Filamentous phages reduce alpha-synuclein oligomerization in the membrane fraction of SH-SY5Y cells.

BACKGROUND

alpha-Synuclein (AS) is an abundant neuronal protein predominantly localized in presynaptic terminals in the central nervous system. AS aggregation is a molecular hallmark of several neurodegenerative diseases, including Parkinson's disease, and is thought to play a significant role in the etiology of the disease. Recent experimental evidence indicates that AS exists in two forms, a membrane-bound form and a disordered cytosolic form. Much effort is dedicated to prevent and dissolve AS aggregates, specifically AS oligomers and protofibrils, which are thought to be the more toxic form of aggregates.

METHODS

The effect of filamentous phages on AS aggregation in SH-SY5Y cells overexpressing wild-type AS was quantified in ELISA designed to detect and quantify AS oligomers.

RESULTS

We found reduced levels of AS oligomers in the membrane fraction in cells treated with filamentous phages compared to nontreated cells.

CONCLUSION

The reduction in AS oligomers from the plasma membrane in treated cells may suggest further therapeutic application.