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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the TIR domain from the Brucella melitensis TIR-domain-containing protein TcpB
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Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the TIR domain from the Brucella melitensis TIR-domain-containing protein TcpB

机译：含布鲁氏菌TIR结构域的蛋白TcpB的TIR结构域的克隆，表达，纯化，结晶和初步X射线晶体学分析

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摘要

In mammals, Toll-like receptors (TLRs) recognize conserved microbial molecular signatures and induce an early innate immune response in the host. TLR signalling is mediated by interactions between the cytosolic TIR (Toll/interleukin-1 receptor) domains of the receptor and the adaptor proteins. Increasingly, it is apparent that pathogens target this interaction via pathogen-expressed TIR-domain-containing proteins to modulate immune responses. A TIR-domain-containing protein TcpB has been reported in the pathogenic bacterium Brucella melitensis. Studies have shown that TcpB interferes with the TLR2 and TLR4 signalling pathways to inhibit TLR-mediated inflammatory responses. Such interference may involve TIR-TIR-domain interactions between bacterial and mammalian proteins, but there is a lack of information about these interactions at the molecular level. In this study, the cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the protein construct corresponding to the TIR domain of TcpB (residues 120-250) are reported. The crystals diffracted to 2.6 angstrom resolution, have the symmetry of the monoclinic space group P2(1) and are most likely to contain four molecules in the asymmetric unit. The structure should help in understanding the molecular basis of how TcpB affects the innate immunity of the host.
机译：在哺乳动物中，Toll样受体（TLR）识别保守的微生物分子特征并在宿主中诱导早期的先天免疫应答。 TLR信号传导是通过受体的胞质TIR（Toll /白介素1受体）结构域与衔接子蛋白之间的相互作用介导的。越来越明显的是，病原体通过表达病原体的含TIR域的蛋白质来靶向这种相互作用，从而调节免疫反应。在病原菌布鲁氏菌中已经报道了含有TIR结构域的蛋白TcpB。研究表明，TcpB会干扰TLR2和TLR4信号通路，从而抑制TLR介导的炎症反应。这种干扰可能涉及细菌和哺乳动物蛋白之间的TIR-TIR域相互作用，但是在分子水平上缺乏有关这些相互作用的信息。在这项研究中，报道了对应于TcpB的TIR结构域（残基120-250）的蛋白质构建体的克隆，表达，纯化，结晶和初步X射线晶体学分析。衍射到2.6埃分辨率的晶体具有单斜空间群P2（1）的对称性，最有可能在不对称单元中包含四个分子。该结构应有助于理解TcpB如何影响宿主的先天免疫力的分子基础。

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