TY - JOUR

T1 - Bacterial Biofilms as a Reservoir of Amyloids Formed through Specific and Nonspecific Mechanisms

AU - Нижников, Антон Александрович

PY - 2025/11/30

Y1 - 2025/11/30

N2 - Abstract: Amyloids are protein aggregates with fibrillar morphology and a characteristic spatial structure called “cross-β.” Amyloids have been known for over 150 years, and many of them are associated with the development of predominantly incurable human diseases called amyloidoses, some of which, including Alzheimer’s disease, are of high social significance. At the turn of the 21st century, it was established that amyloids not only result from protein misfolding disorders but are involved in performing biological functions in all three domains of the living world: archaea, bacteria, and eukaryotes, including humans. The greatest diversity of functional amyloids has been described in bacteria in which these protein aggregates are involved mainly in the processes of formation of biofilms that play an important role in the development of bacterial infections and antibiotic resistance. Amyloid fibrils represent an important structural component of the biofilm matrix in various groups of bacteria. Although some bacterial amyloids are formed by specific secretion and assembly systems, the mechanisms of formation of another group of bacterial amyloids, including amyloid states of outer membrane proteins and components of the translation apparatus, are unclear. Current evidence suggests that more general, “nonspecific” mechanisms, including regulated cell death during biofilm development, may be involved in the formation of such amyloids.

AB - Abstract: Amyloids are protein aggregates with fibrillar morphology and a characteristic spatial structure called “cross-β.” Amyloids have been known for over 150 years, and many of them are associated with the development of predominantly incurable human diseases called amyloidoses, some of which, including Alzheimer’s disease, are of high social significance. At the turn of the 21st century, it was established that amyloids not only result from protein misfolding disorders but are involved in performing biological functions in all three domains of the living world: archaea, bacteria, and eukaryotes, including humans. The greatest diversity of functional amyloids has been described in bacteria in which these protein aggregates are involved mainly in the processes of formation of biofilms that play an important role in the development of bacterial infections and antibiotic resistance. Amyloid fibrils represent an important structural component of the biofilm matrix in various groups of bacteria. Although some bacterial amyloids are formed by specific secretion and assembly systems, the mechanisms of formation of another group of bacterial amyloids, including amyloid states of outer membrane proteins and components of the translation apparatus, are unclear. Current evidence suggests that more general, “nonspecific” mechanisms, including regulated cell death during biofilm development, may be involved in the formation of such amyloids.

KW - amyloid

KW - bacteria

KW - biofilm

KW - fibril

KW - infection

KW - pathogenesis

KW - proteome

UR - https://www.mendeley.com/catalogue/fcc01c36-93c4-3a62-acc1-c253bdb59425/

U2 - 10.1134/s1022795425701078

DO - 10.1134/s1022795425701078

M3 - Review article

VL - 61

SP - 1514

EP - 1522

JO - Russian Journal of Genetics

JF - Russian Journal of Genetics

SN - 1022-7954

IS - 11

ER -