New Publication

Structural and functional overview of Als5p and its role in amyloid-mediated adhesion and biofilm formation. Gruber, D. et al. Virulence, 2025, 16, 1, 2597576.

Candida species are major causes of hospital-acquired infections, largely because they form biofilms that help them persist and resist antifungal treatment. A key step in biofilm formation is how fungal cells stick together, which involves surface proteins like Als5p in Candida albicans. A short amyloid-forming peptide within Als5p (Als5pFP) is known to support adhesion, but its impact on biofilm structure has been unclear. In our study by Daniel Gruber, Jan-Christoph Walter, Grigory Bolotnikov, Benedikt Miegel, Elisabeth Bierla, Andreas Bellmann, Christina Sandra Einsiedler, Amelie Therese Eiblmayr, Mauritz Maser, Denise Obert, Elisa Lin Men Qi Sun, Jonas Schnaubelt, Seda Söylemezgiller, Bianca Andrea Widy, Barbara Spellerberg, Steffen Stenger, Armando Rodríguez-Alfonso, Nico Preising, Ludger Ständker, Carolina Firacative, Ann- Kathrin Kissmann, and Frank Rosenau as an example of “citizen science”, we found that adding Als5pFP increased biofilm biomass under laboratory conditions, including in complex media and at clinically relevant temperatures. Image analysis revealed that the peptide also changes the biofilm’s architecture: it creates sharper-edged microcolonies by clustering cells into tighter groups and reducing cells in the spaces between them. This suggests that amyloid-like fibrils formed by the peptide influence how C. albicans biofilms are spatially organized. These results add a new perspective on how amyloid structures shape biofilm architecture and may inform future efforts to develop antifungal strategies or biosensors that target or detect amyloid formation.

Link to the publication: Full article: Amyloid fibrils of the Als5p-derived peptide NH2-SNGIVIVATTRTV-COOH influence the biofilm formation of Candida albicans by shape-edging microcolony morphology