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    Bacterial Sphingomyelinases and Phospholipases as virulence factors

    Flores-Díaz, M. and Monturiol-Gross, L. and Naylor, Claire and Alape-Girón, A. and Flieger, A. (2016) Bacterial Sphingomyelinases and Phospholipases as virulence factors. Microbiology and Molecular Biology Reviews 80 (3), pp. 597-628. ISSN 1092-2172.

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    Abstract

    SUMMARY Bacterial sphingomyelinases and phospholipases are a heterogeneous group of esterases which are usually surface associated or secreted by a wide variety of Gram-positive and Gram-negative bacteria. These enzymes hydrolyze sphingomyelin and glycerophospholipids, respectively, generating products identical to the ones produced by eukaryotic enzymes which play crucial roles in distinct physiological processes, including membrane dynamics, cellular signaling, migration, growth, and death. Several bacterial sphingomyelinases and phospholipases are essential for virulence of extracellular, facultative, or obligate intracellular pathogens, as these enzymes contribute to phagosomal escape or phagosomal maturation avoidance, favoring tissue colonization, infection establishment and progression, or immune response evasion. This work presents a classification proposal for bacterial sphingomyelinases and phospholipases that considers not only their enzymatic activities but also their structural aspects. An overview of the main physiopathological activities is provided for each enzyme type, as are examples in which inactivation of a sphingomyelinase- or a phospholipase-encoding gene impairs the virulence of a pathogen. The identification of sphingomyelinases and phospholipases important for bacterial pathogenesis and the development of inhibitors for these enzymes could generate candidate vaccines and therapeutic agents, which will diminish the impacts of the associated human and animal diseases.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 28 Jun 2016 12:14
    Last Modified: 28 Jun 2016 12:14
    URI: http://eprints.bbk.ac.uk/id/eprint/15646

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