Burkholderia pseudomallei type III secreted protein BipC: role in actin modulation and translocation activities required for the bacterial intracellular lifecycle.
Burkholderia pseudomallei type III secreted protein BipC: role in actin modulation and translocation activities required for the bacterial intracellular lifecycle.
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作者：
Kang WT;Vellasamy KM;Rajamani L;Beuerman RW;Vadivelu J
类鼻疽是一种由兼性胞内病原体类鼻疽伯克霍尔德菌引起的感染，已被归类为一种新兴疾病，患者数量以惊人的速度稳步增加。B。假单胞菌具有多种毒力决定因子，使其能够侵入宿主并逃避宿主免疫应答，例如III型分泌系统（TTSS）。这种特殊分泌系统的产物对B特别重要。类鼻疽感染。缺乏TTSS的一个或多个组分表明B的细胞内生命周期存在不同程度的缺陷。假鼻疽进一步了解参与B的蛋白质的功能作用。假鼻疽TTSS将使我们能够剖析B之谜。类鼻疽-宿主细胞相互作用。在这项研究中，BipC（一种转运蛋白），这是以前报道的参与B的发病机制。利用生物信息学和分子生物学方法进一步表征了假鼻疽。首先从B中PCR扩增出编码推定的侵袭蛋白的bipC基因。pseudomallei K96243基因组DNA，并克隆到表达载体中用于在大肠杆菌中过表达。随后纯化可溶性蛋白并测定肌动蛋白聚合和解聚。如通过在体外抑制肌动蛋白的能力所证明的，证实了BipC破坏宿主肌动蛋白动力学。同源模建也被尝试来预测BipC的结构。总的来说，我们的研究结果表明，由bipC基因编码的蛋白质作为一个效应子参与肌动蛋白结合活性，以促进B的内化。pseudomallei进入宿主细胞。
Melioidosis, an infection caused by the facultative intracellular pathogen Burkholderia pseudomallei, has been classified as an emerging disease with the number of patients steadily increasing at an alarming rate. B. pseudomalleipossess various virulence determinants that allow them to invade the host and evade the host immune response, such as the type III secretion systems (TTSS). The products of this specialized secretion system are particularly important for the B. pseudomallei infection. Lacking in one or more components of the TTSS demonstrated different degrees of defects in the intracellular lifecycle of B. pseudomallei. Further understanding the functional roles of proteins involved in B. pseudomallei TTSS will enable us to dissect the enigma of B. pseudomallei-host cell interaction. In this study, BipC (a translocator), which was previously reported to be involved in the pathogenesis of B. pseudomallei, was further characterized using the bioinformatics and molecular approaches. The bipCgene, coding for a putative invasive protein, was first PCR amplified from B. pseudomallei K96243 genomic DNA and cloned into an expression vector for overexpression in Escherichia coli. The soluble protein was subsequently purified and assayed for actin polymerization and depolymerization. BipC was verified to subvert the host actin dynamics as demonstrated by the capability to polymerize actin in vitro. Homology modeling was also attempted to predict the structure of BipC. Overall, our findings identified that the protein encoded by the bipC gene plays a role as an effector involved in the actin binding activity to facilitate internalization of B. pseudomalleiinto the host cells.
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