Related Experiment Video
Updated: Oct 23, 2025

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
Published on: August 8, 2017
Molecular foundations of prion strain diversity
Manfredi Carta1, Adriano Aguzzi1
1Institute of Neuropathology, University Hospital of Zurich, University of Zurich, Schmelzbergstrasse 12, 8091 Zurich, Switzerland.
Abstract:
Despite being caused by a single protein, prion diseases are strikingly heterogenous. Individual prion variants, known as strains, possess distinct biochemical properties, form aggregates with characteristic morphologies and preferentially seed certain brain regions, causing markedly different disease phenotypes. Strain diversity is determined by protein structure, post-translational modifications and the presence of extracellular matrix components, with single amino acid substitutions or altered protein glycosylation exerting dramatic effects. Here, we review recent advances in the study of prion strains and discuss how a deeper knowledge of the molecular origins of strain heterogeneity is providing a foundation for the development of anti-prion therapeutics.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Modern Molecular Taxonomy
Exon Recombination
Exon shuffling follows “splice frame rules.” Each exon...
Mutations in Microorganisms
Diversity of Archaea III
Mutation, Gene Flow, and Genetic Drift

