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

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, normally used to...
Subviral Agents01:29

Subviral Agents

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...

You might also read

Related Articles

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

Sort by
Same author

Short Report: Update on CCHFV Seroprevalence in Mauritanian Camels and Cattle Sampled Between 2020 and 2021.

Tropical medicine & international health : TM & IH·2026
Same author

Sero-epidemiology of Crimean-Congo haemorrhagic fever in mixed crop-livestock farming households in Burkina Faso: a one health study.

PloS one·2026
Same author

Relevance of potential endocytosis motifs in Cedar virus glycoprotein G for its biological activity.

Journal of virology·2026
Same author

Pathogen screening of Zambian ticks: new insights on the occurrence of tick-borne pathogens in the country.

Parasites & vectors·2026
Same author

First Detection of Usutu Virus in Harbor Seals (<i>Phoca vitulina</i>).

Viruses·2026
Same author

Case Report: Two cases of mammary intraductal papillary adenomas in nulliparous aged dairy cattle.

Frontiers in veterinary science·2026
Same journal

Characterization of a novel gene, Lsa(F), conferring resistance to pleuromutilins, lincosamides and streptogramin A in Streptococcus parasuis.

Veterinary research·2026
Same journal

Investigating the evolution of the Arctic lineage of canine distemper virus circulating in Italy.

Veterinary research·2026
Same journal

From inserts to 3D spheroids: MAC-T and BME-UV1 co-culture models for in vitro reconstruction of the bovine mammary epithelial architecture.

Veterinary research·2026
Same journal

The role of PlsC in Brucella melitensis virulence: impacts on membrane homeostasis, stress tolerance, and pathogenesis.

Veterinary research·2026
Same journal

Unveiling the clinical signs and pathology in red deer (Cervus elaphus) naturally infected with epizootic haemorrhagic disease virus serotype 8.

Veterinary research·2026
Same journal

Virus and host-associated variations in the interaction of low-pathogenic avian influenza viruses with the epithelial target tissue of the chicken reproductive tract.

Veterinary research·2026
See all related articles

Related Experiment Video

Updated: Jul 7, 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

Rodent models for prion diseases.

Martin H Groschup1, Anne Buschmann

  • 1Friedrich-Loeffler-Institut , Institute for Novel and Emerging Infectious Diseases, Südufer 10, 17493 Greifswald - Insel Riems, Germany. martin.groschup@fli.bund.de

Veterinary Research
|February 21, 2008
PubMed
Summary
This summary is machine-generated.

Transgenic mouse models are crucial for studying prion diseases, offering insights into disease mechanisms and the role of prion proteins (PrP) when cell culture systems are limited.

More Related Videos

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster
10:26

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Published on: March 12, 2018

Related Experiment Videos

Last Updated: Jul 7, 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

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster
10:26

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Published on: March 12, 2018

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Prion diseases, or transmissible spongiform encephalopathies (TSEs), lack robust cell culture models for propagation and infectivity assays.
  • Animal models, particularly transgenic mice, are essential for studying TSE pathogenesis and the prion protein (PrP).

Purpose of the Study:

  • To highlight the utility of transgenic mouse models in prion disease research.
  • To detail the applications of these models in understanding prion protein function and disease mechanisms.

Main Methods:

  • Utilizing transgenic mouse lines expressing cellular prion proteins (PrP) from various species.
  • Employing these models to investigate PrP(C) physiological roles, species barrier effects, and prion propagation.
  • Analyzing the impact of PrP mutations and polymorphisms on disease pathomechanisms.

Main Results:

  • Transgenic mice allow systematic analysis of TSE pathogenesis and prion strain infectivity.
  • These models facilitate research into PrP glycosylation, prion spread, and the roles of PrP(C) and PrP(D).
  • Mapping of PrP regions involved in conversion and replication, and modeling of familial human prion diseases.

Conclusions:

  • Transgenic mouse models are indispensable tools for advancing prion disease research due to limitations in cell culture systems.
  • They provide critical insights into the molecular and cellular mechanisms underlying prion pathogenesis and host interactions.