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 non-treated cells. Conclusion: The reduction in AS oligomers from the plasma membrane in treated cells may suggest further therapeutic application. Copyright (C) 2010 S. Karger AG, Basel