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Procedures for Identifying Infectious Prions After Passage Through the Digestive System of an Avian Species
Published on: November 6, 2013
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Prion and prion-like diseases in animals
Patricia Aguilar-Calvo1, Consolación García1, Juan Carlos Espinosa1
1Centro de Investigación en Sanidad Animal (CISA-INIA), 28130 Valdeolmos, Madrid, Spain.
Virus Research
|December 3, 2014
Summary
Transmissible spongiform encephalopathies (TSEs) are fatal brain diseases caused by misfolded prion proteins. This review explores prion-like diseases and evidence suggesting non-prion proteins may also transmit similarly.
Area of Science:
- Neurodegenerative diseases
- Protein misfolding disorders
- Prion biology
Background:
- Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases.
- Prion protein aggregation is a hallmark of TSEs.
- Other proteins like amyloid-beta and tau may share pathogenic mechanisms with prions.
Purpose of the Study:
- To review prion and prion-like diseases in animals.
- To discuss findings on the transmissibility of non-prion proteins.
- To explore similarities between prion and prion-like protein propagation.
Main Methods:
- Literature review of prion and prion-like diseases.
- Analysis of recent research on protein misfolding and transmission.
- Comparative study of pathogenic mechanisms.
Main Results:
- Prion diseases are characterized by misfolded prion protein accumulation.
- Proteins like amyloid-beta, tau, and SAA are implicated in prion-like diseases.
- Emerging evidence suggests potential transmissibility of certain non-prion proteins.
Conclusions:
- Prion-like diseases share features with prion diseases.
- Further research is needed to confirm the transmissibility of non-prion proteins.
- Understanding these mechanisms is crucial for developing therapies.
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