The ClpP protease is required for the stress tolerance and biofilm formation in Actinobacillus pleuropneumoniae.

The ClpP protease is required for the stress tolerance and biofilm formation in Actinobacillus pleuropneumoniae.
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ClpP 蛋白酶是胸膜肺炎放线杆菌的应激耐受和生物膜形成所必需的。

DOI:
10.1371/journal.pone.0053600
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发表时间:
2013
期刊:
影响因子:
3.7
通讯作者:
Wang C
Wang C
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Xie F;Zhang Y;Li G;Zhou L;Liu S;Wang C

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在呼吸道和肺组织中,平衡的生理反应对于胸膜肺炎放线杆菌在各种类型的挑战中生存至关重要。ClpP是Clp蛋白水解复合物的催化核心,参与多种病原菌的应激反应和生物膜形成的调控。探讨ClpP在A.在猪胸膜肺炎中,通过同源重组将clpP基因缺失,得到突变株S8 Δ clpP。S8 Δ clpP突变体在高温和其他几种胁迫条件下生长的降低表明ClpP蛋白是A.胸膜肺炎有趣的是,我们观察到与野生型菌株相比,S8 Δ clpP突变体在体外摄取铁的能力增加。我们还发现,没有ClpP的细胞显示粗糙和不规则的表面和增加的细胞体积相对于野生型菌株使用扫描电子显微镜(SEM)。共聚焦激光扫描显微镜(CLSM)显示,与野生型菌株相比,S8 Δ clpP突变体显示出减少的生物膜形成。我们检测了野生型S8和S8 Δ clpP突变株的转录谱。胸膜肺炎的RNA测序。我们的分析表明,16个基因的表达改变了clpP基因的缺失。本研究的数据表明ClpP蛋白酶在与A.进一步表明ClpP蛋白酶在毒力调节中的假定作用。
In the respiratory tract and lung tissue, a balanced physiological response is essential for Actinobacillus pleuropneumoniae to survive various types of challenges. ClpP, the catalytic core of the Clp proteolytic complex, is involved in various stresses response and regulation of biofilm formation in many pathogenic bacteria. To investigate the role of ClpP in the virulence of A. pleuropneumoniae, the clpP gene was deleted by homologous recombination, resulting in the mutant strain S8ΔclpP. The reduced growth of S8ΔclpP mutant at high temperatures and under several other stress conditions suggests that the ClpP protein is required for the stress tolerance of A. pleuropneumoniae. Interestingly, we observed that the S8ΔclpP mutant exhibited an increased ability to take up iron in vitro compared to the wild-type strain. We also found that the cells without ClpP displayed rough and irregular surfaces and increased cell volume relative to the wild-type strain using scanning electron microscopy (SEM). Confocal laser scanning microscopy (CLSM) revealed that the S8ΔclpP mutant showed decreased biofilm formation compared to the wild-type strain. We examined the transcriptional profiles of the wild type S8 and the S8ΔclpP mutant strains of A. pleuropneumoniae using RNA sequencing. Our analysis revealed that the expression of 16 genes was changed by the deletion of the clpP gene. The data presented in this study illustrate the important role of ClpP protease in the stress response, iron acquisition, cell morphology and biofilm formation related to A. pleuropneumoniae and further suggest a putative role of ClpP protease in virulence regulation.
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