proteinaceous Infectious particles - Toxicology

Proteinaceous infectious particles, commonly known as prions, represent a unique class of infectious agents that significantly impact both human health and veterinary science. Unlike bacteria, viruses, or fungi, prions are not living organisms. Instead, they are misfolded proteins that can induce other normal proteins in the brain to also misfold, leading to severe neurodegenerative diseases. This article delves into their significance in the field of toxicology, addressing several pertinent questions.

What Are Prions and How Are They Different from Other Infectious Agents?

Prions are abnormal, pathogenic agents that are transmissible and can induce abnormal folding of specific normal cellular proteins called prion proteins, primarily found in the brain. The misfolding of the prion protein leads to brain damage and the characteristic signs and symptoms of prion diseases. Unlike other infectious agents, prions do not contain nucleic acids (DNA or RNA), setting them apart from viruses and bacteria. This unique feature makes them resistant to standard decontamination procedures, posing challenges in clinical settings.

How Do Prions Relate to Toxicology?

In the context of toxicology, prions are considered biological toxins due to their ability to cause disease upon exposure. Their resistance to physical and chemical methods of deactivation, such as heat and disinfectants, complicates their management and containment. Toxicologists study the transmission pathways, environmental persistence, and potential methods for decontamination to mitigate prion-related risks. Understanding prion toxicity is crucial for developing safe handling procedures and therapeutic interventions.

What Diseases Are Associated with Prions?

Prions are responsible for a group of progressive conditions that affect the nervous system in humans and animals, known as transmissible spongiform encephalopathies (TSEs). In humans, notable diseases include Creutzfeldt-Jakob disease (CJD), variant Creutzfeldt-Jakob disease (vCJD), and kuru. In animals, prion diseases include bovine spongiform encephalopathy (BSE)

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Viroids, Satellite RNAs and Prions: Folding of Nucleic Acids and Misfolding of Proteins.

Issue Release: 2024

Prion diseases, always a threat?

Issue Release: 2024

Heterozygosity for cervid S138N polymorphism results in subclinical CWD in gene-targeted mice and progressive inhibition of prion conversion.

Issue Release: 2023

Injectable Slow-Release Hydrogel Formulation of a Plant Virus-Based COVID-19 Vaccine Candidate.

Issue Release: 2022

Reovirus uses temporospatial compartmentalization to orchestrate core versus outercapsid assembly.

Issue Release: 2022

Uptake, Retention, and Excretion of Infectious Prions by Experimentally Exposed Earthworms.

Issue Release: 2021

Chronic wasting disease in Europe: new strains on the horizon.

Issue Release: 2021

Ethanolamine Is a New Anti-Prion Compound.

Issue Release: 2021

Microbial Prions: Dawn of a New Era.

Issue Release: 2021

Transmissible α-synuclein seeding activity in brain and stomach of patients with Parkinson\'s disease.

Issue Release: 2021

Association of chronic wasting disease susceptibility with prion protein variation in white-tailed deer ().

Issue Release: 2020

Anti-prion drug screening system in Saccharomyces cerevisiae based on an artificial [LEU2] prion.

Issue Release: 2019

A Non-amyloid Prion Particle that Activates a Heritable Gene Expression Program.

Issue Release: 2019

Combining autophagy stimulators and cellulose ethers for therapy against prion disease.

Issue Release: 2019

Heterogeneity and Architecture of Pathological Prion Protein Assemblies: Time to Revisit the Molecular Basis of the Prion Replication Process?

Issue Release: 2019

Prion-like propagation of α-synuclein in neurodegenerative diseases.

Issue Release: 2019

A prolonged chronological lifespan is an unexpected benefit of the [PSI+] prion in yeast.

Issue Release: 2017

Region-specific protein misfolding cyclic amplification reproduces brain tropism of prion strains.

Issue Release: 2017

Prions on the run: How extracellular vesicles serve as delivery vehicles for self-templating protein aggregates.

Issue Release: 2017

Stepwise reversible nanomechanical buckling in a viral capsid.

Issue Release: 2017

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