Effect of αB-Crystallin on Protein Aggregation in Drosophila

Disorganisation and aggregation of proteins containing expanded polyglutamine (polyQ) repeats, or ectopic expression of alpha-synuclein, underlie neurodegenerative diseases including Alzheimer's, Parkinson, Huntington, Creutzfeldt diseases. Small heatshock proteins, such as alpha B-crystallin, act as chaperones to prevent protein aggregation and play a key role in the prevention of such protein disorganisation diseases. In this study, we have explored the potential for chaperone activity of alpha B-crystallin to suppress the formation of protein aggregates. We tested the ability of aB-crystallin to suppress the aggregation of a polyQ protein and alpha-synuclein in Drosophila. We found that alpha B-crystallin suppresses both the compound eye degeneration induced by polyQ and the alpha-synuclein-induced rough eye phenotype. Furthermore, by using histochemical staining we have determined that alpha B-crystallin inhibits the aggregation of polyQ in vivo. These data provide a clue for the development of therapeutics for neurodegenerative diseases.