Historically, the term amyloid was used strictly with reference to human neurodegenerative diseases. Nowadays, it is known that many proteins have the potential to conformational changes into β-sheet structures with tendency to form insoluble amyloid fibrils. Moreover, amyloid proteins are widespread among microorganisms. Bacteria and fungi produce functional amyloids which exhibit all characteristics of amyloid proteins, but in contrast to a numerous group of human toxic amyloids, they play important physiological functions in microorganisms. There is growing evidence that functional amyloids are important in bacterial adhesion and invasion. Furthermore, amyloids make biofilms thicker, rougher, and more resistant to drying out. The increasing interest in better understanding of the nature of these unusual microbial proteins and their role in pathogenesis are likely to contribute to the effective treatment or prevention of infectious diseases in humans.
1. Introduction. 2. Bacterial amyloids. 2.1. Curli fibers. 2.1.1. Curli biogenesis. 2.1.2. Regulation of csg operon. 2.1.3. Participation of curli in bacterial virulence. 2.1.4. Role of curli in pathogenesis. 2.2. Other bacterial amyloids. 2.3. Fungal amyloids. 3. Recapitulation
1. Wprowadzenie. 2. Amyloidy bakteryjne. 2.1. Fimbrie spiralne. 2.1.1. Synteza fimbrii spiralnych. 2.1.2. Regulacja ekspresji operonu csg. 2.1.3. Udział fimbrii spiralnych w wirulencji bakterii. 2.1.4. Rola fimbrii spiralnych w patogenezie zakażeń człowieka. 2.2. Inne amyloidy bakteryjne. 2.3. Amyloidy grzybicze. 3. Podsumowanie
