Curli {90000130}

Shared Reference Notes

• [1.1] [#Parkinson’s Disease] [#Escherichia coli] 
  - E. coli genes promote neurodegeneration. - Two of these genes, csgA and csgB, code for proteins that form curli, one type of bacterial amyloid fibers. - Curli cross-seeds and colocalizes with α-syn both in C. elegans neurons and human neuroblastoma cells. - Curli-induced α-syn aggregations down-regulate mitochondrial genes, causing energy failure in neurons. - Curli may have general effects in promoting neuropathologies induced by different aggregation-prone proteins, such as A-β in #Alzheimer’s disease, Huntingtin in #Huntington’s Disease, and SOD1 in #Amyotrophic lateral sclerosis.
• [1.2] 
  - Curli fibers are produced by Enterobacteriaceae, Bacteroidetes, Proteobacteria, Firmicutes and Theromosulfobacteria. - Curli fibers are involved in cytokine production such as type I interferons, activate the Toll-like receptors TLR1 and TLR2 and the intracellular NLR family Pyrin Domain Containing 3 (NLRP3) inflammasome resulting in inflammation. - #Amyloid-producing bacteria have been described in systemic lupus erythematosus, reactive arthritis, neurodegenerative diseases, colorectal cancers and other diseases, and progress in understanding their contribution to disease pathogenesis will hopefully bring about potential therapies
• [1.3] [#Autism] [#Alpha-synuclein, #Amyloid, #Beta-glucan] [#Nichi Glucan] 
• [1.4] [#Parkinson’s Disease] 
  - curli, an amyloidogenic protein produced by Gram-negative Escherichia coli, induces #Alpha-synuclein aggregation and accelerates disease in the gut and neurodegeneration in the brain. - Many Enterobacteriaceae species encode curli.
• [1.5] [#Parkinson’s Disease] [#Escherichia coli] [#Alpha-synuclein] 
  - #Desulfovibrio strains, particularly those from PD patients, were more competent than curli-producing E. coli in stimulating the accumulation of larger and more abundant alpha-syn aggregates.
• [1.6] 
  - colonization of curli-producing #Escherichia coli accelerates aSyn pathology in the gut and brain. - #Escherichia coli needs Curli expression to exacerbate α-Syn-induced intestinal and motor disorders
• - #Epigallocatechin gallate, a plant-derived dietary polypheno can prevent pathology and motor symptoms in Thy1-SNCA mice by blocking amyloidogenic subunit of curli fibers (CsgA) amyloidogenesis and repressing CsgA transcript expression in #Escherichia coli
• [1.7] [#Fiber-free diet, #Low fibre Diet] 
  - the lowest levels of tight junction proteins #ZO-1 and #Occludin in TG mice challenged by fiber deprivation and curli.
• - Curli is a bacterial protein produced by #Enterobacteriaceae.
• [#Parkinson’s Disease] [#Alpha-synuclein] - Either gavaged or supplemented in a human fecal microbiota transplant, curli promotes PD pathologies, such as αSyn aggregation, in gut and brain.
• [#Parkinson’s Disease] - Enhanced curli exposure in PD could be the result of its secretion by #Enterobacteriaceae for biofilm formation covering the intestinal mucosa.
• [1.8] [#Vitamin B12] 
  - Unlike curli, B12 does not affect α-syn aggregation (Figure S1) and modulates neurodegeneration downstream of α-syn by inducing the breakdown of #Propionate, which is a key activator of metabolic genes involved in fatty acid and amino acid metabolism and energy production. - Removing B12 or supplementing #Propionate in the diet could metabolically rescue neurodegeneration without reversing α-syn aggregation, indicating the possibility of treating neurodegenerative diseases by simply changing the level of certain metabolites.
• [#Parkinson’s Disease] [#Escherichia coli] [#Alpha-synuclein] - Among the 38 proneurodegenerative E. coli genes identified in the #Genome-wide screen, we previously characterized the genes responsible for producing the bacterial #Amyloid fibril curli, which could enter the host neurons to cross-seed the aggregation of α-syn and promote neurodegeneration.

References Notes