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

12.5K
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,...
12.5K
Subviral Agents01:29

Subviral Agents

708
Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
708

You might also read

Related Articles

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

Sort by
Same author

TAF15 amyloids propagate via defined motifs in a prion-like fashion.

Nature communications·2026
Same author

A functional amyloid scaffold shapes insect egg coats.

bioRxiv : the preprint server for biology·2026
Same author

Early onset rapidly progressive frontotemporal dementia due to a novel MAPT P301A variant with functional validation of pathogenicity.

NPJ dementia·2026
Same author

Cysteines are critical determinants of spontaneous and seeded tau aggregation in cells.

bioRxiv : the preprint server for biology·2026
Same author

A quantitative cell-based reporter links TDP-43 aggregation and dysfunction to define pathogenic mechanisms.

PLoS biology·2026
Same author

A cytokine receptor-targeting chimera toolbox for expanding extracellular targeted protein degradation.

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

Related Experiment Video

Updated: Mar 12, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

16.6K

Cellular Models for the Study of Prions.

Brandon B Holmes1,2, Marc I Diamond2

  • 1Medical Scientist Training Program, Washington University School of Medicine, St. Louis, Missouri 63110.

Cold Spring Harbor Perspectives in Medicine
|November 6, 2016
PubMed
Summary

Researchers developed cellular biosensors to study prion-like behavior of neurodegenerative disease proteins like tau. These tools quantify protein seeding and transmission, offering new insights into diseases such as Alzheimer's.

More Related Videos

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
08:12

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

6.8K
Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

20.2K

Related Experiment Videos

Last Updated: Mar 12, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

16.6K
High-throughput Screening for Protein-based Inheritance in S. cerevisiae
08:12

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

6.8K
Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

20.2K

Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Amyloid proteins like tau and alpha-synuclein, implicated in neurodegenerative diseases, exhibit prion-like characteristics.
  • Prions are known for their ability to transmit cellular pathology in vivo.

Purpose of the Study:

  • To develop and utilize cellular biosensors for studying prion activity of neurodegenerative disease proteins.
  • To gain mechanistic insights into prion transmission and neurodegenerative disease progression.

Main Methods:

  • Development of genetically engineered cellular bioassays with quantitative fluorescence detection.
  • Measurement of tau seed binding and uptake into cultured cells.
  • Quantification of prion seeding activity in brain samples.
  • Propagation of tau prion strains in cell culture models.

Main Results:

  • Demonstrated the utility of cellular biosensors in measuring key features of prion activity.
  • Successfully quantified tau seed interactions with cells and seeding activity in brain tissue.
  • Established cell models capable of indefinitely propagating tau prion strains.

Conclusions:

  • Cellular biosensors provide a powerful tool for studying the mechanisms of prion transmission.
  • These biosensors facilitate a reductionist approach to understanding complex neurodegenerative diseases.
  • The developed assays enable quantitative analysis of prion-like protein behavior in vitro and in vivo.