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首页> 外文期刊>Journal of bacteriology >An Intracellular Peptidyl-Prolyl cis/trans Isomerase Is Required for Folding and Activity of the Staphylococcus aureus Secreted Virulence Factor Nuclease
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An Intracellular Peptidyl-Prolyl cis/trans Isomerase Is Required for Folding and Activity of the Staphylococcus aureus Secreted Virulence Factor Nuclease

机译：细胞内肽基脯氨酰顺/反异构酶是金黄色葡萄球菌分泌的毒力因子核酸酶的折叠和活性所必需的。

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Staphylococcus aureus is an important human pathogen that relies on a large repertoire of secreted and cell wall-associated proteins for pathogenesis. Consequently, the ability of the organism to cause disease is absolutely dependent on its ability to synthesize and successfully secrete these proteins. In this study, we investigate the role of peptidyl-prolyl cis/trans isomerases (PPIases) on the activity of the S. aureus secreted virulence factor nuclease (Nuc). We identify a staphylococcal cyclophilin-type PPIase (PpiB) that is required for optimal activity of Nuc. Disruption of ppiB results in decreased nuclease activity in culture supernatants; however, the levels of Nuc protein are not altered, suggesting that the decrease in activity results from misfolding of Nuc in the absence of PpiB. We go on to demonstrate that PpiB exhibits PPIase activity in vitro, is localized to the bacterial cytosol, and directly interacts with Nuc in vitro to accelerate the rate of Nuc refolding. Finally, we demonstrate an additional role for PpiB in S. aureus hemolysis and demonstrate that the S. aureus parvulin-type PPIase PrsA also plays a role in the activity of secreted virulence factors. The deletion of prsA leads to a decrease in secreted protease and phospholipase activity, similar to that observed in other Gram-positive pathogens. Together, these results demonstrate, for the first time to our knowledge, that PPIases play an important role in the secretion of virulence factors in S. aureus.
机译：金黄色葡萄球菌是一种重要的人类病原体，其依赖大量的与细胞壁相关的分泌蛋白来进行发病。因此，生物体引起疾病的能力完全取决于其合成和成功分泌这些蛋白质的能力。在这项研究中，我们调查了肽基脯氨酰顺式/反式异构酶（PPIases）对金黄色葡萄球菌分泌的毒力因子核酸酶（Nuc）活性的作用。我们确定了葡萄球菌亲环型PPIase（PpiB）的最佳活性的Nuc。 ppiB 的破坏导致培养上清液中核酸酶活性的降低;但是，Nuc蛋白的水平没有改变，这表明活性的降低是由于在没有PpiB的情况下Nuc的错误折叠造成的。我们继续证明，PpiB在体外表现出PPIase活性，位于细菌的细胞质中，并与Nuc在体外直接相互作用，以加快Nuc的复性速度。最后，我们证明了PpiB在金黄色葡萄球菌溶血中的其他作用，并证明了金黄色葡萄球菌小肠蛋白型PPIase PrsA在分泌的毒力因子的活性中也起作用。 prsA 的缺失导致分泌的蛋白酶和磷脂酶活性降低，这与其他革兰氏阳性病原体中观察到的相似。总之，这些结果首次证明我们知道，PPIase在金黄色葡萄球菌的毒力因子分泌中起重要作用。

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