Misregulation of the broad-range phospholipase C activity increases the susceptibility of Listeria monocytogenes to intracellular killing by neutrophils

Blank, Bryant S.; Abdallah, Delbert S. Abi; Park, Justin J.; Nazarova, Evgeniya V.; Bitar, Alan Pavinski; Maurer, Kirk J.; Marquis, Hélène

doi:10.1016/j.micinf.2013.10.014

Cited by 8 publications

(6 citation statements)

References 32 publications

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“…However, premature discharge of PC-PLC into the host cell cytosol can be lethal to L. monocytogenes; thus, the pathogen has a PC-PLC regulation mechanism for efficient pathogenicity [41]. A PC-PLC mutant exhibited low resistance against intracellular killing by neutrophils, suggesting PC-PLC may potentiate the action of neutrophils against L. monocytogenes [42]. L. monocytogenes regulates the activity of PC-PLC by increasing the pH within the double-membrane vacuole [41].…”

Section: Phospholipasesmentioning

confidence: 99%

Listeria monocytogenes Virulence, Antimicrobial Resistance and Environmental Persistence: A Review

Matereke

Okoh

2020

Pathogens

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Listeria monocytogenes is a ubiquitous opportunistic pathogen responsible for the well-known listeriosis disease. This bacterium has become a common contaminant of food, threatening the food processing industry. Once consumed, the pathogen is capable of traversing epithelial barriers, cellular invasion, and intracellular replication through the modulation of virulence factors such as internalins and haemolysins. Mobile genetic elements (plasmids and transposons) and other sophisticated mechanisms are thought to contribute to the increasing antimicrobial resistance of L. monocytogenes. The environmental persistence of the pathogen is aided by its ability to withstand environmental stresses such as acidity, cold stress, osmotic stress, and oxidative stress. This review seeks to give an insight into L. monocytogenes biology, with emphasis on its virulence factors, antimicrobial resistance, and adaptations to environmental stresses.

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Section: Phospholipasesmentioning

confidence: 99%

Listeria monocytogenes Virulence, Antimicrobial Resistance and Environmental Persistence: A Review

Matereke

Okoh

2020

Pathogens

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“…Activation of pro-LmPlcB is also mediated by an Mpl-independent pathway, utilizing host cysteine proteases [43]. Finally, LmPlcB catalytic activity is regulated by vacuolar pH, and its compartmentalization to the spreading vacuole is critical for intracellular survival in neutrophils [44].…”

Section: Substrate Specificity Comparisonmentioning

confidence: 99%

“…It has been shown that LmPlcB activation by Mpl inside vacuoles is important for its virulence because an LmPlcB pro-mutant, secreted as an already mature and active enzyme, is strongly attenuated in a mouse infection model [110]. Later, it was found that the LmPlcB pro-mutant interferes less with mitochondrial homeostasis than wild-type strain, and is more susceptible to intracellular killing by peritoneal mice neutrophils, which explains its impaired virulence [44].…”

Section: Effects On Animal Models Of Infectionmentioning

confidence: 99%

Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase

et al. 2021

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Bacterial phospholipases and sphingomyelinases are lipolytic esterases that are structurally and evolutionarily heterogeneous. These enzymes play crucial roles as virulence factors in several human and animal infectious diseases. Some bacterial phospholipases C (PLCs) have both phosphatidylcholinesterase and sphingomyelinase C activities. Among them, Listeria monocytogenes PlcB, Clostridium perfringens PLC, and Pseudomonas aeruginosa PlcH are the most deeply understood. In silico predictions of substrates docking with these three bacterial enzymes provide evidence that they interact with different substrates at the same active site. This review discusses structural aspects, substrate specificity, and the mechanism of action of those bacterial enzymes on target cells and animal infection models to shed light on their roles in pathogenesis.

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“…Both the lecithinase and the SMase C activities of this enzyme are important for bacterial spread in cultured cells (189,204). PlcB catalytic activity is regulated by vacuolar pH, and its compartmentalization to the spreading vacuole is critical for intracellular survival in neutrophils (205). Accordingly, an L. monocytogenes strain carrying a mutated plcB gene encoding an enzyme lacking control of its catalytic activity has 100-fold-attenuated virulence in mice (205,206).…”

Section: Phospholipase Csmentioning

confidence: 99%

“…PlcB catalytic activity is regulated by vacuolar pH, and its compartmentalization to the spreading vacuole is critical for intracellular survival in neutrophils (205). Accordingly, an L. monocytogenes strain carrying a mutated plcB gene encoding an enzyme lacking control of its catalytic activity has 100-fold-attenuated virulence in mice (205,206). Furthermore, an L. monocytogenes mutant strain lacking plcB has defects in phagosomal escape and cell-to-cell propagation and consequently has a 10-to 20-fold increased 50% lethal dose (LD 50 ) (187) and reduced virulence in a murine cerebral listeriosis model (207).…”

Section: Phospholipase Csmentioning

confidence: 99%

Bacterial Sphingomyelinases and Phospholipases as Virulence Factors

Flores-Dı́az

Monturiol-Gross

Naylor

et al. 2016

Microbiol Mol Biol Rev

164

143

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SUMMARYBacterial 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.

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Misregulation of the broad-range phospholipase C activity increases the susceptibility of Listeria monocytogenes to intracellular killing by neutrophils

Cited by 8 publications

References 32 publications

Listeria monocytogenes Virulence, Antimicrobial Resistance and Environmental Persistence: A Review

Listeria monocytogenes Virulence, Antimicrobial Resistance and Environmental Persistence: A Review

Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase

Bacterial Sphingomyelinases and Phospholipases as Virulence Factors

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