The Actinomyces oris type 2 fimbrial shaft FimA mediates co-aggregation with oral streptococci, adherence to red blood cells and biofilm development.

The Actinomyces oris type 2 fimbrial shaft FimA mediates co-aggregation with oral streptococci, adherence to red blood cells and biofilm development.
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DOI:
10.1111/j.1365-2958.2010.07252.x
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发表时间:
2010-08
影响因子:
3.6
通讯作者:
Ton-That H
Ton-That H
中科院分区:
生物学2区
文献类型:
--
作者:
Mishra A;Wu C;Yang J;Cisar JO;Das A;Ton-That H

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口腔链球菌和放线菌之间的细菌间相互作用及其对牙齿表面和相关宿主细胞的粘附是促进称为牙菌斑的复杂口腔生物膜发展的关键早期事件。这些相互作用在很大程度上取决于与口腔放射菌2型菌毛相关的凝集素样活性,这是一种由轴和尖端菌毛(分别为FimA和FimB)的分选酶(SrtC 2)依赖性聚合组装的表面结构。为了研究特定菌毛蛋白在不同粘附过程中的功能,我们开发了一种方便的新技术,用于产生A.奥里斯。在这里,我们表明,fimB突变体,产生2型菌毛组成的FimA,像野生型coaggregated强烈与受体携带链球菌,与唾液酸酶处理的红细胞凝集,并形成单种生物膜。相比之下,fimA和srtC2突变体缺乏2型菌毛,并且在这些测定中的每一个中都是非粘附的。在各自的突变体中基于质粒的表达的缺失的基因恢复到野生型水平的坚持。这些发现揭示了凝集素样活性的聚合FimA轴,而不是尖端的重要性。FimA的多价粘附功能使其成为探索控制菌斑生物膜形成的新干预策略的理想分子。
Interbacterial interactions between oral streptococci and actinomyces and their adherence to tooth surface and the associated host cells are key early events that promote development of the complex oral biofilm referred to as dental plaque. These interactions depend largely on a lectin-like activity associated with the Actinomyces oris type 2 fimbria, a surface structure assembled by sortase (SrtC2)-dependent polymerization of the shaft and tip fimbrillins, FimA and FimB, respectively. To dissect the function of specific fimbrillins in various adherence processes, we have developed a convenient new technology for generating unmarked deletion mutants of A. oris. Here, we show that the fimB mutant, which produced type 2 fimbriae composed only of FimA, like the wild type coaggregated strongly with receptor-bearing streptococci, agglutinated with sialidase-treated RBC, and formed monospecies biofilm. In contrast, the fimA and srtC2 mutants lacked type 2 fimbriae and were non-adherent in each of these assays. Plasmidbased expression of the deleted gene in respective mutants restored adherence to wild-type levels. These findings uncover the importance of the lectin-like activity of the polymeric FimA shaft rather than the tip. The multivalent adhesive function of FimA makes it an ideal molecule for exploring novel intervention strategies to control plaque biofilm formation.
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