TY - JOUR

T1 - Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions

AU - Kosolapova, Anastasiia O.

AU - Antonets, Kirill S.

AU - Belousov, Mikhail V.

AU - Nizhnikov, Anton A.

N1 - Publisher Copyright: © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2020/10/1

Y1 - 2020/10/1

N2 - Amyloids are fibrillar protein aggregates with an ordered spatial structure called “cross-β”. While some amyloids are associated with development of approximately 50 incurable diseases of humans and animals, the others perform various crucial physiological functions. The greatest diversity of amyloids functions is identified within prokaryotic species where they, being the components of the biofilm matrix, function as adhesins, regulate the activity of toxins and virulence factors, and compose extracellular protein layers. Amyloid state is widely used by different pathogenic bacterial species in their interactions with eukaryotic organisms. These amyloids, being functional for bacteria that produce them, are associated with various bacterial infections in humans and animals. Thus, the repertoire of the disease-associated amyloids includes not only dozens of pathological amyloids of mammalian origin but also numerous microbial amyloids. Although the ability of symbiotic microorganisms to produce amyloids has recently been demonstrated, functional roles of prokaryotic amyloids in host–symbiont interactions as well as in the interspecies interactions within the prokaryotic communities remain poorly studied. Here, we summarize the current findings in the field of prokaryotic amyloids, classify different interspecies interactions where these amyloids are involved, and hypothesize about their real occurrence in nature as well as their roles in pathogenesis and symbiosis.

AB - Amyloids are fibrillar protein aggregates with an ordered spatial structure called “cross-β”. While some amyloids are associated with development of approximately 50 incurable diseases of humans and animals, the others perform various crucial physiological functions. The greatest diversity of amyloids functions is identified within prokaryotic species where they, being the components of the biofilm matrix, function as adhesins, regulate the activity of toxins and virulence factors, and compose extracellular protein layers. Amyloid state is widely used by different pathogenic bacterial species in their interactions with eukaryotic organisms. These amyloids, being functional for bacteria that produce them, are associated with various bacterial infections in humans and animals. Thus, the repertoire of the disease-associated amyloids includes not only dozens of pathological amyloids of mammalian origin but also numerous microbial amyloids. Although the ability of symbiotic microorganisms to produce amyloids has recently been demonstrated, functional roles of prokaryotic amyloids in host–symbiont interactions as well as in the interspecies interactions within the prokaryotic communities remain poorly studied. Here, we summarize the current findings in the field of prokaryotic amyloids, classify different interspecies interactions where these amyloids are involved, and hypothesize about their real occurrence in nature as well as their roles in pathogenesis and symbiosis.

KW - amyloid

KW - Bacteria

KW - interspecies interactions

KW - host–pathogen

KW - host–symbiont

KW - microbial community

KW - Outer membrane protein

KW - biofilm

KW - Omp

KW - Toxin

KW - Host–pathogen

KW - Biofilm

KW - Amyloid

KW - Host–symbiont

KW - Microbial community

KW - Interspecies interactions

KW - STREPTOCOCCUS-MUTANS

KW - bacteria

KW - ESCHERICHIA-COLI

KW - outer membrane protein

KW - THIN AGGREGATIVE FIMBRIAE

KW - EPIDERMIDIS BIOFILM FORMATION

KW - toxin

KW - PSEUDOMONAS-AERUGINOSA

KW - STAPHYLOCOCCUS-AUREUS

KW - OUTER-MEMBRANE

KW - host&#8211

KW - RHIZOBIUM-LEGUMINOSARUM

KW - SURFACE-PROTEINS

KW - symbiont

KW - pathogen

KW - ACCUMULATION-ASSOCIATED PROTEIN

UR - http://www.scopus.com/inward/record.url?scp=85091989592&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/e7ef564d-903a-3598-bada-f098c2cf8349/

U2 - 10.3390/ijms21197240

DO - 10.3390/ijms21197240

M3 - Review article

C2 - 33008049

VL - 21

SP - 1

EP - 26

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1422-0067

IS - 19

M1 - 7240

ER -