Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6
Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6
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DOI：
10.1038/sj.emboj.7600732
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发表时间：
2005-07-20
期刊：
影响因子：
11.4
通讯作者：
Carr, MD
中科院分区：
文献类型：
--
作者：
Renshaw, PS;Lightbody, KL;Carr, MD
分泌的结核分枝杆菌复合蛋白 CFP-10 和 ESAT-6 最近被证明在结核病发病机制中发挥重要作用。我们确定了由 CFP-10 和 ESAT-6 形成的紧密 1:1 复合物的溶液结构，并利用荧光显微镜证明了该复合物与巨噬细胞和单核细胞表面的特异性结合。该复合物的一个显着特征是由 CFP-10 C 末端形成的长柔性臂，人们发现它对于与细胞表面的结合至关重要。 CFP-10 的表面特征。 ESAT-6 复合物以及观察到的与特定宿主细胞的结合，强烈表明该复合物具有关键的信号传导作用，其中与细胞表面受体的结合导致宿主细胞行为的调节，从而有利于病原体。
The secreted Mycobacterium tuberculosis complex proteins CFP-10 and ESAT-6 have recently been shown to play an essential role in tuberculosis pathogenesis. We have determined the solution structure of the tight, 1:1 complex formed by CFP-10 and ESAT-6, and employed fluorescence microscopy to demonstrate specific binding of the complex to the surface of macrophage and monocyte cells. A striking feature of the complex is the long flexible arm formed by the C-terminus of CFP-10, which was found to be essential for binding to the surface of cells. The surface features of the CFP-10. ESAT-6 complex, together with observed binding to specific host cells, strongly suggest a key signalling role for the complex, in which binding to cell surface receptors leads to modulation of host cell behaviour to the advantage of the pathogen.