Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

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Record number 418146
Title Prion protein self-interaction in prion disease therapy approaches
Author(s) Rigter, A.; Priem, J.; Langeveld, J.P.M.; Bossers, A.
Source Veterinary Quarterly 31 (2011)3. - ISSN 0165-2176 - p. 115 - 128.
DOI https://doi.org/10.1080/01652176.2011.604976
Department(s) Central Veterinary Institute
CVI Infection Biology
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) creutzfeldt-jakob-disease - in-vitro conversion - susceptibility-linked polymorphisms - bovine spongiform encephalopathy - natural scrapie - insert mutation - cell-cultures - prp genotypes - closed flock - prnp gene
Abstract 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.
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