The Staphylococcus aureus Extracellular Adherence Protein Eap Is a DNA Binding Protein Capable of Blocking Neutrophil Extracellular Trap Formation.
The Staphylococcus aureus Extracellular Adherence Protein Eap Is a DNA Binding Protein Capable of Blocking Neutrophil Extracellular Trap Formation.
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DOI：
10.3389/fcimb.2018.00235
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发表时间：
2018
影响因子：
5.7
通讯作者：
Bischoff M
中科院分区：
文献类型：
--
作者：
Eisenbeis J;Saffarzadeh M;Peisker H;Jung P;Thewes N;Preissner KT;Herrmann M;Molle V;Geisbrecht BV;Jacobs K;Bischoff M
金黄色葡萄球菌的细胞外粘附蛋白（Eap）是已知发挥许多粘附和免疫调节特性的分泌蛋白。在这里，我们描述了这种多功能分泌因子的内在DNA结合活性。通过使用原子力显微镜，我们提供的证据表明，Eap可以结合和聚集DNA。而DNA底物的来源（例如，真核生物、细菌、噬菌体和人工DNA）似乎不是主要重要的，DNA结构（例如，线性或环状）对于Eap结合和凝聚DNA的能力起关键作用。进一步的功能测定证实了Eap作为DNA结合蛋白的性质，因为Eap抑制了由DNA-组蛋白支架组成的“中性粒细胞胞外陷阱”（NET）的形成，其被认为是作为嗜中性粒细胞介导的胞外陷阱机制发挥作用。Eap的DNA结合和聚集活性可能因此保护S。金黄色葡萄球菌对抗宿主的特异性抗微生物防御反应。
The extracellular adherence protein (Eap) of Staphylococcus aureus is a secreted protein known to exert a number of adhesive and immunomodulatory properties. Here we describe the intrinsic DNA binding activity of this multifunctional secretory factor. By using atomic force microscopy, we provide evidence that Eap can bind and aggregate DNA. While the origin of the DNA substrate (e.g., eukaryotic, bacterial, phage, and artificial DNA) seems to not be of major importance, the DNA structure (e.g., linear or circular) plays a critical role with respect to the ability of Eap to bind and condense DNA. Further functional assays corroborated the nature of Eap as a DNA binding protein, since Eap suppressed the formation of “neutrophil extracellular traps” (NETs), composed of DNA-histone scaffolds, which are thought to function as a neutrophil-mediated extracellular trapping mechanism. The DNA binding and aggregation activity of Eap may thereby protect S. aureus against a specific anti-microbial defense reaction from the host.
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