Amyloid prions in fungi

Sven J. Saupe, Daniel F. Jarosz, Heather L. True

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

1 Scopus citations

Abstract

In 1994, a paper signed by a single author based on genetic approaches opened a decisive breach leading to a dramatic expansion of our perception of the biological significance of the prion phenomenon (1). In the following years, biochemical reconstitution and transformation established that these biological entities, originally identified and defined in the context of mammalian diseases such as Kuru or Creutzfeldt-Jacob disease, also exist in yeast as "protein-based genes" and correspond to previously described non-Mendelian genetic elements (2, 3). It is now clear that in most known cases the physical basis for prion propagation is the formation, growth, and fragmentation of an amyloid aggregate. Amyloids are ordered protein polymers with a so-called cross-beta; structure (4). The original definition of prions as "infectious proteinaceous particles" is imprecise enough to still be operational today but as a consequence embraces a variety of biological phenomena and structural features (5). Defining prions thus remains a nontrivial task. While a more restrictive definition is perhaps neither possible nor desirable, this general term induces some confusion and controversy. In an attempt to clarify discourse, at some point investigators in the mammalian disease-related field denied the fungal "infectious proteinaceous particles" the name of prions and proposed instead to term them "prionoids" (6). These semantic battles should not be disregarded as sterile, but rather should be taken as an indication of the variety of the biological realities that the term covers.

Original languageEnglish
Title of host publicationThe Fungal Kingdom
Publisherwiley
Pages673-685
Number of pages13
ISBN (Electronic)9781683670827
ISBN (Print)9781555819576
DOIs
StatePublished - Sep 5 2017

Keywords

  • Amyloid prions
  • Biotic interactions
  • Chaperones modulate prion formation
  • Fungal prion structures
  • Genetic diversity
  • Prion formation
  • Signal transduction

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