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Updated: May 31, 2026
09:43
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
The PrP-like proteins Shadoo and Doppel.
David Westaway1, Nathalie Daude, Serene Wohlgemuth
1Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, AB, Canada. david.westaway@ualberta.ca
Topics in Current Chemistry
|July 6, 2011
Summary
The prion protein (PrP) has a subtle role in cell biology. Related proteins, Doppel (Dpl) and Sho, may offer simpler models to understand PrP function and mammalian prion biology.
Area of Science:
- Biochemistry and Molecular Biology
- Cell Biology
- Neuroscience
Background:
- The cellular prion protein (PrP(C)) has a poorly understood, subtle role in normal cell biology, potentially representing a novel plasma membrane ecosystem.
- Existing research on PrP(C) lacks a unifying molecular framework, despite extensive study.
- The GPI-anchored, N-glycosylated proteins Doppel (Dpl) and Sho share structural similarities with PrP(C), suggesting they could serve as simpler models.
Purpose of the Study:
- To explore the potential of Doppel (Dpl) and Sho proteins as simpler models for understanding the complex biology of the cellular prion protein (PrP(C)).
- To highlight the distinct biological roles of Dpl and Sho, particularly their potential contributions to gametogenesis and central nervous system (CNS) biochemistry, respectively.
- To propose Dpl and Sho as valuable research avenues for advancing the study of mammalian prion proteins.
Main Methods:
- Comparative analysis of PrP(C), Doppel (Dpl), and Sho protein structures and functions.
- Review of existing literature on the biochemistry and cellular roles of these proteins.
- Identification of parallels and divergences in their molecular characteristics and biological activities.
Main Results:
- Doppel (Dpl) protein exhibits a significant role in successful gametogenesis.
- Sho protein, a recently discovered CNS-expressed protein, shows numerous parallels with established aspects of PrP biochemistry.
- Dpl and Sho proteins can be viewed as structurally and functionally related entities to PrP(C), offering alternative research targets.
Conclusions:
- Doppel (Dpl) and Sho proteins represent promising, potentially simpler systems for investigating the broader biology of mammalian prion proteins.
- Further research into Dpl and Sho could provide fresh insights and help unify current understanding of PrP(C) function.
- These related proteins offer distinct avenues for exploring prion protein biochemistry and cellular roles, expanding the research landscape.
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