Bovine PrPC directly interacts with alphaB-crystalline.
We used a bovine brain cDNA library to perform a yeast two-hybrid assay with bovine mature PrP(C) as bait. The screening result showed that alphaB-crystalline interacted with PrP(C). 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 alphaB-crystalline may have the ability to refold denatured prion proteins, and provided first evidence that alphaB-crystalline is directly associated with prion protein.
Sun
Guihong
G
The Modern Virology Research Centre and State Key Laboratory of Virology, College of Life Sciences, Wuhan University, PR China.
Guo
Mingxiong
M
Shen
Ao
A
Mei
Fanghua
F
Peng
Xiaoxue
X
Gong
Rui
R
Guo
Deyin
D
Wu
Jianguo
J
Tien
Po
P
Xiao
Gengfu
G
D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005455:Fluorescent Antibody Technique; D018621:PrPC Proteins / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding; D020798:Two-Hybrid System Techniques
D003459:Crystallins; D018621:PrPC Proteins