Special Issue "Feature Papers Prions"


A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Prions".

Deadline for manuscript submissions: closed (31 March 2014)

Special Issue Editor

Associate Editor
Dr. Byron Caughey
Senior Investigator, Chief, TSE/prion Biochemistry Section, Laboratory of Persistent Viral Diseases, NIH/NIAID Rocky Mountain Laboratories, 903 S 4th St., Hamilton, MT 59840, USA
Website: http://www.niaid.nih.gov/labsandresources/labs/aboutlabs/lpvd/tseprionbiochemistrysection/pages/caughey.aspx
Fax: +1 406 363 9286
Interests: TSEs (prion diseases); Prion structure, amplification and detection, and disease prevention and therapeutics; Prion protein functions and cell biology; Protein-folding diseases

Special Issue Information


Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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Published Papers

No papers have been published in this special issue yet, see below for planned papers.

Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: Prion-like Misfolding and Vasicular Spread of Toxic Proteins in Neurodegenerative Diseases
Authors: Edward Pokrishevsky, Judith M. Silverman and Neil R. Cashman*
Affiliation: Brain Research Centre, The University of British Columbia, 2211 Wesbrook Mall, Vancouver, BC V6T2B5, Canada (Neil.Cashman@vch.ca)
Abstract: Prion diseases, such as Creutzfeldt–Jakob disease, have been traditionally considered to be caused by a separate class of infectious agents. The pathologically misfolded prion protein can catalyze the conversion of its natively folded counterpart into the toxic form; therefore forming a recruiting seed for protein misfolding that may spread intercellularly until the entire tissue is infected. The transmission is thought to occur through an ongoing release and uptake of exosomes, small membranous vesicles used by both neurons and astrocytes for cell-to-cell communication. Recent discoveries expand the prion field, to include prion-like proteins implicated in other neurodegenerative diseases, including Alzheimer's, Parkinson's, Huntington's, amyotrophic lateral sclerosis, and the tauopathies. In addition to sustaining an intracellular recruitment, misfolding of prion-like proteins may also spread intercellularly, a process that is implied by the systematic spread of neurodegeneration. This pattern of infectivity suggests intercellular mechanisms of communications involving exosomes or continuous exchange of inclusions containing the disease specific infectious prion-like proteins. The goal of this review was twofold: to summarize the current state of knowledge of the prion-like proteins in neurodegenerative diseases and to examine their potential mechanisms of transmission.
Keywords: neurodegenerative diseases; Alzheimer’s; Huntington’s; Parkinson’s; amyotrophic lateral sclerosis; prions; exosomes

Last update: 25 March 2014

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