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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,...
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Neutralizing Mutations Significantly Inhibit Amyloid Formation by Human Prion Protein and Decrease Its Cytotoxicity.

Jun-Jie Huang1, Xiang-Ning Li1, Wan-Li Liu1

  • 1Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan 430072, China.

Journal of Molecular Biology
|December 11, 2019
PubMed
Summary
This summary is machine-generated.

A common genetic variation, G127V, protects against prion diseases by inhibiting prion protein (PrP) misfolding and reducing cell damage. This discovery opens doors for new prion disease treatments.

Keywords:
Neutralizing mutationPrion diseasesPrion proteinProtein aggregationProtein phase separation

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Prion diseases are fatal neurodegenerative disorders caused by misfolded prion protein (PrP).
  • A human PrP polymorphism, G127V, offers protection, but its mechanism is unclear.
  • Understanding PrP misfolding is crucial for developing treatments.

Purpose of the Study:

  • To elucidate the protective mechanism of the G127V polymorphism in human prion protein (PrP).
  • To investigate the impact of introducing different hydrophobic amino acids at position 127 of PrP.
  • To assess the therapeutic potential of G127V and related mutations against PrP-induced cytotoxicity.

Main Methods:

  • Investigated the effect of the G127V polymorphism on human PrP amyloid fibril formation.
  • Introduced an isoleucine (Ile) at position 127 (G127I) to assess the role of hydrophobic chains.
  • Evaluated the impact of G127V and G127I on PrP-induced cytotoxicity, mitochondrial damage, and reactive oxygen species (ROS) production using the PrP 106-126 peptide.

Main Results:

  • The G127V polymorphism significantly inhibits human PrP amyloid fibril formation due to an introduced hydrophobic chain.
  • The G127I mutation, with a similar hydrophobic modification, demonstrated comparable protective effects to G127V.
  • Both G127V and G127I mutations substantially reduced PrP-induced cytotoxicity, mitochondrial damage, and ROS production.

Conclusions:

  • The hydrophobic nature of amino acid substitutions at position 127 is key to inhibiting PrP misfolding and aggregation.
  • G127V and G127I act as effective neutralizing mutations, mitigating PrP cytotoxicity.
  • These findings provide a molecular basis for natural protection against prion diseases and suggest new therapeutic avenues.