Differentiation of ruminant transmissible spongiform encephalopathy isolate types, including bovine spongiform encephalopathy and CH1641 scrapie

Jacobs, J.G.; Sauer, Maurice J.; Keulen, L.J.M. van; Tang, Yue; Bossers, Alex; Langeveld, J.P.M.

doi:10.1099/vir.0.026153-0

Cited by 24 publications

(44 citation statements)

References 53 publications

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“…For antigen retrieval, 4 mm tissue sections were immersed in formic acid for 5 min at 20 uC followed by autoclaving in 0.2 % citrate retrieval solution (pH 6.8) at 121 uC for 30 min. After washing in tap water and quenching in hydrogen peroxide (3 % in methanol) for 20 min, tissue sections were blocked with the MOM kit liquid protein concentrate solution (Vector Laboratories) at a dilution of 1 : 20 for 60 min and incubated overnight at 23 uC with 1 mg 2G11 ml 21 (Novus Biologicals) or 0.2 mg SAF84 ml 21 (SPI Bio), which are both mouse mAbs recognizing aa 153-158 (Thuring et al, 2004) and aa 166-172 (Jacobs et al, 2011) of ovine PrP, respectively. The subsequent steps of the IHC procedure were performed using an immunoperoxidase Elite ABC kit (Vector Laboratories).…”

Section: Methodsmentioning

confidence: 99%

Archival search for historical atypical scrapie in sheep reveals evidence for mixed infections

Chong

Kennedy

Goldmann

et al. 2015

Journal of General Virology

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Section: Methodsmentioning

confidence: 99%

Archival search for historical atypical scrapie in sheep reveals evidence for mixed infections

Chong

Kennedy

Goldmann

et al. 2015

Journal of General Virology

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“…SAF84 detection was carried out with a Zenon labeling Alexa 488 kit, and L42 or Sha31 was detected with a Zenon labeling Alexa 647 kit (see above for kit specifications). The VRQ-PrP and ARQ-PrP fractions in PrP res samples were calculated as follows (33,38,39). When the SAF84/L42 antibody combination was used, the fraction of the 171Q-PrP product [Fr(171Q-PrP); the VRQ-or ARQ-PrP levels] in scrapie or BSE was obtained by applying the formula Fr(171Q-PrP) ϭ ratio x /ratio Q/Q , where ratio x is the SAF84/L42 ratio of an unknown sample, and ratio Q/Q is the SAF84/L42 ratio determined for Q/Q homozygous material, which is the average of measurements of the different scrapie (n ϭ 10) or BSE (n ϭ 8) Q/Q samples; the fraction of the 171R-PrP product (the ARR-PrP level) could be de- duced from the formula (ratio Q/Q Ϫ ratio x )/ratio Q/Q .…”

Section: Methodsmentioning

confidence: 99%

“…PrP res was prepared from 10% (wt/ vol) brain stem homogenates prepared in lysis buffer, digested with PK at 37°C, and further partially purified by precipitation with 1-propanol as described previously (38). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of denatured samples in loading buffer (with lithium-dodecyl sulfate and ␤-mercaptoethanol) was performed in 17-well gels (33).…”

Section: Methodsmentioning

confidence: 99%

“…Immunochemical quantification of PrP res was subsequently performed by fluorimetric detection monitored in a three-laser-beam imager (Typhoon Trio variable-mode imager; Amersham Biosciences) (38). For estimation of the ARR-and VRQ-PrP fractions in PrP res , a mixture of two antibodies was applied, one of which (SAF84) binds only if the 171Q polymorphism is present (VRQ-PrP or ARQ-PrP) while the other binds equally well to VRQ-, ARQ-, and ARR-PrP (33,38,39). Two different mixtures with SAF84 were used: SAF84 with L42 (L42/SAF84 combination) and SAF84 with Sha31 (Sha31/SAF84 combination).…”

Section: Methodsmentioning

confidence: 99%

“…This was accomplished by comparing brain PrP res in scrapie-and BSE-infected ARR/VRQ sheep. A previously developed robust triplex Western blotting (WB) method (38,39) was used to quantitatively estimate PrP concentrations. In this technique the Q171-PrP fraction (VRQ and ARQ) can be quantitatively estimated using a mixture of two antibodies on the same blot membrane, with one antibody (SAF84) recognizing only the VRQ fraction while the other binds equally well both VRQ-PrP and ARR-PrP.…”

mentioning

confidence: 99%

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Prion Type-Dependent Deposition of PRNP Allelic Products in Heterozygous Sheep

