Search research articles

Related Concept Videos

Subviral Agents

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...

Rabies

Rabies

Rabies is a lethal zoonotic disease caused by a single-stranded, negative-sense RNA virus of the Lyssavirus genus, within the family Rhabdoviridae. Its primary mode of transmission to humans is through bites or saliva-contaminated scratches from infected mammals such as dogs, bats, raccoons, or foxes. Transmission can also occur if infectious saliva contacts abraded skin or intact mucous membranes, including the conjunctiva.Viral Entry and Early ReplicationOnce introduced at the bite or scratch...

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Home
A Molecular Switch Controls Interspecies Prion Disease Transmission In Mice.

Home
A Molecular Switch Controls Interspecies Prion Disease Transmission In Mice.

Related Experiment Video

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

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

Published on: January 8, 2015

A molecular switch controls interspecies prion disease transmission in mice.

Christina J Sigurdson¹, K Peter R Nilsson, Simone Hornemann

¹Department of Pathology and Department of Medicine, University of California, San Diego, La Jolla, California 92093, USA. csigurdson@ucsd.edu

The Journal of Clinical Investigation

|June 17, 2010

View abstract on PubMed

Summary

This summary is machine-generated.

Prion protein structure significantly impacts cross-species transmission of transmissible spongiform encephalopathies. Similar beta2-alpha2 loop structures in prion proteins facilitate transmission, while differences create barriers.

More Related Videos

Protein Misfolding Cyclic Amplification of Prions

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay

Published on: March 10, 2015

Related Experiment Videos

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

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

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay

Published on: March 10, 2015

Area of Science:

Neurodegenerative diseases
Prion biology
Structural biology

Background:

Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative disorders caused by misfolded prion proteins (PrPSc).
Cross-species transmission of TSEs is influenced by prion protein sequence and structure.
The beta2-alpha2 loop of the prion protein is a key region varying between species.

Purpose of the Study:

To investigate the role of the prion protein's beta2-alpha2 loop structure in interspecies transmission barriers.
To determine if structural similarity or dissimilarity in the beta2-alpha2 loop influences prion transmissibility.
To correlate specific amino acid polymorphisms (170S/N) with transmission efficiency.

Main Methods:

Inoculation of prions from five species into transgenic mice expressing engineered PrPC variants with altered beta2-alpha2 loops (disordered vs. rigid).

Analysis of transmission efficiency based on structural similarity between incoming PrPSc and host PrPC.

Classification of existing literature data on cross-species prion transmission based on the 170S/N polymorphism.

Main Results:

Efficient prion transmission occurred when the beta2-alpha2 loop structures were similar between species.
Dissimilar loop structures correlated with strong transmission barriers.
Cross-species transmission barriers were generally lower between species sharing the same amino acid residue at position 170.

Conclusions:

The structural conformation of the beta2-alpha2 loop in prion proteins plays a critical role in determining interspecies transmissibility.
Amino acid variations at position 170 significantly influence prion transmission barriers.
Understanding loop structure is key to predicting and potentially mitigating prion disease spread between species.