Proteinaceous Infectious Particle (Prion) Biology

A special issue of Biology (ISSN 2079-7737). This special issue belongs to the section "Neuroscience".

Deadline for manuscript submissions: closed (30 April 2024) | Viewed by 234

Special Issue Editor


E-Mail Website
Guest Editor
1. CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), 205 route de Narbonne BP64182, F-31077 Toulouse, France
2. UPS, IPBS, Université de Toulouse, F-31077 Toulouse, France
3. LCC UPR8241 CNRS, F-31400 Toulouse, France
Interests: prion; amyloid; necroptosis; MLKL RIP kinase; Podospora
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Special Issue Information

Dear Colleagues,

Prions have been defined as infectious protein particles capable of spreading from one cell to another and infecting an entire tissue (or organ). While the term "PRION" was coined by S. Prusiner in 1992 to describe the element responsible for Kuru disease, RB Wickner's genetic studies in the yeast S. cerevisiae in 1994 provided proof that the transmission of the "PRION+" trait was supported by non-Mendelian heredity, i.e., via the expression of the gene encoding the protein. It was also demonstrated in yeast that the phenomena of variants (strains) of the prion form of the same protein corresponded to different states of aggregation. Indeed, prion proteins always include an amyloid hydrophobic domain whose aggregation modifies the function of the adjacent globular domain.

Structural analyses characterized the phenomenon of amyloid aggregation and the influence of the cellular environment on the stability of the aggregation core and thus explained the different propagation capacities of the structural variants. Amyloid domains are also present in many proteins that regulate cell fate, such as MLKL, the effector of necroptosis, whose fungal orthologue, HET-S from P. anserina, is itself stimulated by a prion form. The aim of this Special Issue is to provide a better understanding of potential prion amyloid proteins.

Dr. Marie-Lise Maddelein
Guest Editor

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Keywords

  • prions
  • prion diseases
  • infectious protein particles
  • prion formation
  • amyloid aggregation
  • prion amyloid proteins
  • yeast

Published Papers

There is no accepted submissions to this special issue at this moment.
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