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Bovine PrP C directly interacts with αB‐crystalline
Author(s) -
Sun Guihong,
Guo Mingxiong,
Shen Ao,
Mei Fanghua,
Peng Xiaoxue,
Gong Rui,
Guo Deyin,
Wu Jianguo,
Tien Po,
Xiao Gengfu
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.08.065
Subject(s) - colocalization , cdna library , gel electrophoresis , complementary dna , in vitro , yeast , chemistry , polyacrylamide gel electrophoresis , microbiology and biotechnology , recombinant dna , biochemistry , biology , enzyme , gene
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 αB‐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 αB‐crystalline may have the ability to refold denatured prion proteins, and provided first evidence that αB‐crystalline is directly associated with prion protein.