Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

13.1K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
13.1K
The Unfolded Protein Response01:37

The Unfolded Protein Response

7.1K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
7.1K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

18.5K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
18.5K
Protein Folding01:25

Protein Folding

12.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.7K
Protein Folding01:22

Protein Folding

131.3K
Overview
131.3K
Protein Folding01:22

Protein Folding

36.7K
36.7K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Functional minigenome system reveals polymerase features of swine orthopneumovirus.

Journal of virology·2026
Same author

In vitro liquid-liquid phase separation induced by respiratory syncytial virus proteins and RNA.

Science advances·2026
Same author

Exploring PrP<sup>C</sup> unfolding as a critical step preceding its refolding in the context of PrP<sup>Sc</sup> propagation.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

A model-based prion vaccine protects a transgenic mouse line carrying a Gerstmann-Sträussler-Scheinker disease mutation.

Acta neuropathologica·2026
Same author

Can plitidepsin be used as an antiviral against RSV?

mSphere·2025
Same author

Expression of progerin enhances disease-related endpoints in a tau seeding reporter cell system.

GeroScience·2025

Related Experiment Video

Updated: Apr 15, 2026

Purification and Refolding to Amyloid Fibrils of His6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
09:43

Purification and Refolding to Amyloid Fibrils of His6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

Published on: December 19, 2015

14.9K

Interaction between Shadoo and PrP Affects the PrP-Folding Pathway.

Danica Ciric1, Charles-Adrien Richard1, Mohammed Moudjou1

  • 1National Institute for Agricultural Research (INRA), Pathological Macro-Assemblies and Prion Pathology Group (MAP), UR892, Virologie Immunologie Moléculaires, Jouy-en-Josas, France.

Journal of Virology
|April 10, 2015
PubMed
Summary

Shadoo (Sho) protein interacts with prion protein (PrP) and enhances prion replication. This interaction suggests Sho acts as a cofactor, influencing prion disease pathways by modifying PrP folding.

More Related Videos

Purification of Hsp104, a Protein Disaggregase
07:17

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

17.9K
Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain
11:29

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Published on: October 3, 2012

11.3K

Related Experiment Videos

Last Updated: Apr 15, 2026

Purification and Refolding to Amyloid Fibrils of His6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
09:43

Purification and Refolding to Amyloid Fibrils of His6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

Published on: December 19, 2015

14.9K
Purification of Hsp104, a Protein Disaggregase
07:17

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

17.9K
Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain
11:29

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Published on: October 3, 2012

11.3K

Area of Science:

  • Neuroscience
  • Biochemistry

Background:

  • Prion diseases involve misfolding of cellular prion protein (PrP(C)) into infectious PrP(Sc) conformers.
  • Shadoo (Sho), a prion protein family member, is expressed in the central nervous system and shares similarities with PrP.
  • Previous studies suggested a functional relationship and direct interaction between Sho and PrP.

Purpose of the Study:

  • To investigate the role of Shadoo (Sho) in prion protein (PrP) structural dynamics and prion conversion.
  • To biochemically characterize the interaction between Sho and PrP and its effect on prion replication.

Main Methods:

  • Biochemical and biophysical assays to study Sho-PrP complex formation and binding kinetics.
  • Two-hybrid analysis to confirm direct interaction.
  • Cell-based prion titration assays to quantify PrP(Sc) conversion rates.

Main Results:

  • Sho forms a 1:1 complex with full-length PrP, modifying its folding pathway.
  • Sho exhibits allosteric binding behavior with a truncated PrP fragment, suggesting tetramerization.
  • Increased PrP(Sc) conversion rates were observed in the presence of Sho, indicating Sho acts as a holdase and interferes with inhibitory fragments.

Conclusions:

  • Shadoo (Sho) directly interacts with PrP and influences its structural dynamics.
  • Sho enhances prion replication by acting as a holdase and modulating the inhibitory effect of PrP C1 fragment.
  • These findings identify Sho as a potential cofactor in prion conversion and disease pathogenesis.