The transmissible spongiform encephalopathies (TSE) don´t occur in swine in natural conditions. However, the bovine spongiform encephalopathy (BSE) agent, inoculated by 3 simultaneous routes in pigs, is able to reproduce a neurological disease in these animals. On the other hand, the BSE agent after passage in sheep under experimental conditions (sheep-BSE) exhibits altered pathobiologic properties. This new agent is able to cross the cattle-pig transmission barrier more efficiently than BSE..

Andreoletti, Olivier

Badiola, Juan José

Bolea, Rosa

Corbiere, Fabian

Filali, Hicham

Hedman, Carlos

Hernández, Rodrigo S.

Jiron, William

Marin, Belen

Moreno, Bernardino

Pitarch, Jose Luis

Pumarola, Martí

Vázquez, Francisco José

English

Repositorio Universidad de Zaragoza

This article was downloaded by: [138.102.135.242]On: 12 March 2015, At: 06:44Publisher: Taylor & FrancisInforma Ltd Registered in England and Wales Registered Number: 1072954 Registered office: Mortimer House,37-41 Mortimer Street, London W1T 3JH, UKClick for updatesPrionPublication details, including instructions for authors and subscription information:http://www.tandfonline.com/loi/kprn20Prion Diseases in AnimalsPublished online: 01 Apr 2014.To cite this article: (2014) Prion Diseases in Animals, Prion, 8:sup1, 59-109, DOI: 10.4161/pri.29370To link to this article:  http://dx.doi.org/10.4161/pri.29370PLEASE SCROLL DOWN FOR ARTICLETaylor & Francis makes every effort to ensure the accuracy of all the information (the “Content”) contained inthe publications on our platform. Taylor & Francis, our agents, and our licensors make no representations orwarranties whatsoever as to the accuracy, completeness, or suitability for any purpose of the Content. Versionsof published Taylor & Francis and Routledge Open articles and Taylor & Francis and Routledge Open Selectarticles posted to institutional or subject repositories or any other third-party website are without warrantyfrom Taylor & Francis of any kind, either expressed or implied, including, but not limited to, warranties ofmerchantability, fitness for a particular purpose, or non-infringement. Any opinions and views expressed in thisarticle are the opinions and views of the authors, and are not the views of or endorsed by Taylor & Francis. Theaccuracy of the Content should not be relied upon and should be independently verified with primary sourcesof information. Taylor & Francis shall not be liable for any losses, actions, claims, proceedings, demands,costs, expenses, damages, and other liabilities whatsoever or howsoever caused arising directly or indirectly inconnection with, in relation to or arising out of the use of the Content. This article may be used for research, teaching, and private study purposes. Terms & Conditions of access anduse can be found at http://www.tandfonline.com/page/terms-and-conditions It is essential that you check the license status of any given Open and Open Select article to confirmconditions of access and use.86 Prion Volume 8 Supplementcentral nervous system. Although multiple events, including ER stress caused by the accumulation of PrPSc aggregates, activated astrocytes and/or microglia or synaptic and dendritic alterations, have been suggested to be involved in neurodegeneration, its molecular mechanism is not fully understood yet. Neuronal cell lines used for analyses of the cellular mechanism of prion propa-gation have so far shown little cytopathic effect. Thus, a novel ex vivo experiment system, in which the generation of PrPSc in neurons and neurodegeneration can be reproduced, is required. Thus we analyzed prion infection in primary cortical neurons.Materials and Methods. Mouse primary cortical neurons were obtained from 15-day mouse embryo. Four different prion strains, 22L, Chandler, Obihiro, and BSE-KUS, were used. PrPSc-specific staining was carried out using mAb132.Results and Discussion. All the four prion strains could effectively produce PrPSc in primary cortical neurons, confirm-ing the prion infection. Interestingly, the shape of PrPSc-staining observed confocal microscopy differed with strains; string shape staining was pronounced in cortical neurons infected with 22L or Chandler strains, whereas granular staining was mainly observed in Obihiro and BSE-KUS strain infection. A slight decrease in cell viability and in the expression of synaptic proteins such as PSD95 and N-cadherin was observed; however, double stain-ing of PrPSc with tunnel-staining and cleaved caspase-3 did not reveal apoptosis of primary cortical neurons infected with prions. Efficient PrPSc generation in cortical neurons without neuronal cell death suggests that certain causes other than neurons, such as factors produced from activated astrocytes and/or microglia play a critical role in the neurodegeneration caused by prion infection. Analyses of neuron-glia interaction using prion-infected primary cortical neurons co-cultured with astrocytes or microglia may provide a clue to elucidate the neurodegenerative mechanisms of prion diseases.P.131: Transmission of sheep-bovine spongiform encephalopathy in pigsCarlos Hedman,1 Belén Marín,1 Fabian Corbière,3 Hicham Filali,1 Francisco Vázquez, José Luis Pitarch,1 William Jirón,1 rodrigo S Hernandez,1 Bernardino Moreno,1 Martí Pumarola,2 olivier Andréoletti,3 Juan José Badiola,1 and rosa Bolea11University of Zaragoza; Zaragoza, Spain; 2University of Barcelona; Barcelona, Spain; 3institut national de la recherche (inrA); Toulouse, FranceIntroduction. The transmissible spongiform encephalopa-thies (TSE) don t´ occur in swine in natural conditions. However, the bovine spongiform encephalopathy (BSE) agent, inoculated by 3 simultaneous routes in pigs, is able to reproduce a neurologi-cal disease in these animals. On the other hand, the BSE agent after passage in sheep under experimental conditions (sheep-BSE) exhibits altered pathobiologic properties. This new agent is able to cross the cattle-pig transmission barrier more efficiently than BSE. The potential propagation of TSE in animals from the human food chain, including pigs, needs to be assessed regarding the risk for human infection by animals other than TSE-infected ruminants. The aim of this work was to determine the suscepti-bility of pigs to the Sheep-BSE agent and describe the pathologi-cal findings and PrPSc deposition in different tissues.Material and Methods. Seven minipigs were challenged intra-cerebrally with sheep-BSE agent. Clinical observation and post-mortem histopathology, immunohistochemistry (antibody 2G11) and Western blotting were performed on central nervous system (CNS), peripheral nervous system (PNS) and other tissues.Results. One pig was culled in an early incubation stage, and remaining six were culled at the presence of clinical sings. Pigs developed a clinical disease with locomotor disorders in an aver-age time of 23 months post inoculation, showing clinical findings in most of them earlier than those described in the BSE in pigs experimental infection. TSE wasn t´ confirmed in the preclinical pig. In clinical pigs, the entire cerebral cortex showed severe neu-ropil vacuolation, extensive and severe vacuolar changes affecting the thalamus, hippocampus and cerebellum. PrPSc was found in CNS of all clinical pigs (6/6). Intracellular (intraneuronal and intraglial) and neuropil-associated PrPSc deposition was consis-tently observed in the brainstem, thalamus, and deeper layers of the cerebral cortex. Also, PrPSc was observed in PNS, mainly in the myenteric plexus and also in nerves belonging to the skeleton muscle. Moreover, the glycosylation profile showed a 3 band pat-tern with a predominant monoglycosylated band in positive pig samples. This features concern on the potential risk of utilization of meat and bound meal of small ruminants in feeding pigs.P.132: Full-length PrPC but not PrP-C1 is depleted  in autolytic brainstem samples of cattleFabienne Serra,1,2 Sandra McCutcheon,3 and Torsten Seuberlich11neuroCenter, Division of neurological Sciences; DCr-VPH, Vetsuisse Faculty; University of Berne; