Novel fimbrilin PGN_1808 in Porphyromonas gingivalis.
Novel fimbrilin PGN_1808 in Porphyromonas gingivalis.
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DOI：
10.1371/journal.pone.0173541
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发表时间：
2017
期刊：
影响因子：
3.7
通讯作者：
Yoshimura F
中科院分区：
文献类型：
--
作者：
Nagano K;Hasegawa Y;Yoshida Y;Yoshimura F
牙龈卟啉单胞菌是一种牙周病革兰氏阴性厌氧菌，通常表达两种类型的菌毛，FimA和Mfa1。然而，最近通过计算机结构同源性搜索在牙龈卟啉单胞菌菌株ATCC 33277中鉴定出一种新的潜在菌毛蛋白PGN_1808。在这项研究中，我们通过实验研究了蛋白质是否形成了菌毛结构。阴离子交换层析显示，蛋白质的洗脱峰与FimA和Mfa1的主要菌毛蛋白的洗脱峰不相同，表明PGN_1808不是这些菌毛的组分。电泳分析表明，PGN_1808形成聚合物，尽管与FimA和Mfa 1相比，它是去污剂和热不稳定的。透射电子显微镜显示，在PGN_1808过表达牙龈卟啉单胞菌突变体（FimA和Mfa1菌毛缺陷）和PGN_1808组分的细胞表面上存在丝状结构（2 × 3 nm × 200 × 400 nm）。通过蛋白质印迹法在84株牙龈卟啉单胞菌野生型菌株中的81株中检测到PGN_1808，表明该蛋白质通常存在于牙龈卟啉单胞菌中。
Porphyromonas gingivalis, a periodontopathic gram-negative anaerobic bacterium, generally expresses two types of fimbriae, FimA and Mfa1. However, a novel potential fimbrilin, PGN_1808, in P. gingivalis strain ATCC 33277 was recently identified by an in silico structural homology search. In this study, we experimentally examined whether the protein formed a fimbrial structure. Anion-exchange chromatography showed that the elution peak of the protein was not identical to those of the major fimbrilins of FimA and Mfa1, indicating that PGN_1808 is not a component of these fimbriae. Electrophoretic analyses showed that PGN_1808 formed a polymer, although it was detergent and heat labile compared to FimA and Mfa1. Transmission electron microscopy showed filamentous structures (2‒3 nm × 200‒400 nm) on the cell surfaces of a PGN_1808-overexpressing P. gingivalis mutant (deficient in both FimA and Mfa1 fimbriae) and in the PGN_1808 fraction. PGN_1808 was detected in 81 of 84 wild-type strains of P. gingivalis by western blotting, suggesting that the protein is generally present in P. gingivalis.