Biochemical and immunohistochemical characterization of feline spongiform encephalopathy in a German captive cheetah

Eiden, Martin; Hoffmann, Christine; Balkema‐Buschmann, Anne; Müller, Matthias; Baumgärtner, Katrin; Groschup, Martin H.

doi:10.1099/vir.0.022103-0

Cited by 34 publications

(26 citation statements)

References 37 publications

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“…Mice inoculated with brain homogenates from cats with FSE and cattle with BSE developed a TSE with similar profiles of neuropathological lesions and incubation periods. Strain typing studies in these mice also revealed a similarity between the FSE and BSE strains, supporting the hypothesis that FSE is caused by an infection with BSE prions [17,63,64]. However, in 1998, a domestic cat and his owner have been shown to be affected with a similar strain distinct from PrP BSE .…”

Section: Introductionsupporting

confidence: 67%

An overview of animal prion diseases

Imran

Mahmood

2011

Virol J

112

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Prion diseases are transmissible neurodegenerative conditions affecting human and a wide range of animal species. The pathogenesis of prion diseases is associated with the accumulation of aggregates of misfolded conformers of host-encoded cellular prion protein (PrPC). Animal prion diseases include scrapie of sheep and goats, bovine spongiform encephalopathy (BSE) or mad cow disease, transmissible mink encephalopathy, feline spongiform encephalopathy, exotic ungulate spongiform encephalopathy, chronic wasting disease of cervids and spongiform encephalopathy of primates. Although some cases of sporadic atypical scrapie and BSE have also been reported, animal prion diseases have basically occurred via the acquisition of infection from contaminated feed or via the exposure to contaminated environment. Scrapie and chronic wasting disease are naturally sustaining epidemics. The transmission of BSE to human has caused more than 200 cases of variant Cruetzfeldt-Jacob disease and has raised serious public health concerns. The present review discusses the epidemiology, clinical neuropathology, transmissibility and genetics of animal prion diseases.

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Section: Introductionsupporting

confidence: 67%

An overview of animal prion diseases

Imran

Mahmood

2011

Virol J

112

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“…Nonetheless, the use of BSE-contaminated meals to feed felids seems to be the most likely source of the disease since the majority of the FSE cases were reported in UK coinciding with the BSE epidemics. Moreover, similar neuropathological lesions and incubation periods were obtained in mice experimentally inoculated with brains of FSE or BSEinfected cats (Bencsik et al, 2009;Eiden et al, 2010). Nonetheless, in 1998 in Italy, a domestic cat and its owner were concurrently infected by a prion agent different from FSE or BSE.…”

Section: Feline Spongiform Encephalopathymentioning

confidence: 51%

“…Neurological alterations consist of spongiform degeneration of the neuropil in the gray matter of the brain and spinal cord, more intense in the medial geniculate nucleus of the thalamus and the basal nuclei (Sigurdson and Miller, 2003;Wyatt et al, 1991). In addition to CNS, PrP Sc florid plaques have been observed in peripheral nervous system, retina, lymphoreticular system, spleen, kidney and adrenal glands (Bencsik et al, 2009;Eiden et al, 2010;Lezmi et al, 2003;Ryder et al, 2001;Sigurdson and Miller, 2003) [http://www.cfsph.iastate.edu].…”

Section: Feline Spongiform Encephalopathymentioning

confidence: 97%

Prion and prion-like diseases in animals

Aguilar‐Calvo¹,

García²,

Espinosa³

et al. 2015

Virus Research

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“…Prions also adsorb to various minerals found in soil (14,20,27). Phosphotungstic acid has been used to precipitate PrP Sc in the laboratory (26) and may also be used to concentrate prions for PMCA detection (10). Superparamagnetic nanoparticles present a novel method for binding and concentrating PrP Sc , making use of specific and efficient capture.…”

Section: Discussionmentioning

confidence: 99%

Superparamagnetic Nanoparticle Capture of Prions for Amplification

Miller

Supattapone

2011

J Virol

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Prion diseases are associated with the presence of PrPSc , a disease-associated misfolded conformer of the prion protein. We report that superparamagnetic nanoparticles bind PrP Sc molecules efficiently and specifically, permitting magnetic separation of prions from a sample mixture. Captured PrP Sc molecules retain the activity to seed protein misfolding cyclic amplification (PMCA) reactions, enabling the rapid concentration of dilute prions to improve detection. Furthermore, superparamagnetic nanoparticles clear contaminated solutions of PrP Sc . Our findings suggest that coupling magnetic nanoparticle capture with PMCA could accelerate and improve prion detection. Magnetic nanoparticles may also be useful for developing a nontoxic prion decontamination method for biologically derived products.Bovine spongiform encephalopathy, Creutzfeldt-Jakob disease, and other prion diseases are caused by an infectious agent that contains PrP Sc , a misfolded conformer of the normal cellular prion protein (PrP C ) (24). Low-abundance sources of prions, such as blood, may still transmit disease (17,23). Prion diseases currently have no therapy, nor can prions be specifically removed from contaminated material.Inoculation bioassay serves as the gold standard for specific detection of prion infectivity. For sensitive detection, protein misfolding cyclic amplification (PMCA) has emerged as a rapid alternative to bioassay. PMCA exploits prion multiplication mechanisms to amplify PrP Sc in vitro using PrP C substrate (1, 5). Analogous to amplification of DNA sequence template by PCR, PrP Sc template seeds the conversion of PrP C substrate in PMCA, resulting in propagation and amplification of the PrP Sc conformation. Each serial PMCA round increases the detection sensitivity exponentially but requires ϳ72 h (7). The application of PMCA is also limited by prion propagation inhibitors present in blood and other biological solutions (6). An effective method to concentrate prions would improve subsequent PMCA sensitivity and utility.Nanotechnology presents many opportunities for fine control of molecular events. Certain iron oxide crystals less than ϳ25 nm in diameter exhibit superparamagnetism, with a net magnetization only occurring in the presence of an external magnetic field (15). MagnaBind and Dynal superparamagnetic beads contain many iron oxide crystals, dispersed such that no permanent magnetic order can form. This enables the whole particles to be superparamagnetic, allowing them to be rapidly attracted to a magnet and to lose magnetic interactions upon removal of the magnet (28). In molecular biology, superparamagnetic beads are often conjugated to specifically bind a target molecule.Using superparamagnetic nanoparticles, we have identified a novel binding interaction with PrPSc . Magnetic capture of PrP Sc may be applied to prion detection and prion decontamination. MATERIALS AND METHODSPreparation of scrapie-infected and uninfected brain homogenate. CD-1 mouse (prion strains RML, Me7, and 301C) and Syrian hamster (prion ...

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Biochemical and immunohistochemical characterization of feline spongiform encephalopathy in a German captive cheetah

Cited by 34 publications

References 37 publications

An overview of animal prion diseases

An overview of animal prion diseases

Prion and prion-like diseases in animals

Superparamagnetic Nanoparticle Capture of Prions for Amplification

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