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Amyloid Fibrils03:03

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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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Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells
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Distinct amyloid fibril structures formed by ALS-causing SOD1 mutants G93A and D101N.

Mu-Ya Zhang1, Yeyang Ma2,3, Li-Qiang Wang4

  • 1Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, TaiKang Center for Life and Medical Sciences, Wuhan University, 430072, Wuhan, China.

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|August 26, 2025
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Summary

Amyotrophic lateral sclerosis (ALS) is linked to SOD1 mutations. Cryo-EM structures reveal distinct G93A and D101N mutant SOD1 amyloid fibril formations, with G93A fibrils showing higher toxicity.

Keywords:
Amyloid FibrilsAmyotrophic Lateral Sclerosis (ALS)Cryo-EM StructureSOD1 MutantsToxicity

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Area of Science:

  • Neuroscience
  • Structural Biology
  • Biochemistry

Background:

  • Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease.
  • Over 200 genetic mutations in SOD1 are associated with ALS.
  • SOD1-G93A transgenic mice are widely used ALS research models.

Purpose of the Study:

  • To determine the cryo-electron microscopy (cryo-EM) structures of amyloid fibrils formed by SOD1 G93A and D101N mutants.
  • To investigate the structural differences between mutant SOD1 fibrils and native SOD1 fibrils.
  • To compare the cytotoxicity of G93A and D101N SOD1 fibrils.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to resolve fibril structures.
  • Structural analysis of fibril core configurations.
  • Toxicity assays to compare mutant SOD1 fibrils.

Main Results:

  • Two distinct cryo-EM structures of SOD1 G93A and D101N amyloid fibrils were determined.
  • Both mutants formed amyloid fibrils with unique serpentine configurations, distinct from native SOD1 fibrils.
  • G93A fibrils exhibited significantly higher toxicity than D101N fibrils, which showed toxicity comparable to wild-type SOD1 fibrils.

Conclusions:

  • SOD1 mutations G93A and D101N lead to distinct amyloid fibril structures.
  • The structural variations correlate with differential cytotoxicity, offering insights into ALS pathogenesis.
  • This study elucidates structural mechanisms of SOD1 aggregation and cytotoxicity in ALS.