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.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 498135
Title Prion type-dependent deposition of PRNP allelic products in heterozygous sheep
Author(s) Langeveld, J.P.M.; Jacobs, J.G.; Hunter, N.; Keulen, L.J.M. van; Lantier, F.; Zijderveld, F.G. van; Bossers, A.
Source Journal of Virology 90 (2016)2. - ISSN 0022-538X - p. 805 - 812.
DOI https://doi.org/10.1128/JVI.02316-15
Department(s) CVI Infection Biology
CVI onderzoek
Publication type Refereed Article in a scientific journal
Publication year 2016
Abstract

Susceptibility or resistance to prion infection in humans and animals depends on single prion protein (PrP) amino acid substitutions in the host, but the agent's modulating role has not been well investigated. Compared to disease incubation times in wild-type homozygous ARQ/ARQ (where each triplet represents the amino acids at codons 136, 154, and 171, respectively) sheep, scrapie susceptibility is reduced to near resistance in ARR/ARR animals while it is strongly enhanced in VRQ/VRQ carriers. Heterozygous ARR/VRQ animals exhibit delayed incubation periods. In bovine spongiform encephalopathy (BSE) infection, the polymorphism effect is quite different although the ARR allotype remains the least susceptible. In this study, PrP allotype composition in protease-resistant prion protein (PrPres) from brain of heterozygous ARR/ VRQ scrapie-infected sheep was compared with that of BSE-infected sheep with a similar genotype. A triplex Western blotting technique was used to estimate the two allotype PrP fractions in PrPres material from BSE-infected ARR/VRQ sheep. PrPres in BSE contained equimolar amounts of VRQ- and ARR-PrP, which contrasts with the excess (>95%) VRQPrP fraction found in PrP in scrapie. This is evidence that transmissible spongiform encephalopathy (TSE) agent properties alone, perhaps structural aspects of prions (such as PrP amino acid sequence variants and PrP conformational state), determine the polymorphic dependence of the PrPres accumulation process in prion formation as well as the disease-associated phenotypic expressions in the host.

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