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首页> 外文期刊>Journal of bacteriology >The Propeptide of the Metalloprotease of Listeria monocytogenes Controls Compartmentalization of the Zymogen during Intracellular Infection
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The Propeptide of the Metalloprotease of Listeria monocytogenes Controls Compartmentalization of the Zymogen during Intracellular Infection

机译：单核细胞增生李斯特氏菌金属蛋白酶的肽在细胞内感染过程中控制发酵原的区室化

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Integral to the virulence of the intracellular bacterial pathogen Listeria monocytogenes is its metalloprotease (Mpl). Mpl regulates the activity and compartmentalization of the bacterial broad-range phospholipase C (PC-PLC). Mpl is secreted as a proprotein that undergoes intramolecular autocatalysis to release its catalytic domain. In related proteases, the propeptide serves as a folding catalyst and can act either in cis or in trans. Propeptides can also influence protein compartmentalization and intracellular trafficking or decrease folding kinetics. In this study, we aimed to determine the role of the Mpl propeptide by monitoring the behavior of Mpl synthesized in the absence of its propeptide (MplΔpro) and of two Mpl single-site mutants with unstable propeptides: Mpl(H75V) and Mpl(H95L). We observed that all three Mpl mutants mediate PC-PLC activation when bacteria are grown on semisolid medium, but to a lesser extent than wild-type Mpl, indicating that, although not essential, the propeptide enhances the production of active Mpl. However, the mutant proteins were not functional in infected cells, as determined by monitoring PC-PLC maturation and compartmentalization. This defect could not be rescued by providing the propeptide in trans to the mplΔpro mutant. We tested the compartmentalization of Mpl during intracellular infection and observed that the mutant Mpl species were aberrantly secreted in the cytosol of infected cells. These data indicated that the propeptide of Mpl serves to maintain bacterium-associated Mpl and that this localization is essential to the function of Mpl during intracellular infection.
机译：金属蛋白酶（Mpl）是细胞内细菌病原体单核细胞增生性李斯特菌毒力的重要组成部分。 Mpl调节细菌广谱磷脂酶C（PC-PLC）的活性和分区。 Mpl以原蛋白形式分泌，该原蛋白经过分子内自催化释放其催化结构域。在相关的蛋白酶中，前肽起折叠催化剂的作用，可以以顺式或顺式起作用。前肽还可以影响蛋白质区室化和细胞内运输或降低折叠动力学。在这项研究中，我们旨在通过监测在没有前肽（MplΔpro）和两个具有不稳定前肽的Mpl单点突变体的情况下合成的Mpl的行为来确定Mpl前肽的作用：Mpl（H75V）和Mpl（H95L） ）。我们观察到，当细菌在半固体培养基上生长时，所有三个Mpl突变体都介导PC-PLC活化，但程度低于野生型Mpl，表明尽管不是必需的，但前肽可增强活性Mpl的产生。但是，通过监测PC-PLC成熟度和区室化确定，突变蛋白在受感染的细胞中不起作用。通过向 mpl Δpro突变体提供 trans 中的前肽不能挽救这一缺陷。我们在细胞内感染过程中测试了Mpl的区室化，并观察到突变的Mpl物种在感染细胞的细胞质中异常分泌。这些数据表明Mpl的前肽用于维持细菌相关的Mpl，并且该定位对于细胞内感染期间Mpl的功能是必不可少的。

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