Naturally occurring scrapie-like spongiform encephalopathy in five domestic cats

Wyatt, J. M.; Pearson, G. R.; Smerdon, TN; Gruffydd-Jones, TJ; Wells, G.; Wilesmith, J. W.

doi:10.1136/vr.129.11.233

Cited by 145 publications

(94 citation statements)

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“…13 Similar diseases have been described in many other species, including mink, 19 deer, 36 elk, 37 cattle, 35 cats, 38 zoo ruminants, 7 and humans. 3 The primary tissue affected is the central nervous system, resulting in a variety of clinical neurologic signs.…”

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confidence: 67%

Immunohistochemical Detection of Prion Protein in Sheep with Scrapie

et al. 1993

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Abstract. Prion protein (PrP), which is involved in the pathogenesis of scrapie, occurs in 2 forms. The form extracted from scrapie brain is protease resistant (PrP-res), whereas PrP from normal brain is protease sensitive (PrP-sen). This study examined whether PrP-res could be detected in brains of sheep with scrapie by immunohistochemistry (IHC). A suitable IHC procedure was developed using brain tissue from hamsters that had been inoculated with the transmissible mink encephalopathy agent. Tissue samples were fixed in PLP (periodate, lysine, paraformaldehyde) that contained paraformaldehyde at a concentration of 0.125%. Before application of the IHC technique, tissue sections were deparaffinized and treated with formic acid to simultaneously enhance PrP-res immunoreactivity and degrade PrP-sen. Primary antibody was obtained from a rabbit immunized to PrP-res extracted from brains of mice with experimentally induced scrapie. Brains from 21 sheep with histopathologically confirmed scrapie were examined by IHC. In all 21 brains, PrP-res was widely distributed throughout the brain stem. Staining was particularly intense in neuronal cell bodies and around blood vessels. The IHC technique successfully detected PrP-res in brain samples that had been frozen or that were severely autolyzed before fixation in PLP. Brains from 11 scrapie-suspect sheep that were not considered histologically positive were also examined by IHC. PrP-res was found in 4 of these brains. Sections of brains from 14 clinically normal sheep did not have detectable PrP-res. Results of this study indicate that IHC detection of PrP-res is equivalent, and perhaps superior, to histopathology for the diagnosis of scrapie in sheep. Furthermore, IHC is applicable to tissues that have autolytic changes or processing artifacts that prevent satisfactory histopathologic evaluation for lesions of scrapie.

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confidence: 67%

Immunohistochemical Detection of Prion Protein in Sheep with Scrapie

et al. 1993

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“…D. Foster, personal communication;Barlow & Middleton, 1990;Fraser et al, 1988). Very similar naturally occurring encephalopathies have been described in mink (Hartsough & Burger, 1965;Marsh et al, 1991), mule deer and Rocky Mountain elk (Williams & Young, 1980 in the U.S.A., and in a nyala (Jeffrey & Wells, 1988), an oryx, a kudu (Kirkwood et al, 1990) and the domestic cat (Wyatt et al, 1991) more recently in the U.K.…”

Section: Introductionmentioning

confidence: 84%

“…It became epidemic in the British Isles following the first recognized cases in 1985 (Wells et al, 1987) and by November 1991 over 30000 cases had been reported (Wilesmith et al, 1991 ;personal communication). It is experimentally transmissible to cattle, pigs, sheep and goats, and to laboratory mice (Dawson et al, 1990(Dawson et al, , 1991J.…”

Section: Introductionmentioning

confidence: 99%

Transmission of bovine spongiform encephalopathy and scrapie to mice

Fraser

Bruce²,

Chree³

et al. 1992

Journal of General Virology

180

133

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Transmission from four cases of bovine spongiform encephalopathy (BSE) to mice resulted in neurological disease in 100% of recipient animals, after incubation periods of between 265 and 700 days post-injection. The results from the four cases were very similar to one another. There were major differences in the incubation period between the four inbred strains of mice tested, and even between strains of the same Sinc genotype, and the incubation periods of Sinc heterozygote mice were much longer than those for any of the inbred strains. Transmission from a case of natural scrapie differed in two important respects: there were no differences in the incubation period between mouse strains of the same Sinc genotype, and that of the heterozygotes was between those of the Sinc homozygotic parental strains. The distribution of vacuolar degeneration in the brains of mice infected with scrapie also differed from those infected with the BSE isolates. Transmission was also achieved from formol-fixed BSE brain. These results show that the same strain of agent caused disease in the BSE cases, and that the relationship of BSE to scrapie in sheep is unclear.

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“…Surprisingly, BSE prions affect a wide range of host species. In nature, BSE is transmitted to cattle (Wells & Wilesmith, 1995), several zoo ruminants (Kirkwood & Cunningham, 1994) and wild and domestic cats (Wyatt et al, 1990(Wyatt et al, , 1991. Experimentally, BSE has been transmitted to mice (Fraser et al, 1992), sheep, goats , minks (Robinson et al, 1994), marmosets (Baker et al, 1998), macaques (Lasmézas et al, 1996) and lemurs (Bons et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Alteration of the biological and biochemical characteristics of bovine spongiform encephalopathy prions during interspecies transmission in transgenic mice models

Yokoyama

Masujin

Iwamaru

et al. 2009

Journal of General Virology

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In the interspecies transmission of prions, the species barrier influences the susceptibility of the host. Bovine spongiform encephalopathy (BSE) prions affect a wide range of host species but do not affect hamsters. In order to study this species barrier, this study analysed the transmissibility of BSE prions to several lines of transgenic (Tg) mice, including those expressing mouse and hamster chimeric prion proteins (MH2M and MHM2 mice). BSE prions were transmitted to tga20, MHM2 and ICR mice, and the incubation period was approximately 400 days. Thus, these mice were classified as 'susceptible mice'. However, BSE prions were not transmitted to MH2M and TgHaNSE mice, and these mice were classified as 'resistant mice'. After the BSE prions were passaged once in wild-type mice, they could be transmitted to resistant mice. The characteristics of the accumulated abnormal isoform of PrP (PrP Sc ) in susceptible and resistant mice were determined using Western blotting. A BSE-like glycoform pattern of PrP Sc was detected in all of the susceptible mice using two different antibodies that recognized either the N-or the C-terminal end of the 27-30 kDa protease-resistant fragment of PrP (PrP 27-30 ) as the epitope. In contrast, proteinase digestion followed by deglycosylation analysis showed that, in addition to PrP 27-30 , truncated PrP Sc fragments existed in resistant mice. These mixed PrP Sc fragments may have resulted from the adaptation of resistant mice to BSE prions.

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Naturally occurring scrapie-like spongiform encephalopathy in five domestic cats

Cited by 145 publications

References 0 publications

Immunohistochemical Detection of Prion Protein in Sheep with Scrapie

Immunohistochemical Detection of Prion Protein in Sheep with Scrapie

Transmission of bovine spongiform encephalopathy and scrapie to mice

Alteration of the biological and biochemical characteristics of bovine spongiform encephalopathy prions during interspecies transmission in transgenic mice models

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