Open AccessBacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase
Author(s) -
MonturiolGross Laura,
VillaltaRomero Fabian,
FloresDíaz Marietta,
AlapeGirón Alberto
Publication year - 2021
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.13320
Subject(s) - listeria monocytogenes , virulence , sphingomyelin , microbiology and biotechnology , phospholipase , biology , enzyme , in silico , pseudomonas aeruginosa , clostridium perfringens , biofilm , biochemistry , bacteria , gene , genetics , membrane
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.