Issue |
Vet. Res.
Volume 39, Number 4, July-August 2008
Prion diseases in animals
|
|
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Number of page(s) | 30 | |
DOI | https://doi.org/10.1051/vetres:2008024 | |
Published online | 03 June 2008 | |
How to cite this article | Vet. Res. (2008) 39:47 |
DOI: 10.1051/vetres:2008024
Review
Prion agent diversity and species barrier
Vincent Béringue1, Jean-Luc Vilotte2 and Hubert Laude11 Institut National de la Recherche Agronomique (INRA), UR892, Virologie et Immunologie Moléculaires, F-78350 Jouy-en-Josas, France
2 INRA, UR339, Génétique Biochimique et Cytogénétique, F-78350 Jouy-en-Josas, France
Received 25 March 2008; accepted 30 May 2008; published online 03 June 2008
Abstract - Mammalian prions are the infectious agents responsible for transmissible
spongiform encephalopathies (TSE), a group of fatal, neurodegenerative
diseases, affecting both domestic animals and humans. The most widely
accepted view to date is that these agents lack a nucleic acid genome and
consist primarily of PrP, a misfolded, aggregated form of the
host-encoded cellular prion protein (PrP
) that propagates by
autocatalytic conversion and accumulates mainly in the brain. The BSE
epizooty, allied with the emergence of its human counterpart, variant CJD,
has focused much attention on two characteristics that prions share with
conventional infectious agents. First, the existence of multiple prion
strains that impose, after inoculation in the same host, specific and stable
phenotypic traits such as incubation period, molecular pattern of PrP
and neuropathology. Prion strains are thought to be enciphered within
distinct PrP
conformers. Second, a transmission barrier exists that
restricts the propagation of prions between different species. Here we
discuss the possible situations resulting from the confrontation between
species barrier and prion strain diversity, the molecular mechanisms
involved and the potential of interspecies transmission of animal prions,
including recently discovered forms of TSE in ruminants.
Key words: prion / strain / misfolding / species barrier / PrP
Corresponding author: vincent.beringue@jouy.inra.fr
© INRA, EDP Sciences 2008