Experimental transmission of BSE and scrapie to the common marmoset

Baker, H.F.; Ridley, R. M.; Wells, G.

doi:10.1136/vr.132.16.403

Cited by 81 publications

(38 citation statements)

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“…There was minimal involvement of the cerebellum. In addition Discussion BSE has been transmitted experimentally to mice, cattle, pigs, sheep, goats and marmosets (Baker et al, 1993;Barlow & Middleton, 1990;Dawson et al, 1990a, b;Fraser et al, 1988). The present study extends the experimental host range to mink.…”

Section: M Robinson and Othersmentioning

confidence: 69%

Experimental infection of mink with bovine spongiform encephalopathy

Robinson

Hadlow²,

Huff

et al. 1994

Journal of General Virology

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Section: M Robinson and Othersmentioning

confidence: 69%

Experimental infection of mink with bovine spongiform encephalopathy

Robinson

Hadlow²,

Huff

et al. 1994

Journal of General Virology

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“…BSE has been transmitted experimentally by parenteral routes from cattle to mice (Fraser et al, 1988(Fraser et al, , 1992, cattle (Dawson et al, 1990a), sheep and goats (Foster et al, 1993;Fraser & Foster, 1994), mink (Mustela vison) (Robinson et al, 1994), marmoset (Callithrix jacchus) (Baker et al, 1993), cynomolgus macaque (Lasmézas et al, 1996) and guinea pig (M. Dawson, P. Griffiths & S. J. Ryder, unpublished data). The present study shows that BSE is transmissible from cattle to pigs that were exposed parenterally.…”

Section: Discussionmentioning

confidence: 99%

Studies of the transmissibility of the agent of bovine spongiform encephalopathy to pigs

Wells

Hawkins

Austin³

et al. 2003

Journal of General Virology

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Studies to test the transmissibility of the bovine spongiform encephalopathy (BSE) agent to pigs began in 1989. Parenteral inoculation of the agent by three routes simultaneously (intracranially, intravenously and intraperitoneally) produced disease with an incubation period range of 69-150 weeks. Pre-clinical pathological changes were detected in two pigs killed electively at 105 and 106 weeks post-inoculation. Infectivity was detected by bioassay in inbred mice in the CNS of those pigs that developed spongiform encephalopathy. Infectivity was also found in the stomach, jejunum, distal ileum and pancreas of terminally affected pigs. These findings show that pigs are susceptible to BSE. In contrast, disease failed to occur in pigs retained for 7 years after exposure by feeding BSE-affected brain on three separate days, at 1-2 week intervals. The amounts fed each day were equivalent to the maximum daily intake of meat and bone meal in rations for pigs aged 8 weeks. No infectivity was found in tissues assayed from the pigs exposed orally. This included tissues of the alimentary tract. It is suggested that these pigs did not become infected. The relatively high oral exposure used in these experiments compared with feed-borne exposure in the field may explain the absence of an epidemic of spongiform encephalopathy in domestic pigs concurrent with the BSE epidemic in the UK.

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“…These unusual neuropathologic changes have not been seen in CJD cases in the United States, Australia, or Japan (307,309). Both macaque monkeys and marmosets developed neurologic disease several years after inoculation with bovine prions (310), but only the macaques exhibited numerous PrP plaques similar to those found in vCJD (311) (Table 5). Histoblot of PrP Sc deposition in a coronal section a Tg(MHu2M)Prnp 0/0 mouse through the hippocampus and thalamus (27).…”

mentioning

confidence: 99%

Molecular characterization of proteolytic cleavage sites of the Pseudomonas syringae effector AvrRpt2

Chisholm

Dahlbeck

Krishnamurthy

et al. 2005

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

137

138

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Prions are unprecedented infectious pathogens that cause a group of invariably fatal neurodegenerative diseases by an entirely novel mechanism. Prion diseases may present as genetic, infectious, or sporadic disorders, all of which involve modification of the prion protein (PrP). Bovine spongiform encephalopathy (BSE), scrapie of sheep, and Creutzfeldt-Jakob disease (CJD) of humans are among the most notable prion diseases. Prions are transmissible particles that are devoid of nucleic acid and seem to be composed exclusively of a modified protein (PrP Sc ). The normal, cellular PrP (PrP C ) is converted into PrP Sc through a posttranslational process during which it acquires a high ␤-sheet content. The species of a particular prion is encoded by the sequence of the chromosomal PrP gene of the mammals in which it last replicated. In contrast to pathogens carrying a nucleic acid genome, prions appear to encipher strain-specific properties in the tertiary structure of PrP Sc . Transgenetic studies argue that PrP Sc acts as a template upon which PrP C is refolded into a nascent PrP Sc molecule through a process facilitated by another protein. Miniprions generated in transgenic mice expressing PrP, in which nearly half of the residues were deleted, exhibit unique biological properties and should facilitate structural studies of PrP Sc . While knowledge about prions has profound implications for studies of the structural plasticity of proteins, investigations of prion diseases suggest that new strategies for the prevention and treatment of these disorders may also find application in the more common degenerative diseases.

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Experimental transmission of BSE and scrapie to the common marmoset

Cited by 81 publications

References 0 publications

Experimental infection of mink with bovine spongiform encephalopathy

Experimental infection of mink with bovine spongiform encephalopathy

Studies of the transmissibility of the agent of bovine spongiform encephalopathy to pigs

Molecular characterization of proteolytic cleavage sites of the Pseudomonas syringae effector AvrRpt2

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