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Patatin-like phospholipases in microbial infections with emerging roles in fatty acid metabolism and immune regulation by Apicomplexa.
- Source :
-
Molecular microbiology [Mol Microbiol] 2018 Jan; Vol. 107 (1), pp. 34-46. Date of Electronic Publication: 2017 Nov 23. - Publication Year :
- 2018
-
Abstract
- Emerging lipidomic technologies have enabled researchers to dissect the complex roles of phospholipases in lipid metabolism, cellular signaling and immune regulation. Host phospholipase products are involved in stimulating and resolving the inflammatory response to pathogens. While many pathogen-derived phospholipases also manipulate the immune response, they have recently been shown to be involved in lipid remodeling and scavenging during replication. Animal and plant hosts as well as many pathogens contain a family of patatin-like phospholipases, which have been shown to have phospholipase A <subscript>2</subscript> activity. Proteins containing patatin-like phospholipase domains have been identified in protozoan parasites within the Apicomplexa phylum. These parasites are the causative agents of some of the most widespread human diseases. Malaria, caused by Plasmodium spp., kills nearly half a million people worldwide each year. Toxoplasma and Cryptosporidium infect millions of people each year with lethal consequences in immunocompromised populations. Parasite-derived patatin-like phospholipases are likely effective drug targets and progress in the tools available to the Apicomplexan field will allow for a closer look at the interplay of lipid metabolism and immune regulation during host infection.<br /> (© 2017 John Wiley & Sons Ltd.)
- Subjects :
- Amino Acid Sequence
Animals
Antigens, Human Platelet immunology
Antigens, Human Platelet metabolism
Apicomplexa immunology
Apicomplexa metabolism
Fatty Acids metabolism
Humans
Inflammation metabolism
Lipase metabolism
Lipids
Parasites metabolism
Parasites parasitology
Phospholipases immunology
Lipid Metabolism physiology
Phospholipases metabolism
Phospholipases physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1365-2958
- Volume :
- 107
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Molecular microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 29090840
- Full Text :
- https://doi.org/10.1111/mmi.13871