Hyaluronate lyase A (HylA) (HylA)

Hyaluronate lyase A (HylA) is a secreted enzyme produced by Cutibacterium acnes, a commensal bacterium that plays a central role in the development of acne vulgaris. HylA is specifically associated with the more virulent and inflammatory phylotypes of C. acnes, such as Type IA1, which are frequently isolated from severe acne lesions (Nazipi et al., 2017, PMID: 28835644). The enzyme functions by cleaving hyaluronic acid, a major component of the human dermal extracellular matrix, into low molecular weight fragments. These fragments act as pro-inflammatory signals, triggering the release of cytokines and contributing to the redness and swelling characteristic of inflammatory acne (Tyner & Sullivan, 2005, PMID: 15805501). Because HylA facilitates bacterial invasion and exacerbates host inflammation, it is considered a promising therapeutic target for localized acne treatment. Targeting HylA allows for a more selective approach compared to traditional antibiotics, potentially reducing the risk of antibiotic resistance and minimizing disruption to the broader skin microbiome.

Other names

Hyaluronidase ACutibacterium acnes hyaluronate lyasePropionibacterium acnes hyaluronidaseExtracellular hyaluronate lyase

Inhibition of the HylA enzyme prevents the degradation of high molecular weight hyaluronic acid into pro-inflammatory fragments, thereby reducing tissue damage and inflammatory signaling in the skin.