peptide 226-245 (peptide containing residues 226 to 245) and peptide 293-306 were identified by using smaller fragments prepared either by trypsin cleavage of the peptide 226-245 or by synthesis of smaller segments of peptide 293-306. Hemagglutinin activity, lectinlike binding, and ionic interaction did not seem to be involved in this binding since lysine, arginine, carbohydrates, and calcium ions failed to affect the binding of P. gingivalis. The observation that poly-L-lysine, bovine serum albumin, and defatted bovine serum albumin, even at high concentrations, only partially blocked the binding of P. gingivalis indicates that hydrophobic interactions are not the major forces involved in P. gingivalis binding to sHAP beads. Protease inhibitors such as EDTA, leupeptin, pepstatin, 1,10-phenanthroline, and phenylmethylsulfonyl fluoride did not interfere with the binding of P. gingivalis. However, the binding of P. gingivalis to trypsin- or chymotrypsin-pretreated sHAP beads was reduced.(ABSTRACT TRUNCATED AT 400 WORDS)
机译：菌毛在许多细菌物种粘附到它们最终定殖的表面方面很重要。牙龈卟啉单胞菌（Bacteroides）菌毛似乎介导了对口腔上皮细胞和覆盖有防护膜的牙齿表面的粘附。研究了菌毛在牙龈卟啉单胞菌与涂有唾液的羟基磷灰石（HAP）的结合中的作用和贡献，该膜是薄膜覆盖膜的模型。将3H标记的牙龈卟啉单胞菌或放射性碘标记的纯化菌毛与2 mg涂有全人唾液（sHAP）的HAP珠一起孵育，并铺在100％Percoll上以分离未结合的与sHAP结合的组分。洗涤过的珠子的放射性是结合成分的量度。牙龈卟啉单胞菌2561（381）细胞和纯化菌毛的结合是浓度依赖性的，在分别加入约10（8）个细胞和加入40微克菌毛后，它们是可饱和的。菌毛的添加抑制齿龈假单胞菌与sHAP珠的结合达65％，而作为齿龈假单胞菌2561另一个主要表面成分的75-kDa蛋白没有显示出明显的抑制作用，表明该菌毛在粘附方面很重要。 。封装和稀疏的纤维状齿龈假单胞菌W50不与sHAP珠结合。根据菌毛蛋白的预测序列，菌毛蛋白的结构亚基，合成了一系列肽，并用于定位参与牙龈卟啉单胞菌粘附于sHAP珠的活性菌毛蛋白结构域。来自纤丝蛋白的羧基末端三分之一的肽强烈抑制牙龈卟啉单胞菌与sHAP珠的结合。通过使用胰蛋白酶切割肽226-245或合成较小的肽293片段而制备的较小片段来鉴定抑制性肽226-245序列中的活性残基（含有226至245残基的肽）。 -306。血凝素活性，凝集素样结合和离子相互作用似乎不参与这种结合，因为赖氨酸，精氨酸，碳水化合物和钙离子不能影响牙龈卟啉单胞菌的结合。聚-L-赖氨酸，牛血清白蛋白和脱脂的牛血清白蛋白即使在高浓度下也只能部分阻止牙龈卟啉单胞菌的结合的观察结果表明，疏水相互作用不是牙龈卟啉单胞菌与sHAP结合的主要作用力珠子。蛋白酶抑制剂，例如EDTA，亮肽素，胃抑素，1,10-菲咯啉和苯甲基磺酰氟不干扰牙龈卟啉单胞菌的结合。但是，牙龈卟啉单胞菌与胰蛋白酶或胰凝乳蛋白酶预处理的sHAP珠的结合减少了（摘要截短了400个单词）

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