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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...
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...
Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...
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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Published on: January 8, 2015

Prions: protein aggregation and infectious diseases.

Adriano Aguzzi1, Anna Maria Calella

  • 1Institute of Neuropathology, University Hospital of Zurich, Zurich, Switzerland. adriano.aguzzi@usz.ch

Physiological Reviews
|October 1, 2009
PubMed
Summary

Transmissible spongiform encephalopathies (TSEs), or prion diseases, involve abnormal prion protein propagation causing neurodegeneration. Understanding the cellular prion protein (PrPC) role is key to elucidating disease mechanisms and developing therapies.

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

  • Neuroscience
  • Pathology
  • Biochemistry

Background:

  • Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative conditions affecting humans and animals.
  • Prions, misfolded proteins, propagate by converting host cellular prion protein (PrPC) into the abnormal form.
  • The exact mechanisms of neuronal damage and death in prion diseases remain unclear.

Purpose of the Study:

  • To review the evolution of the prion concept.
  • To explore prion-like mechanisms in other protein aggregation diseases.
  • To discuss the clinical and pathological features, neuroinvasion, and brain damage in prion diseases.
  • To cover potential antiprion therapies and diagnostic advancements.

Main Methods:

  • Literature review and synthesis of existing research on prions and TSEs.
  • Discussion of prion replication and propagation mechanisms.
  • Analysis of clinical presentations and pathological findings in affected species.
  • Examination of therapeutic strategies and diagnostic tools.

Main Results:

  • Prion propagation is dependent on the host's PrPC.
  • Prion toxicity may stem from disruption of normal PrPC functions.
  • Prion-like mechanisms are relevant to other proteinopathies.
  • Neuroinvasion and brain damage involve complex pathological cascades.

Conclusions:

  • Understanding PrPC's physiological role is crucial for deciphering prion disease pathogenesis.
  • Further research into antiprion therapies and diagnostics is ongoing.
  • Prion diseases share common features with other neurodegenerative disorders involving protein misfolding.