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Prion Strains and Transmission Barrier Phenomena.

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TLDR
This review presents a focus on a few advances in the field of prion structure and prion strains characterization: from the historical approaches that allowed the concept of prions to emerge, to the last results demonstrating that a prion strain may in fact be a combination of a few quasi species with subtle biophysical specificities.
Abstract
Several experimental evidences show that prions are non-conventional pathogens, which physical support consists only in proteins. This finding raised questions regarding the observed prion strain-to-strain variations and the species barrier that happened to be crossed with dramatic consequences on human health and veterinary policies during the last 3 decades. This review presents a focus on a few advances in the field of prion structure and prion strains characterization: from the historical approaches that allowed the concept of prion strains to emerge, to the last results demonstrating that a prion strain may in fact be a combination of a few quasi species with subtle biophysical specificities. Then, we will focus on the current knowledge on the factors that impact species barrier strength and species barrier crossing. Finally, we present probable scenarios on how the interaction of strain properties with host characteristics may account for differential selection of new conformer variants and eventually species barrier crossing.

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Journal ArticleDOI

The ecology of chronic wasting disease in wildlife.

TL;DR: Research gaps in CWD prion ecology include the need to identify specific biological characteristics of potential CWD reservoir species that better explain susceptibility to spillover, landscape and climate configurations that are suitable for CWD transmission, and the magnitude of sampling bias in the current understanding of CWD distribution and risk.
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Cofactor and glycosylation preferences for in vitro prion conversion are predominantly determined by strain conformation

TL;DR: The hypothesis that strain-specific patterns of prion neurotropism are generated by selection of differentially distributed cofactors molecules and/or PrPC glycoforms during prion replication is supported.
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Transmission studies of chronic wasting disease to transgenic mice overexpressing human prion protein using the RT-QuIC assay.

TL;DR: CWD transmission into two additional strains of transgenic mice (tg66 and tgRM) are tested, finding that these mice over-express human prion protein at high levels and are highly sensitive to infection by human-tropic prions.
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Immunotherapy against Prion Disease

TL;DR: It is proposed that immunotherapy is a plausible and practical therapeutic strategy and advocate more studies in this area to develop effective measures to control and treat these devastating disorders.
References
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Journal ArticleDOI

Novel proteinaceous infectious particles cause scrapie

TL;DR: A new term "prion" is proposed to denote a small proteinaceous infectious particle which is resistant to inactivation by most procedures that modify nucleic acids.
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Mice devoid of PrP are resistant to scrapie

TL;DR: These experiments show that PrPC, possibly at close to normal levels, is required for the usual susceptibility to scrapie and that lack of homology between incoming prions and the host's PrP genes retards disease.
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Transmissions to mice indicate that ‘new variant’ CJD is caused by the BSE agent

TL;DR: It is shown that the strain of agent from cattle affected by bovine spongiform encephalopathy (BSE) produces a characteristic pattern of disease in mice that is retained after experimental passage through a variety of intermediate species, providing strong evidence that the same agent strain is involved in both BSE and vCJD.
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Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD

TL;DR: Strain characteristics revealed here suggest that the prion protein may itself encode disease phenotype, consistent with BSE being the source of this new disease.
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Eight prion strains have PrP Sc molecules with different conformations

TL;DR: It is indicated that each of the eight prion strains has a PrP sc molecule with a unique conformation and that the variation in incubation times is related to the relative protease sensitivity of PrPSc in each strain.
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