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.