Classic Scrapie in Sheep with the ARR/ARR Prion Genotype in Germany and France

Groschup, Martin H.; Lacroux, Caroline; Buschmann, A.; Lühken, Gesine; Mathey, Jacinthe; Eiden, Martin; Lugan, Séverine; Hoffmann, Christine; Espinosa, Juan Carlos; Baron, Thierry; Torres, Juan María; Erhardt, G.; Andréoletti, Olivier

doi:10.3201/eid1308.070077

Cited by 89 publications

(75 citation statements)

References 20 publications

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“…Occasionally R2 animals are found with scrapie [7] which up to recently distinguished them from R1 animals (ARR/ARR) which were regarded as fully resistant to natural scrapie, although not to experimental exposure to BSE [46]. It has now been shown for two ARR/ARR animals from two different populations that they can carry classical scrapie, though both were subclinical cases [39].…”

Section: Classical Scrapie In Sheepmentioning

confidence: 99%

PrPgenetics in ruminant transmissible spongiform encephalopathies

2008

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-Scrapie, bovine spongiform encephalopathy (BSE), and chronic wasting disease (CWD) are prion diseases in ruminants with considerable impact on animal health and welfare. They can also pose a risk to human health and control is therefore an important issue. Prion protein (PrP) genetics may be used to control and eventually eradicate animal prion diseases. The PrP gene in sheep and other representatives of the order Artiodactyles has many polymorphisms of which several are crucial determinants of susceptibility to prion diseases, also known as transmissible spongiform encephalopathies (TSE). This review will present the current understanding of PrP genetics in ruminants highlighting similarity and difference between the species in the context of TSE.

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Section: Classical Scrapie In Sheepmentioning

confidence: 99%

PrPgenetics in ruminant transmissible spongiform encephalopathies

2008

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“…The ARR allele has been associated with resistance to scrapie. However, the experimental infection of homozygous ARR sheep with BSE [42] and the recent detection of two cases of classical scrapie in ARR homozygous sheep [38] imply that resistance is not absolute in ARR homozygous individuals. The AHQ, ARH, ARQ, and VRQ alleles are generally associated with susceptibility.…”

Section: Introductionmentioning

confidence: 99%

The evidence of associations between prion protein genotype and production, reproduction, and health traits in sheep

Sweeney

Hanrahan

2008

Vet. Res.

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“…Sheep homozygous for the V 136 R 154 Q 171 (VRQ) allele are highly susceptible to classical scrapie whereas sheep homozygous for A 136 R 154 R 171 (ARR) exhibit pronounced resistance [16,72]. The latter characteristic has been rarely overcome [84]. Such a tight control of scrapie prion replication by ovine PrP polymorphisms can be reproduced both at the cellular level, in infected cell cultures [168], and in cell-free assays [29], arguing for a preponderant role of the PrP sequence over other genetic factors in sheep breeds.…”

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confidence: 99%

Prion agent diversity and species barrier

2008

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-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 Sc , a misfolded, aggregated form of the host-encoded cellular prion protein (PrP C ) 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 Sc and neuropathology. Prion strains are thought to be enciphered within distinct PrP Sc 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.prion / strain / misfolding / species barrier / PrP Table of Mammalian prion diseases or transmissible spongiform encephalopathies (TSE) form a group of related, invariably fatal neurodegenerative disorders of both animals and humans. The brain pathology consists of spongiosis, astrocytosis, neuronal loss and neural tissue from affected individuals contains an infectious agent, the prion, setting these diseases apart from other neurodegenerative diseases. Prion replication is thought to involve in essence the self-perpetuating conversion of the host-encoded cellular prion protein (PrP C ) into a misfolded form (PrP Sc ) that tends to aggregate and may be neurotoxic (for reviews [1,157]). Prion replication may also occur in lymphoid tissues but is there poorly if not pathogenic (for review [126], [133]). PrP C is a protein with two variably occupied glycosylation sites. It is attached at the outer of the plasma membrane by a glycosylphosphatidylinositol anchor. Its secondary structure is rich in alpha-helix and the protein is likely to be in a monomeric state in mild detergents. While its precise physiological function has not been assigned, PrP C is essential for prion replication and neurotoxicity to occur [57,129]. Upon infection, PrP C is refolded -without apparent post-translational modification -into beta-sheet -rich PrP Sc , initially in the presence of exogenous PrP Sc and then by an autocatalytic process. It leads to the formation of aggregates, sometimes of amyloid type, that can be differentiated from PrP C because of their partial resistance to protease digestion and of their insolubility into non-denaturing detergents [153]. Proteinase K, the most commonly used protease, di...

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Classic Scrapie in Sheep with the ARR/ARR Prion Genotype in Germany and France

Abstract: We report 2 natural scrapie cases in sheep carrying the ARR/ARR prion genotype, which is believed to confer resistance against classic scrapie and bovine spongiform encephalopathy.

Cited by 89 publications

References 20 publications

PrPgenetics in ruminant transmissible spongiform encephalopathies

PrPgenetics in ruminant transmissible spongiform encephalopathies

The evidence of associations between prion protein genotype and production, reproduction, and health traits in sheep

Prion agent diversity and species barrier

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