Langeveld

Jacobs

Hunter

et al. 2016

J Virol

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Susceptibility or resistance to prion infection in humans and animals depends on single prion protein (PrP) amino acid substitutions in the host, but the agent's modulating role has not been well investigated. Compared to disease incubation times in wild-type homozygous ARQ/ARQ (where each triplet represents the amino acids at codons 136, 154, and 171, respectively) sheep, scrapie susceptibility is reduced to near resistance in ARR/ARR animals while it is strongly enhanced in VRQ/VRQ carriers. Heterozygous ARR/VRQ animals exhibit delayed incubation periods. In bovine spongiform encephalopathy (BSE) infection, the polymorphism effect is quite different although the ARR allotype remains the least susceptible. In this study, T ransmissible spongiform encephalopathies (TSEs), or prion diseases, are fatal neurological diseases occurring in some mammalian species, including humans. The TSE agent or prion is characterized by the pivotal role of the host prion protein (PrP) that in disease appears aggregated and structurally abnormal and is named PrP Sc , where "Sc" refers to scrapie in small ruminants, which was recognized in the 18th century in Spanish Merino sheep (1). In healthy situations PrP is a cellular membrane protein (PrP C ) and fully susceptible to proteases, while its PrP Sc isoform is partially resistant to digestion with proteinase K (PK), usually leading to an N-terminally shortened protein called PrP res that still retains the associated infectivity (2-4).From many studies it is obvious that TSEs occur in distinct phenotypic forms that are recognized as TSE or prion disease types, such as classical scrapie in sheep and goat, Creutzfeldt-Jakob disease in humans, chronic wasting disease in cervids, and bovine spongiform encephalopathy (BSE) in cattle (5-15). In the experimental situation, these types can be considered strains when they are subpassaged to homogeneity in rodent bioassays (16)(17)(18)(19)(20). Susceptibility (and resistance) to animal and human prion diseases, either under infectious or spontaneous conditions, is dependent on single amino acid substitutions in the host's PrP sequence. In most species such substitutions are naturally occurring polymorphisms (7,10,(21)(22)(23)(24).In sheep two PrP polymorphisms in the PrP sequence, V 136 and R 171 (where V is valine and R is arginine, according to the singleletter code used by the IUPAC-IUB Joint Commission on Biochemical Nomenclature), provide, respectively, high and very low susceptibilities to natural scrapie compared to the homozygous

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Animal Prion Diseases

Windl

Dawson

2012

Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease

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Prion diseases occur in many animal species, most notably in ruminants. While scrapie in sheep has been recognised for three centuries and goat scrapie has been recognised for decades, BSE in cattle is a relatively novel disease which was first diagnosed in the UK in the mid 1980s. BSE was most likely caused through dietary exposure to animal feed contaminated with prions and disease was subsequently transmitted to people. The BSE epidemic is almost at an end, but the recent identification of so called atypical forms of BSE and scrapie pose many questions about the possible spectrum of prion diseases in animals and their transmissibility to other species, including humans.The pathogenesis of animal prion diseases has been studied both in natural infections and in experimental animal models. Detection of infectivity is greatly helped by suitable rodent models, in particular transgenic mice. Clinically infected animals show characteristic neuropathology in the brain and spinal cord which is accompanied by the accumulation of a conformationally altered, protease-resistant host protein. The post-mortem diagnosis is based on the detection of this protein, PrP(Sc), but despite recent impressive developments a routine ante-mortem diagnostic test has proved elusive.There is no treatment for prion diseases in animals, but disease outbreaks are controlled through a mixture of movement restrictions on holdings, culling of affected animals and herds and, for classical scrapie in sheep, selective breeding for genetic resistance. Prions are very stable and can remain in the environment for prolonged periods. This poses serious practical questions with regard to the decontamination of infected premises. The control of BSE specifically through restrictions in animal feeding practises has been successful, but the changing spectrum of these diseases plus the economic pressures to relax feed bans and reduce levels of surveillance will require constant vigilance to safeguard animal and public health.

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Differentiation of ruminant transmissible spongiform encephalopathy isolate types, including bovine spongiform encephalopathy and CH1641 scrapie

Cited by 24 publications

References 53 publications

Archival search for historical atypical scrapie in sheep reveals evidence for mixed infections

Archival search for historical atypical scrapie in sheep reveals evidence for mixed infections

Prion Type-Dependent Deposition of PRNP Allelic Products in Heterozygous Sheep

Animal Prion Diseases

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