Disulfide loop cleavage of Legionella pneumophila PlaA boosts lysophospholipase A activity

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Disulfide bond oxidoreductase DsbA2 of Legionella pneumophila exhibits protein disulfide isomerase activity.

The extracytoplasmic assembly of the Dot/Icm type IVb secretion system (T4SS) of Legionella pneumophila is dependent on correct disulfide bond (DSB) formation catalyzed by a novel and essential disulfide bond oxidoreductase DsbA2 and not by DsbA1, a second nonessential DSB oxidoreductase. DsbA2, which is widely distributed in the microbial world, is phylogenetically distinct from the canonical ...

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Characterization of the gene encoding the major secreted lysophospholipase A of Legionella pneumophila and its role in detoxification of lysophosphatidylcholine.

We previously showed that Legionella pneumophila secretes, via its type II secretion system, phospholipase A activities that are distinguished by their specificity for certain phospholipids. In this study, we identified and characterized plaA, a gene encoding a phospholipase A that cleaves fatty acids from lysophospholipids. The plaA gene encoded a 309-amino-acid protein (PlaA) which had homolo...

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Investigation of Legionella Pneumophila bacteria in hospital water supply systems

Introduction: Legionella Pneumophila bacteria is known as one of the most important nosocomial infections and the most common cause of death in patients. This study was aimed to identify Legionella Pneumophila bacteria in hospital water supply systems. Material and Methods: This descriptive cross-sectional study was performed to identify Legionella pneumophila in hot and cold-water systems of i...

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ژورنال

عنوان ژورنال: Scientific Reports

سال: 2017

ISSN: 2045-2322

DOI: 10.1038/s41598-017-12796-4