The Fusobacterium nucleatum outer membrane protein RadD is an arginine-inhibitable adhesin required for inter-species adherence and the structured architecture of multispecies biofilm.
The Fusobacterium nucleatum outer membrane protein RadD is an arginine-inhibitable adhesin required for inter-species adherence and the structured architecture of multispecies biofilm.
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DOI：
10.1111/j.1365-2958.2008.06503.x
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发表时间：
2009-01
影响因子：
3.6
通讯作者：
Shi W
中科院分区：
文献类型：
--
作者：
Kaplan CW;Lux R;Haake SK;Shi W
疑似牙周病原体核梭杆菌的一个决定性特征是它能够粘附大量口腔细菌。这一显著特征被认为在口腔生物膜的形成和发病机制中起着重要作用，梭杆菌被认为是口腔生物膜结构中的中心“桥接生物”，将原本不会相互作用的物种聚集在一起。先前的研究表明，这些细菌相互作用是由半乳糖或精氨酸抑制粘附素介导的，尽管这些粘附素的作用和性质的遗传证据仍然难以捉摸。为了在分子水平上对这些粘附素进行表征，我们对可遗传转化的F. nucleatum菌株ATCC 23726进行了粘附特性筛选，发现精氨酸抑制粘附明显，而半乳糖抑制粘附未被检测到。从F. nucleatum ATCC 23726的膜组分中分离到6个潜在的精氨酸结合蛋白，并通过质谱鉴定为F. nucleatum外膜蛋白家族的成员。编码这6个精氨酸抑制粘附候选基因和另外两个同源基因的失活表明，只有携带Fn1526插入的突变衍生物（现在称为radD）与革兰氏阳性“早期口腔定植体”的代表显著减少共聚集。缺乏由radD编码的350 kDa外膜蛋白导致在血链球菌ATCC 10556存在下生长时，无法形成与亲本菌株相同的广泛结构的生物膜。这些发现表明radD参与了精氨酸抑制核仁梭菌的粘附，并为核仁梭菌粘附素在种间粘附和多物种生物膜形成中发挥重要作用提供了明确的分子证据。
A defining characteristic of the suspected periodontal pathogen Fusobacterium nucleatum is its ability to adhere to a plethora of oral bacteria. This distinguishing feature is suggested to play an important role in oral biofilm formation and pathogenesis, with fusobacteria proposed to serve as central “bridging organisms” in the architecture of the oral biofilm bringing together species which would not interact otherwise. Previous studies indicate that these bacterial interactions are mediated by galactose- or arginine-inhibitable adhesins although genetic evidence for the role and nature of these proposed adhesins remains elusive. To characterize these adhesins at the molecular level, the genetically transformable F. nucleatum strain ATCC 23726 was screened for adherence properties, and arginine inhibitable adhesion was evident, while galactose-inhibitable adhesion was not detected. Six potential arginine binding proteins were isolated from the membrane fraction of F. nucleatum ATCC 23726 and identified via mass spectroscopy as members of the outer membrane family of proteins in F. nucleatum. Inactivation of the genes encoding these six candidates for arginine-inhibitable adhesion and two additional homologues revealed that only a mutant derivative carrying an insertion in Fn1526 (now designated as radD) demonstrated significantly decreased co-aggregation with representatives of the Gram-positive “early oral colonizers”. Lack of the 350 kDa outer membrane protein encoded by radD resulted in the failure to form the extensive structured biofilm observed with the parent strain when grown in the presence of Streptococcus sanguinis ATCC 10556. These findings indicate that radD is responsible for arginine-inhibitable adherence of F. nucleatum and provides definitive molecular evidence that F. nucleatum adhesins play a vital role in inter-species adherence and multispecies biofilm formation.
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影响因子：
3.2
作者：
Haake, SK;Yoder, SC;Podkaminer, K
通讯作者：
Podkaminer, K
影响因子：
3.1
作者：
OHTA, K;MAKINEN, KK;LOESCHE, WJ
通讯作者：
LOESCHE, WJ
影响因子：
3.1
作者：
CISAR, JO;KOLENBRANDER, PE;MCINTIRE, FC
通讯作者：
MCINTIRE, FC
影响因子：
3.6
作者：
Laarmann, S;Cutter, D;St Geme, JW
通讯作者：
St Geme, JW
DOI：
10.1073/pnas.0507923103
发表时间：
2006-03-28
影响因子：
11.1
作者：
Junker, M;Schuster, CC;Clark, PL
通讯作者：
Clark, PL