Deciphering the Molecular Targets of Prion and Prion-Like Strains

Dear Colleagues,

Prion strains are conformational variants of abnormal prion proteins and can be distinguished by differences in disease incubation times, lesion profiles and electrophoretic mobilities. It has long been postulated that differences in clinical phenotypes may be associated with distinct prion strains, but direct evidence for this hypothesis is missing due to the lack of understanding of molecular disease pathways.

While initially attributed to prion diseases, it is now becoming evident that strains of aggregation-prone proteins are found in other neurodegenerative diseases. Recent data on the strain-properties of α-synuclein, Tau, Aβ, SOD1, and TDP-43 suggests that strains may be a ubiquitous phenomenon of pathogenic protein aggregates. Data on selective neuronal vulnerability and distinct clinical phenotypes in Alzheimer’s disease, Parkinson’s disease, amyotrophic lateral sclerosis and tauopathies show compelling analogies with those in prion diseases.

This common interest in prion-like mechanisms across disciplines in dementia research creates opportunities to identify the critical targets and disease pathways of neurodegeneration that may be difficult or impossible to infer from the data available to a single discipline. The critical and most challenging question concerns the mechanistic underpinning of the selective neuronal vulnerability of strains. To address this, the most suitable and advanced models, from tissue cultures to mouse models, have to be implemented to provide translatable data.

This Special Issue is a forum to share and publish data and insights on the strain properties of protein aggregates, including recent data on the molecular targets of strains, biological and/or adaptive responses to strains and suggestions for new concepts to decipher the molecular targets of selective neuronal vulnerability.

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