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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A Porphyromonas gingivalis haloacid dehalogenase family phosphatase interacts with human phosphoproteins and is important for invasion
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A Porphyromonas gingivalis haloacid dehalogenase family phosphatase interacts with human phosphoproteins and is important for invasion

机译：牙龈卟啉单胞菌卤酸脱卤酶家族磷酸酶与人磷酸蛋白相互作用，对入侵很重要

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摘要

Haloacid dehalogenase (HAD) family phosphatases are widespread in prokaryotes and are generally involved in metabolic processes. Porphyromonas gingivalis, an invasive periodontal pathogen, secretes the HAD family phosphoserine phosphatase SerB653 when in contact with gingival epithelial cells. Here we characterize the structure and enzymatic activity of SerB653 and show that a SerB653 allelic replacement mutant of P. gingivalis is deficient in internalization and persistence in gingival epithelial cells. In contrast, mutation of a second HAD family serine phosphatase of A gingivalis (SerB1170), or of a serine transporter, did not affect invasion. A pull-down assay identified GAPDH and heat-shock protein 90 as potential substrates for SerB653. Furthermore, exogenous phosphatase regulated microtubule dynamics in host cells. These data indicate that P. gingivalis has adapted a formerly metabolic enzyme to facilitate entry into host cells by modulating host cytoskeletal architecture. Our findings define a virulence-related role of a HAD family phosphatase and reveal an invasin of an important periodontal pathogen.
机译：卤酸脱卤酶（HAD）家族的磷酸酶广泛存在于原核生物中，通常参与代谢过程。牙龈卟啉单胞菌是一种侵入性牙周病原体，与牙龈上皮细胞接触时会分泌HAD家族的磷酸丝氨酸磷酸酶SerB653。在这里我们表征SerB653的结构和酶活性，并显示P. gingivalis的SerB653等位基因替代突变体在齿龈上皮细胞的内在化和持久性方面是不足的。相比之下，牙龈菌A（SerB1170）的第二个HAD家族丝氨酸磷酸酶或丝氨酸转运蛋白的突变不会影响侵袭。下拉测定法确定GAPDH和热激蛋白90为SerB653的潜在底物。此外，外源磷酸酶调节宿主细胞中的微管动力学。这些数据表明牙龈卟啉单胞菌已经适应了以前的代谢酶，以通过调节宿主细胞骨架结构来促进进入宿主细胞。我们的发现定义了HAD家族磷酸酶的毒力相关作用，并揭示了重要牙周病原体的浸润素。

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