Susceptibility of Mink to Sheep Scrapie

Hanson, R. P.; Eckroade, Robert J.; Marsh, Richard F.; Rhein, Gabriele M. Zu; Kanitz, C. L.; Gustafson, D. P.

doi:10.1126/science.172.3985.859

Cited by 50 publications

(18 citation statements)

References 7 publications

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“…Although contamination of feed with scrapie-infected sheep parts has been proposed as the cause of TME, the origin of the disease remains elusive. The idea that scrapie in sheep may be a source of TME infection is supported by findings that scrapie-infected mink have a similar distribution of vacuolar pathologic features in the brain and the same clinical signs as mink with natural and experimental TME ( 5 ). However, mink are not susceptible to scrapie infection following oral exposure for up to 4 years postinoculation, which suggests that either the scrapie agent may not be the source of natural TME infection or that only specific strains of the scrapie agent are able to induce TME ( 6 , 7 ) .…”

mentioning

confidence: 98%

Phenotypic Similarity of Transmissible Mink Encephalopathy in Cattle and L-type Bovine Spongiform Encephalopathy in a Mouse Model

Baron

Bencsik

Biacabe

et al. 2007

Emerg. Infect. Dis.

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mentioning

confidence: 98%

Phenotypic Similarity of Transmissible Mink Encephalopathy in Cattle and L-type Bovine Spongiform Encephalopathy in a Mouse Model

Baron

Bencsik

Biacabe

et al. 2007

Emerg. Infect. Dis.

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“…In the laboratory, the disease has been successfully transmitted to other animals, including mice (2), hamsters (3), mink (4), and, more recently, nonhuman primates (5). The unusual biophysical properties of the scrapie agent and the characteristic neurohistologic changes of scrapie are identical in certain respects with those of transmissible spongiform encephalopathies in humans, such as kuru (6), Creutzfeldt-Jakob disease (7), and some cases of Gerstmann-Straussler syndrome (8).…”

mentioning

confidence: 99%

Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent.

Locht¹,

Chesebro²,

Race³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

159

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The prion protein (PrP) is a scrapie-associated fibril protein that accumulates in the brains of hamsters and mice infected with the scrapie agent, and also in the brains of persons affected with kuru or Creutzfeldt-Jakob disease. It has been previously proposed that PrP could be either the primary transmissible agent of scrapie or a secondary component involved in the pathogenesis of scrapie. At present, the second possibility seems more likely, for the PrP-specific mRNA is present in both infected and uninfected brains. We have isolated and sequenced the complete PrP-specific cDNA from mRNA isolated from infected mouse brains. Comparison of the mouse PrP with the hamster PrP reveals a high homology in the amino acid sequence and the presence of a conserved octapeptide repeated four times, whose function is unknown at present. Structural features are discussed and compared with other proteins. Except for its homology with the hamster PrP, mouse PrP has no significant homology to any known protein sequence, including neurofilaments, neuropeptides, and amyloid proteins of Alzheimer disease. Some features of the PrP, however, are similar to structures found in aggregating proteins, such as the wheat glutenin, keratin, and collagen.

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“…TME was first described by and epidemiological studies indicated that the disease was a foodborne infection caused by an unidentified feed ingredient . Experimental attempts to transmit sheep scrapie to mink from sources in both the United States (Hanson et al, 1971) arid the United Kingdom have been inconsistent with the epidemiology of natural TME (Marsh & Hanson, 1979). In 1985, an outbreak of TME in Stetsonville, Wisconsin, U.S.A. was reported in which fallen dairy cattle were the major animal protein in mink feed (Marsh & Hartsough, 1985;Marsh & Hartsough, 1988;Marsh et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters

Bessen

Marsh

1992

Journal of General Virology

267

222

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Experimental transmission of the Stetsonville, Wisconsin, U.S.A. source of transmissible mink encephalopathy (TME) to outbred Syrian golden hamsters resulted in two distinct syndromes, termed hyper (HY) and drowsy (DY), that diverge by the third hamster passage. The syndromes differed with respect to clinical signs, incubation period, brain titre, brain lesion profile and pathogenicity in mink. HY hamster TME had an incubation period of 65 + 1 days and was characterized by clinical signs of hyperaesthesia and cerebeUar ataxia. Lethargy and the absence of hyperexcitability or cerebellar ataxia were representative of DY hamster TME which had an incubation period of 168 + 2 days. At endstage, HY and DY infected animals had brain titres of 109.5 LD5o/g and 10 TM LDso/g of tissue, respectively, indicating that the replication kinetics of these two strains is different. Hamster TME passaged back into mink revealed that only DY retained mink pathogenicity. This suggests that the DY agent is the major mink pathogen in the Stetsonville TME source that is also pathogenic in hamsters after a long incubation period. The HY agent is likely to be a minor component of the original TME mink brain that replicates more rapidly than DY agent in hamsters, but alone is non-pathogenic in mink. The presence of the HY and DY strains of agent that retain their biological characteristics on repeated hamster passage in the Stetsonville TME source requires that the informational molecule encoding these transmissible agents has the capacity to account for this biological diversity.

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Susceptibility of Mink to Sheep Scrapie

Cited by 50 publications

References 7 publications

Phenotypic Similarity of Transmissible Mink Encephalopathy in Cattle and L-type Bovine Spongiform Encephalopathy in a Mouse Model

Phenotypic Similarity of Transmissible Mink Encephalopathy in Cattle and L-type Bovine Spongiform Encephalopathy in a Mouse Model

Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent.

Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters

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