Prion protein self-interaction in prion disease therapy approaches

Autor: J. Priem, Jan P. M. Langeveld, Alan Rigter, Alex Bossers
Jazyk: angličtina
Rok vydání: 2011
Předmět:
Prions
Bovine spongiform encephalopathy
animal diseases
Scrapie
Disease
Biology
Creutzfeldt-Jakob Syndrome
Prion Diseases
Wageningen Bioveterinary Research
Disease therapy
in-vitro conversion
cell-cultures
medicine
Animals
Humans
Prion protein
bovine spongiform encephalopathy
natural scrapie
creutzfeldt-jakob-disease
chemistry.chemical_classification
Host Pathogen Interaction & Diagnostics
closed flock
prnp gene
Polymorphism
Genetic
Sheep
General Veterinary
prp genotypes
Bacteriologie
Bacteriology
Bacteriology
Host Pathogen Interaction & Diagnostics
medicine.disease
Virology
Host Pathogen Interactie & Diagnostiek
Amino acid
nervous system diseases
chemistry
Cell culture
insert mutation
Bacteriologie
Host Pathogen Interactie & Diagnostiek
Species barrier
Cattle
susceptibility-linked polymorphisms
Zdroj: Veterinary Quarterly 31 (2011) 3
Veterinary Quarterly, 31(3), 115-128
ISSN: 0165-2176
DOI: 10.1080/01652176.2011.604976
Popis: Transmissible spongiform encephalopathies (TSEs) or prion diseases are unique disorders that are not caused by infectious micro-organisms (bacteria or fungi), viruses or parasites, but rather seem to be the result of an infectious protein. TSEs are comprised of fatal neurodegenerative disorders affecting both human and animals. Prion diseases cause sponge-like degeneration of neuronal tissue and include (among others) Creutzfeldt-Jacob disease in humans, bovine spongiform encephalopathy (BSE) in cattle and scrapie in sheep. TSEs are characterized by the formation and accumulation of transmissible (infectious) disease-associated protease-resistant prion protein (PrP(Sc)), mainly in tissues of the central nervous system. The exact molecular processes behind the conversion of PrP(C) into PrP(Sc) are not clearly understood. Correlations between prion protein polymorphisms and disease have been found, however in what way these polymorphisms influence the conversion processes remains an enigma; is stabilization or destabilization of the prion protein the basis for a higher conversion propensity? Apart from the disease-associated polymorphisms of the prion protein, the molecular processes underlying conversion are not understood. There are some notions as to which regions of the prion protein are involved in refolding of PrP(C) into PrP(Sc) and where the most drastic structural changes take place. Direct interactions between PrP(C) molecules and/or PrP(Sc) are likely at the basis of conversion, however which specific amino acid domains are involved and to what extent these domains contribute to conversion resistance/sensitivity of the prion protein or the species barrier is still unknown.
Databáze: OpenAIRE
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