Molecular interaction between prion protein and GFAP both in native and recombinant forms in vitro.

Abstract:

:Gliosis of glial fibrillary acidic protein (GFAP) associated astrocytes is considered to be one of the hallmarks of transmissible spongiform encephalopathies (TSEs). In the present study, remarkable GFAP-PrP(Sc) or GFAP-PrP(C) complexes were separately detected in the brain homogenates of 263 K (Scrapie)-infected or normal hamsters by co-immunoprecipitation assay. To get more exact molecular evidences for interaction between prion protein (PrP) and GFAP, various recombinant PrP or GFAP proteins were expressed using prokaryotic-expressing and in vitro translation system. Using pull down and co-immunoprecipitation assays, reliable molecular interaction between PrP and GFAP was observed, and proteinase K (PK)-digested PrP(Sc) molecules were confirmed to be able to bind the recombinant GFAP specifically as well. The region within PrP that was responsible for interaction with GFAP was narrowed to PK-resistant core of PrP (i.e. aa 91-230). The study of the association of PrP with GFAP supplies the molecular evidence for the observation of co-localization of PrP(Sc) and GFAP in the brains of TSEs and may further provide insight into a potential role of GFAP in the biological function of PrP and the pathogenesis of prion diseases.

journal_name

Med Microbiol Immunol

authors

Dong CF,Wang XF,Wang X,Shi S,Wang GR,Shan B,An R,Li XL,Zhang BY,Han J,Dong XP

doi

10.1007/s00430-007-0071-0

subject

Has Abstract

pub_date

2008-12-01 00:00:00

pages

361-8

issue

4

eissn

0300-8584

issn

1432-1831

journal_volume

197

pub_type

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