Complex Interaction between Resident Microbiota and Misfolded Proteins: Role in Neuroinflammation and Neurodegeneration

Journal
Cells
ISSN
2073-4409
Date Issued
2020
Author(s)
Juliana González-Sanmiguel
Christina M. A. P. Schuh
Carola Muñoz-Montesino
Pamina Contreras-Kallens
Luis G. Aguayo
Sebastian Aguayo
Type
Resource Types::text::journal::journal article
Scopus ID
2-s2.0-85096348070
WoS ID
WOS:000592787000001
DOI
URL
URL Institutional Repository
Abstract
<jats:p>Neurodegenerative diseases such as Alzheimer’s disease (AD), Parkinson’s disease (PD) and Creutzfeldt–Jakob disease (CJD) are brain conditions affecting millions of people worldwide. These diseases are associated with the presence of amyloid-β (Aβ), alpha synuclein (α-Syn) and prion protein (PrP) depositions in the brain, respectively, which lead to synaptic disconnection and subsequent progressive neuronal death. Although considerable progress has been made in elucidating the pathogenesis of these diseases, the specific mechanisms of their origins remain largely unknown. A body of research suggests a potential association between host microbiota, neuroinflammation and dementia, either directly due to bacterial brain invasion because of barrier leakage and production of toxins and inflammation, or indirectly by modulating the immune response. In the present review, we focus on the emerging topics of neuroinflammation and the association between components of the human microbiota and the deposition of Aβ, α-Syn and PrP in the brain. Special focus is given to gut and oral bacteria and biofilms and to the potential mechanisms associating microbiome dysbiosis and toxin production with neurodegeneration. The roles of neuroinflammation, protein misfolding and cellular mediators in membrane damage and increased permeability are also discussed.</jats:p>
Project(s)
Subjects
alzheimer’

; 

s disease

; 

parkinson’

; 

s disease

; 

creutzfeldt-jakob disease

; 

neuroinflammation

; 

microbiome

; 

periodontal diseases

; 

biofilms

; 

membrane permeability

; 

alpha-synuclein

; 

alzheimer disease

; 

amyloid beta-peptides

; 

brain

; 

humans

; 

microbiota

; 

parkinson disease

; 

alpha synuclein

; 

amyloid beta protein

; 

amyloid precursor protein

; 

brain derived neurotrophic factor

; 

farnesoid x receptor

; 

galantamine

; 

gamma interferon

; 

glial fibrillary acidic protein

; 

hydrogen sulfide

; 

inositol trisphosphate

; 

interleukin 12

; 

interleukin 13

; 

interleukin 1beta

; 

inulin

; 

occludin

; 

presenilin 1

; 

prion protein

; 

reactive oxygen metabolite

; 

short chain fatty acid

; 

sulindac

; 

tau protein

; 

toll like receptor 2

; 

toll like receptor 4

; 

transcriptome

; 

tumor necrosis factor

; 

virulence factor

; 

alpha synuclein

; 

amyloid beta protein

; 

antibiotic resistance

; 

atomic force microscopy

; 

bacterial flora

; 

bifidobacterium bifidum

; 

blood brain barrier

; 

candida albicans

; 

cell viability

; 

central nervous system

; 

chromosome 14

; 

cytokine production

; 

endoplasmic reticulum stress

; 

escherichia coli

; 

feces microflora

; 

gene expression

; 

helicobacter pylori

; 

human

; 

immune response

; 

immunological tolerance

; 

immunomodulation

; 

innate immunity

; 

intestine flora

; 

intestine innervation

; 

mass spectrometry

; 

microbial community

; 

microbial diversity

; 

mitochondrial dynamics

; 

nerve cell plasticity

; 

nerve degeneration

; 

nervous system inflammation

; 

neuroprotection

; 

nonhuman

; 

oxidative stress

; 

protein aggregation

; 

protein misfolding

; 

review

; 

risk factor

; 

signal transduction

; 

streptococcus mutans

; 

upregulation

; 

alzheimer disease

; 

brain

; 

metabolism

; 

microflora

; 

parkinson disease

; 

physiology