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Updated: Aug 10, 2026

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

A prion disease with a novel 96-base pair insertional mutation in the prion protein gene

T A Campbell1, M S Palmer, R G Will

  • 1Prion Disease Group, Department of Biochemistry and Molecular Genetics, St. Mary's Hospital Medical School, London, UK.

Neurology
|March 1, 1996
PubMed

Insights

A novel four-octarepeat insertion in the prion protein gene was identified in a patient with Creutzfeldt-Jakob disease (CJD). This finding expands the known spectrum of prion protein gene mutations associated with neurodegenerative diseases.

Area of Science:

  • Neurogenetics
  • Prion Diseases
  • Molecular Biology

Background:

  • Inherited prion diseases are associated with mutations in the prion protein gene, including coding and insertional types.
  • Insertional mutations, typically involving multiple octapeptide repeat insertions, often lead to atypical dementias with variable symptoms.

Observation:

  • A previous report described a four-octarepeat insertion in an individual without neurological disease, who died from hepatic cirrhosis.
  • This study identifies a novel four-octarepeat insertional mutation in a patient presenting with classical Creutzfeldt-Jakob disease (CJD).

Findings:

  • The patient exhibited typical clinical, electroencephalographic, and histopathologic features of CJD.
  • A notable observation was pronounced prion protein immunoreactivity in the cerebellum's molecular layer.

Implications:

  • This case expands the known spectrum of prion protein gene mutations linked to inherited prion diseases.
  • The findings suggest that even smaller insertions, like the four-octarepeat, can cause classical CJD.
  • Further research is needed to understand the specific mechanisms by which this mutation leads to CJD and the significance of cerebellar pathology.

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