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Updated: Jun 20, 2026

Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
Published on: December 19, 2015
Mapping the interaction site of prion protein and Sho
1Institute of Military Veterinary, Academy of Military Medical Sciences, 1068 Qinglong Road, Changchun, 130062 China.
Abstract:
The cellular prion protein (PrP(C)) is a highly conserved protein among mammals and is considered to have important cellular functions. Despite decades of intensive research, however, the physiological function of PrP(C) remains unclear. Sho (Shadoo, shadow of prion protein) and PrP(C) have similar N-terminals, which suggests that the two proteins share biological functions. Using truncation mutants of both proteins and yeast two-hybrid analysis, with validation by co-immunoprecipitation and surface plasmon resonance (SPR), we have identified an interaction between Sho 61-77 and PrP(C) 108-126 domains. This indicates that Sho may play a role in the physiological function of PrP(C) and prion pathogenesis.
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