Bovine PrPC directly interacts with alphaB-crystalline

FEBS Lett. 2005 Oct 10;579(24):5419-24. doi: 10.1016/j.febslet.2005.08.065.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Crystallins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Fluorescent Antibody Technique
  • PrPC Proteins / metabolism*
  • Protein Binding
  • Protein Folding
  • Two-Hybrid System Techniques

Substances

  • Crystallins
  • PrPC Proteins