[Interaction between various PrP segments and GFAP in vitro].
OBJECTIVE
To study the potential interaction between PrP protein and glial fibrillary acidic protein (GFAP) and identify the binding region within PrP with GFAP.


METHODS
The supernatant of healthy and scrapie-infected hamsters' brain homogenate was prepared, while various recombinant PrP or GFAP proteins were expressed using prokaryotic-expressing or in-vitro translation system. The possible molecular interaction between PrP proteins and GFAP was tested by Pull-down and immunoprecipitation assays.


RESULTS
Both native PrP(C) and its protease-resistant isoform (PrP(Sc)) formed complexes with the native GFAP. The full-length recombinant PrP proteins interacted with GFAP. The domain responsible for interacting GFAP was located at C-terminal of PrP (residues 91 to 231).


CONCLUSIONS
The studies of the association of PrP with GFAP may further provide insight into a potential role of GFAP in the biological function of PrP and the pathogenesis of prion disease.
Dong
Chen-Fang
CF
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, China.
Shan
Bing
B
Wang
Xiao-Fan
XF
Han
Jun
J
Dong
Xiao-Ping
XP
D000818:Animals; D001921:Brain / Q000378:metabolism; D006224:Cricetinae; D017353:Gene Deletion; D005904:Glial Fibrillary Acidic Protein / Q000235:genetics / Q000378:metabolism*; D047468:Immunoprecipitation; D051379:Mice; D011328:Prions / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism
D005904:Glial Fibrillary Acidic Protein; D011328:Prions; D011994:Recombinant Proteins