Crosstalk Between Alpha-Synuclein and Other Human and Non-Human Amyloidogenic Proteins: Consequences for Amyloid Formation in Parkinson's Disease.

Journal of Parkinson's Disease
Tony WernerPernilla Wittung-Stafshede

Abstract

It was recently shown (Sampson et al., Elife9, 2020) that an amyloidogenic protein, CsgA, present in E. coli biofilms in the gut can trigger Parkinson's disease in mice. This study emphasizes the possible role of the gut microbiome in modulation (and even initiation) of human neurodegenerative disorders, such as Parkinson's disease. As the CsgA protein was found to accelerate alpha-synuclein (the key amyloidogenic protein in Parkinson's disease) amyloid formation in vitro, this result suggests that also other amyloidogenic proteins from gut bacteria, and even from the diet (such as stable allergenic proteins), may be able to affect human protein conformations and thereby modulate amyloid-related diseases. In this review, we summarize what has been reported in terms of in vitro cross-reactivity studies between alpha-synuclein and other amyloidogenic human and non-human proteins. It becomes clear from the limited data that exist that there is a fine line between acceleration and inhibition, but that cross-reactivity is widespread, and it is more common for other proteins (among the studied cases) to accelerate alpha-synuclein amyloid formation than to block it. It is of high importance to expand investigations of cross-reactivity...Continue Reading

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Citations

Oct 16, 2020·Clinical Pharmacology and Therapeutics·Piet H van der Graaf
May 23, 2021·Movement Disorders : Official Journal of the Movement Disorder Society·Dexter N Dean, Jennifer C Lee

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Methods Mentioned

BETA
AFM
gel filtration
circular dichroism
electron
atomic force microscopy
NMR
surface plasmon resonance
confocal microscopy

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