Journal Article (Review Article)

DZNE-2026-01161

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The evolution of prion cell biology: from viruses to prions to prion-like proteins.

Vorberg, I. M. (First author)DZNE* ; Priola, S. A.

2026
Springer Heidelberg

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Please use a persistent id in citations: doi:10.1007/s00401-026-03099-y

Abstract: Prion diseases are inevitably fatal, rare, and infectious neurodegenerative diseases of humans and animals. Initially, they were thought to be caused by unconventional slow viruses, and early research therefore relied heavily on experimental approaches used in virology. This view changed with the discovery that the causative agent of these diseases is not a virus but a conformational variant of a host-encoded protein. The conversion of the normally soluble host prion protein into an insoluble, infectious form enables the spread of pathology between cells and throughout the host. Over the past two decades, it has become clear that similar prion-like mechanisms of protein misfolding and templated self-propagation also underlie more common, non-infectious neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. Thus, just as the cell biology of viruses provided important insights into the first studies of prion cell biology, discoveries in prion research have profoundly influenced our understanding of the cell biology of other amyloid-forming proteins. In this review, we discuss common principles and differences in the cell biology of prions and prion-like particles. We also highlight the seminal contributions of the late Dr. Byron Caughey and his laboratory, whose pioneering work has helped to shape our current understanding of how pathogenic protein aggregates form, propagate, and ultimately cause devastating neurological diseases.

Keyword(s): Humans (MeSH) ; Animals (MeSH) ; Prions: metabolism (MeSH) ; Prion Diseases: metabolism (MeSH) ; Prion Diseases: pathology (MeSH) ; Neurodegeneration ; Prion ; Prion-like ; Seeded polymerization ; TDP-43 ; Tau ; α-Synuclein ; Prions

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Contributing Institute(s):

1. Prion Cell Biology (AG Vorberg)

Research Program(s):

1. 352 - Disease Mechanisms (POF4-352) (POF4-352)

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Database coverage:
; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; DEAL Springer ; DEAL Springer ; Ebsco Academic Search ; Essential Science Indicators ; IF >= 10 ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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