Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase
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 phosphatidylcholinest...
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oai:doaj.org-article:2ccf224eaaff4bc987167fe69d1b37dc2021-12-01T13:36:12ZBacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase2211-546310.1002/2211-5463.13320https://doaj.org/article/2ccf224eaaff4bc987167fe69d1b37dc2021-12-01T00:00:00Zhttps://doi.org/10.1002/2211-5463.13320https://doaj.org/toc/2211-5463Bacterial 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.Laura Monturiol‐GrossFabian Villalta‐RomeroMarietta Flores‐DíazAlberto Alape‐GirónWileyarticlebacterial pathogenesisbacterial phospholipasesbacterial sphingomyelinasesbacterial toxinsvirulence factorsBiology (General)QH301-705.5ENFEBS Open Bio, Vol 11, Iss 12, Pp 3262-3275 (2021) |
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bacterial pathogenesis bacterial phospholipases bacterial sphingomyelinases bacterial toxins virulence factors Biology (General) QH301-705.5 |
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bacterial pathogenesis bacterial phospholipases bacterial sphingomyelinases bacterial toxins virulence factors Biology (General) QH301-705.5 Laura Monturiol‐Gross Fabian Villalta‐Romero Marietta Flores‐Díaz Alberto Alape‐Girón Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase |
description |
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. |
format |
article |
author |
Laura Monturiol‐Gross Fabian Villalta‐Romero Marietta Flores‐Díaz Alberto Alape‐Girón |
author_facet |
Laura Monturiol‐Gross Fabian Villalta‐Romero Marietta Flores‐Díaz Alberto Alape‐Girón |
author_sort |
Laura Monturiol‐Gross |
title |
Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase |
title_short |
Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase |
title_full |
Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase |
title_fullStr |
Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase |
title_full_unstemmed |
Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase |
title_sort |
bacterial phospholipases c with dual activity: phosphatidylcholinesterase and sphingomyelinase |
publisher |
Wiley |
publishDate |
2021 |
url |
https://doaj.org/article/2ccf224eaaff4bc987167fe69d1b37dc |
work_keys_str_mv |
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_version_ |
1718405109042380800 |