Major membrane protein TDE2508 regulates adhesive potency in Treponema denticola.

Major membrane protein TDE2508 regulates adhesive potency in Treponema denticola.
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DOI:
10.1371/journal.pone.0089051
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发表时间:
2014
期刊:
影响因子:
3.7
通讯作者:
Yoshimura F
Yoshimura F
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Abiko Y;Nagano K;Yoshida Y;Yoshimura F

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齿垢密螺旋体是一种与牙周疾病相关的革兰氏阴性口腔螺旋体,其培养和遗传操作仍具有挑战性。在本研究中,我们在市售培养基的基础上配制了一种简单的培养基,并建立了一种高效的转化方法。然后我们分析了T.鉴定了16种主要的膜相关蛋白,并对其中一种TDE 2508进行了鉴定,其生物学功能尚不清楚。虽然这种蛋白质,表现出复杂的构象,可能是定位在外膜,我们没有发现确凿的证据表明,它是暴露在细胞表面。有趣的是,TDE 2508缺陷型突变体在人牙龈上皮细胞上表现出显著增加的生物膜形成和粘附活性。然而,蛋白质缺乏没有改变自聚集,共聚集与牙龈卟啉单胞菌,血凝,细胞表面疏水性,运动性,或Msp的表达,据报道,这是一个粘附分子在这种细菌。总之,主要膜蛋白TDE 2508调节T.但其潜在机制尚不清楚。
The cultivation and genetic manipulation of Treponema denticola, a Gram-negative oral spirochaeta associated with periodontal diseases, is still challenging. In this study, we formulated a simple medium based on a commercially available one, and established a transformation method with high efficiency. We then analyzed proteins in a membrane fraction in T. denticola and identified 16 major membrane-associated proteins, and characterized one of them, TDE2508, whose biological function was not yet known. Although this protein, which exhibited a complex conformation, was presumably localized in the outer membrane, we did not find conclusive evidence that it was exposed on the cell surface. Intriguingly, a TDE2508-deficient mutant exhibited significantly increased biofilm formation and adherent activity on human gingival epithelial cells. However, the protein deficiency did not alter autoaggregation, coaggregation with Porphyromonas gingivalis, hemagglutination, cell surface hydrophobicity, motility, or expression of Msp which was reported to be an adherent molecule in this bacteria. In conclusion, the major membrane protein TDE2508 regulates biofilm formation and the adhesive potency of T. denticola, although the underlying mechanism remains unclear.
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