Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2010 Apr;113(1):92-104.
doi: 10.1111/j.1471-4159.2010.06575.x. Epub 2010 Jan 8.

Wild-type Shadoo Proteins Convert to Amyloid-Like Forms Under Native Conditions

Free article

Wild-type Shadoo Proteins Convert to Amyloid-Like Forms Under Native Conditions

Nathalie Daude et al. J Neurochem. .
Free article


The cellular prion protein PrP(C) refolds into a beta-sheet enriched, infectivity-associated form called PrP(Sc). Shadoo (Sho) is a newly discovered glycoprotein that is also expressed in the adult brain. Wild type (wt) mouse Sho consists of an arginine-rich region, a hydrophobic central domain of five tandem A/LAAG amino acid repeats R1-R5 with similarity to the hydrophobic domain of PrP(C), and a C-terminal domain with one N-linked carbohydrate. As some alanine-rich proteins and PrP with a shortened C-terminal domain form amyloid we investigated conformational properties of wt Sho and polymorphic variants with insertion/deletions centered on R3. Recombinant mouse and sheep Sho converted to an amyloid-like form without recourse to chemical denaturation or acidification. For wt proteins this transition was marked by increased thioflavin T binding, Congo red staining, presence of fibrillar structures by electron microscopy, formation of sodium dodecyl sulfate-resistant complexes and the generation of a C-terminal proteinase K resistant core of 5-8 kDa. Variant Sho proteins differing within the R1-R5 region exhibited most but not all of these properties. Our studies define a proteinase K -resistant signature fragment for the amyloid fold of Sho and raise the question of a physiological role for this form of the wt protein.

Similar articles

See all similar articles

Cited by 15 articles

See all "Cited by" articles

Publication types

MeSH terms

LinkOut - more resources