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 Experiment Videos

Prion protein conversion in vitro.

Surachai Supattapone1

  • 1Departments of Biochemistry and Medicine, Dartmouth Medical School, Hanover, NH 03755, USA. supattapone@dartmouth.edu

Journal of Molecular Medicine (Berlin, Germany)
|March 12, 2004
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Generation of Infectious Prions Amenable to Site-Specific Click Chemistry.

ACS chemical biology·2026
Same author

Fluorescent non-canonical amino acid as a site-specific conformational probe of prion formation.

bioRxiv : the preprint server for biology·2026
Same author

Generation of Infectious Prions Amenable to Site-specific Click Chemistry.

bioRxiv : the preprint server for biology·2026
Same author

Mutant knock-in mice display enhanced susceptibility to pure prion protein fibrils.

The Journal of general virology·2026
Same author

Genome-wide screens identify core regulators of cell surface prion protein expression.

Scientific reports·2026
Same author

Oligosaccharyltransferase (OST) complex inhibition effectively treats rodent and human prions.

PLoS pathogens·2026
Same journal

Non-transferrin-bound iron uptake by cardiomyocytes.

Journal of molecular medicine (Berlin, Germany)·2026
Same journal

Beyond the target: implications of Wnt pathway inhibitors on bone health.

Journal of molecular medicine (Berlin, Germany)·2026
Same journal

Proteomic analysis reveals divergent inflammatory mechanisms of COVID-associated Guillain-Barré syndrome.

Journal of molecular medicine (Berlin, Germany)·2026
Same journal

Integrative genetic and functional analysis of autosomal dominant hearing loss in 108 multigenerational families.

Journal of molecular medicine (Berlin, Germany)·2026
Same journal

Preclinical evaluation of cysteine protease-inhibitor aloxistatin (E64d) for heart failure therapy.

Journal of molecular medicine (Berlin, Germany)·2026
Same journal

Zinc-binding protein metallothionein 3 protects vascular smooth muscle cells from ferroptosis via blocking lysosomal degradation of GPX4.

Journal of molecular medicine (Berlin, Germany)·2026
See all related articles

Prion disease research reveals that protein misfolding requires specific cellular factors, including RNA and heparan sulfate, for efficient conversion of PrPC to PrPSc. These findings advance understanding of prion pathogenesis and diagnostic tool development.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Prion diseases involve the misfolding of host glycoprotein PrPC into infectious PrPSc.
  • The precise molecular mechanism of this PrPC to PrPSc conversion remains largely unknown.
  • In vitro systems are crucial for studying prion protein conformational changes.

Purpose of the Study:

  • To investigate the molecular mechanism of PrPC to PrPSc conversion in vitro.
  • To identify cellular factors that influence prion protein amplification.
  • To explore potential diagnostic and therapeutic targets for prion diseases.

Main Methods:

  • Studied prion-seeded conversion of PrPC to protease-resistant PrPSc-like molecules (PrPres) in purified and crude systems.
  • Utilized a modified protein misfolding cyclic amplification (PMCA) technique with normal brain homogenate.

Related Experiment Videos

  • Investigated the role of thiol-containing factors, RNA molecules, and heparan sulfate in PrPres formation.

    • Main Results:

    • In vitro PrPres amplification is specific to PrP sequence and prion strains.
    • Additional cellular factors in crude homogenates significantly enhance PrPres yield compared to purified systems.
    • PrPres amplification requires time, temperature, a neutral pH, and is inhibited by thiol blockers, indicating a thiol-containing factor is necessary.
    • Specific RNA molecules and heparan sulfate stimulate PrPres conversion, suggesting their role in prion pathogenesis.

    Conclusions:

    • The conformational change of PrPC to PrPSc in vitro is influenced by various cellular components.
    • Host-encoded RNA molecules and heparan sulfate proteoglycans are implicated in prion disease pathogenesis.
    • In vitro conversion and amplification assays offer promising mechanistic insights and potential for developing clinical tools for prion diseases.