Experimental Production of Scrapie in Goats

Pattison, I.H.; Gordon, W. S.; Millson, G.C.

doi:10.1016/s0368-1742(59)80029-1

Cited by 73 publications

(26 citation statements)

References 5 publications

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“…Foster & N. Hunter, unpublished results). Our SSBP/1 results are also in agreement with previous data on SSBP/1-affected goats, which succumbed 420-680 days post-inoculation (Pattison et al, 1959;Pattison & Millson, 1960).…”

Section: Discussionsupporting

confidence: 93%

Novel polymorphisms in the caprine PrP gene: a codon 142 mutation associated with scrapie incubation period

Goldmann

Martin²,

Foster

et al. 1996

Journal of General Virology

162

167

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Section: Discussionsupporting

confidence: 93%

Novel polymorphisms in the caprine PrP gene: a codon 142 mutation associated with scrapie incubation period

Goldmann

Martin²,

Foster

et al. 1996

Journal of General Virology

162

167

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“…When a new disease phenotype is seen following passage, it has been difficult therefore to differentiate between host and strain effects, and in particular to know whether there has been strain mutation or adaptation or whether the new host has selected from a mixture of pre-existing strains in the donor. [38][39][40] Our results confirm that not all the pathological features of cloned murine strains are transferred to the sheep host, in which phenotypic variability appears to be dependant of host factors such as Prnp genotype or breed. Although not definitive as the inocula were cloned this phenotypic variability would not appear to be due to the existence of a mixture of strains in the infectious material given to sheep.…”

Section: Discussionsupporting

confidence: 68%

Disease phenotype in sheep after infection with cloned murine scrapie strains

Sisó

Chianini

Eaton

et al. 2012

Prion

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“…The first example is the observation that experimental transmission of a pool of scrapieinfected sheep brains (SSBP/1) to goats resulted in two clinical disease phenotypeseither a 'scratching' or 'drowsy' syndromethat were conserved on subpassage [145,146]. The question arises of whether distinct strain components pre-existed in the original pool and found clinical manifestation in goats, or whether a variant TSE agent emerged upon confrontation to a foreign PrP sequence.…”

Section: Emergence Of a New Strainmentioning

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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Experimental Production of Scrapie in Goats

Cited by 73 publications

References 5 publications

Novel polymorphisms in the caprine PrP gene: a codon 142 mutation associated with scrapie incubation period

Novel polymorphisms in the caprine PrP gene: a codon 142 mutation associated with scrapie incubation period

Disease phenotype in sheep after infection with cloned murine scrapie strains

Prion agent diversity and species barrier

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