Resilience and Charge-Dependent Fibrillation of Functional Amyloids: Interactions ofPseudomonasBiofilm-Associated FapB and FapC

Abstract

AbstractFapC and FapB are biofilm-associated amyloids involved in the virulence ofPseudomonasand other bacteria. We herein demonstrate their exceptional thermal and chemical resilience, suggesting that biofilm structures might withstand standard sterilization, thereby contributing to the persistence ofP. aeruginosainfections. Our findings also underscore the impact of environmental factors on Fap proteins, suggesting that orthologs in differentPseudomonasstrains adapt to specific environments and roles. Challenging previous assumptions about a simple nucleation role for FapB in promoting FapC aggregation, the study shows a significant influence of FapC on FapB aggregation. The interaction between FapB and FapC is intricate: FapB stabilizes FapC fibrils, while FapC slows down FapB fibrillation but can still serve as a cross-seeding template. This complex interplay is key to understanding their roles in bacterial biofilms. Furthermore, the study highlights distinct differences between Fap andE. coli’s curli CsgA amyloid, where CsgB assumes a simple unidirectional role in nucleating CsgA fibrillation, emphasizing the importance of a comprehensive understanding of various amyloid systems. This knowledge is vital for developing effective intervention strategies against bacterial infections and leveraging the unique properties of these amyloids in technological applications such as novel bio-nanomaterials or protective coatings.