title: [Interaction between various 14-3-3beta segments and PrP in vitro].
abstract: OBJECTIVE To study the potential interaction between PrP protein.
  
  
  METHODS
  The supernatant of health and scrapie-infected hamsters' brain homogenate was prepared, while various recombinant 14-3-3beta or PrP proteins were purified. The possible molecular interaction between 14-3-3beta proteins and PrP was tested by pull-down and immunoprecipitation assays.
  
  
  RESULTS
  Both native PrP(c) and its protease-resistant isoform (PrP(Sc)) formed complexes with 14-3-3beta. The full-length recombinant 14-3-3beta proteins interacted with PrP. The domain responsible for interacting 14-3-3beta was located at N-terminal of 14-3-3beta (residues 1 to 38).
  
  
  CONCLUSIONS
  The studies of the association of PrP with 14-3-3beta may further provide insight into a potential role of 14-3-3beta in the biological function of PrP and the pathogenesis of prion disease.
authors.affiliation: State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China.
authors.forename: Ying-Hui
authors.initials: YH
authors.lastname: Liu
authors.forename: Yan-Ling
authors.initials: YL
authors.lastname: Han
authors.forename: Juan
authors.initials: J
authors.lastname: Song
authors.forename: Ying
authors.initials: Y
authors.lastname: Wang
authors.forename: Wei
authors.initials: W
authors.lastname: Zhou
authors.forename: Bao-Yun
authors.initials: BY
authors.lastname: Zhang
authors.forename: Chan
authors.initials: C
authors.lastname: Tian
authors.forename: Chao-Pin
authors.initials: CP
authors.lastname: Li
authors.forename: Jun
authors.initials: J
authors.lastname: Han
authors.forename: Xiao-Ping
authors.initials: XP
authors.lastname: Dong
mesh_terms: D048948:14-3-3 Proteins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D001923:Brain Chemistry; D006224:Cricetinae; D010450:Endopeptidases / Q000378:metabolism; D018620:PrPSc Proteins / Q000378:metabolism*; D017096:Prion Diseases / Q000473:pathology; D011328:Prions / Q000378:metabolism*; D012608:Scrapie / Q000503:physiopathology
chemical_list: D048948:14-3-3 Proteins; D018620:PrPSc Proteins; D011328:Prions; D010450:Endopeptidases