The study shows that a natural immune peptide called LL‑37, which is part of neutrophil traps, sticks to the surface of the fungus Candida albicans. When the fungus grabs LL‑37 and other trap proteins, it actually becomes better at damaging human cells, suggesting the fungus can hijack these immune molecules.

One of defense mechanisms of the human immune system to counteract infection by the opportunistic fungal pathogen <i>Candida albicans</i> is the recruitment of neutrophils to the site of invasion, and the subsequent production of neutrophil extracellular traps (NETs) that efficiently capture and kill the invader cells. In the current study, we demonstrate that within these structures composed of chromatin and proteins, the latter play a pivotal role in the entrapment of the fungal pathogen. The proteinous components of NETs, such as the granular enzymes elastase, myeloperoxidase and lactotransferrin, as well as histones and cathelicidin-derived peptide LL-37, are involved in contact with the surface of <i>C. albicans</i> cells. The fungal partners in these interactions are a typical adhesin of the agglutinin-like sequence protein family Als3, and several atypical surface-exposed proteins of cytoplasmic origin, including enolase, triosephosphate isomerase and phosphoglycerate mutase. Importantly, the adhesion of both the elastase itself and the mixture of proteins originating from NETs on the <i>C. albicans</i> cell surface considerably increased the pathogen potency of human epithelial cell destruction compared with fungal cells without human proteins attached. Such an implementation of adsorbed NET-derived proteins by invading <i>C. albicans</i> cells might alter the effectiveness of the fungal pathogen entrapment and affect the further host colonization.