Cutibacterium acnes triacylglycerol lipase (GehA)

Cutibacterium acnes triacylglycerol lipase, primarily known as GehA, is a secreted enzyme produced by the anaerobic bacterium Cutibacterium acnes (formerly Propionibacterium acnes), which resides in the human pilosebaceous unit [UniProt: Q6A6N0]. The enzyme's primary biological function is the hydrolysis of triacylglycerols (triglycerides) present in human sebum into glycerol and free fatty acids (FFAs) [PubMed: 15273314]. These released FFAs are highly comedogenic and pro-inflammatory, leading to the irritation of the follicular wall and the recruitment of immune cells, which are hallmark features of acne vulgaris [PubMed: 25431130]. Consequently, this lipase is a critical virulence factor that facilitates the transition of C. acnes from a commensal to a pathogenic state. While most current acne therapies, such as tetracyclines and clindamycin, target the lipase indirectly by reducing the bacterial population and inhibiting protein synthesis, the enzyme itself remains a focus for the development of novel, non-antibiotic topical inhibitors [PubMed: 10898830, PubMed: 30235844]. Targeting this lipase offers a strategy to mitigate inflammation without the broad-spectrum effects of systemic antibiotics.

Other names

Propionibacterium acnes lipaseGlycerol-ester hydrolase AGehATriacylglycerol lipaseC. acnes lipase

Antibiotics inhibit the synthesis and secretion of the lipase by targeting bacterial ribosomes, while other agents reduce the overall population of lipase-producing bacteria.