Sialidase (Cutibacterium acnes) (NanA)

Sialidase, also known as neuraminidase, is an extracellular enzyme produced by Cutibacterium acnes (formerly Propionibacterium acnes), a bacterium central to the development of acne vulgaris (Nakatsuji et al., 2008, J Invest Dermatol). The enzyme functions as a glycosyl hydrolase that cleaves terminal sialic acid residues from host cell surface glycoconjugates, providing a carbon source for the bacteria and facilitating tissue invasion (UniProt, Q6A7Z4). Beyond its metabolic role, sialidase acts as a potent pro-inflammatory factor, triggering the release of cytokines like IL-8 and TNF-alpha from human sebocytes and keratinocytes, which exacerbates the inflammatory lesions seen in acne (PubMed, PMID: 18273044). It also plays a role in bacterial adhesion and the formation of biofilms, which contribute to the persistence of the infection within the pilosebaceous unit. As a therapeutic target, sialidase is being investigated for the development of vaccines and topical inhibitors, such as 2-deoxy-2,3-dehydro-N-acetylneuraminic acid (DANA), which aim to neutralize its virulence without the selective pressure of traditional antibiotics (Nakatsuji et al., 2011). Targeting this enzyme offers a strategy to mitigate inflammation and bacterial colonization while potentially preserving the broader skin microbiome.

Other names

NeuraminidaseExo-alpha-sialidasePropionibacterium acnes sialidaseAcnes sialidase

Inhibition of the enzymatic activity of sialidase to prevent the cleavage of sialic acid from host cell surfaces, thereby reducing pro-inflammatory signaling and bacterial nutrient acquisition (Nakatsuji et al., 2008).