Unknown

Dataset Information

0

Exposure to the Functional Bacterial Amyloid Protein Curli Enhances Alpha-Synuclein Aggregation in Aged Fischer 344 Rats and Caenorhabditis elegans.


ABSTRACT: Misfolded alpha-synuclein (AS) and other neurodegenerative disorder proteins display prion-like transmission of protein aggregation. Factors responsible for the initiation of AS aggregation are unknown. To evaluate the role of amyloid proteins made by the microbiota we exposed aged rats and transgenic C. elegans to E. coli producing the extracellular bacterial amyloid protein curli. Rats exposed to curli-producing bacteria displayed increased neuronal AS deposition in both gut and brain and enhanced microgliosis and astrogliosis compared to rats exposed to either mutant bacteria unable to synthesize curli, or to vehicle alone. Animals exposed to curli producing bacteria also had more expression of TLR2, IL-6 and TNF in the brain than the other two groups. There were no differences among the rat groups in survival, body weight, inflammation in the mouth, retina, kidneys or gut epithelia, and circulating cytokine levels. AS-expressing C. elegans fed on curli-producing bacteria also had enhanced AS aggregation. These results suggest that bacterial amyloid functions as a trigger to initiate AS aggregation through cross-seeding and also primes responses of the innate immune system.

SUBMITTER: Chen SG 

PROVIDER: S-EPMC5052651 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Exposure to the Functional Bacterial Amyloid Protein Curli Enhances Alpha-Synuclein Aggregation in Aged Fischer 344 Rats and Caenorhabditis elegans.

Chen Shu G SG   Stribinskis Vilius V   Rane Madhavi J MJ   Demuth Donald R DR   Gozal Evelyne E   Roberts Andrew M AM   Jagadapillai Rekha R   Liu Ruolan R   Choe Kyonghwan K   Shivakumar Bhooma B   Son Francheska F   Jin Shunying S   Kerber Richard R   Adame Anthony A   Masliah Eliezer E   Friedland Robert P RP  

Scientific reports 20161006


Misfolded alpha-synuclein (AS) and other neurodegenerative disorder proteins display prion-like transmission of protein aggregation. Factors responsible for the initiation of AS aggregation are unknown. To evaluate the role of amyloid proteins made by the microbiota we exposed aged rats and transgenic C. elegans to E. coli producing the extracellular bacterial amyloid protein curli. Rats exposed to curli-producing bacteria displayed increased neuronal AS deposition in both gut and brain and enha  ...[more]

Similar Datasets

| S-EPMC5614702 | biostudies-literature
| S-EPMC7576226 | biostudies-literature
| S-EPMC8190196 | biostudies-literature
| S-EPMC3134098 | biostudies-literature
| S-EPMC5644351 | biostudies-literature
| S-EPMC5401774 | biostudies-literature
| PRJDB12865 | ENA
| S-EPMC7612977 | biostudies-literature
| S-EPMC6524967 | biostudies-literature
| S-EPMC7181609 | biostudies-literature