We used a bovine brain cDNA library to perform a yeast two-hybrid assay with bovine mature PrPC as bait. The screening result showed that αB-crystalline interacted with PrPC. The interaction was further evaluated both in vivo and in vitro with different methods, such as immunofluorescent colocalization, native polyacrylamide-gel electrophoresis, and IAsys biosensor assays. The results suggested that αB-crystalline may have the ability to refold denatured prion proteins, and provided first evidence that αB-crystalline is directly associated with prion protein. © 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Sun, G., Guo, M., Shen, A., Mei, F., Peng, X., Gong, R., … Xiao, G. (2005). Bovine PrPC directly interacts with αB-crystalline. FEBS Letters, 579(24), 5419–5424. https://doi.org/10.1016/j.febslet.2005.08.065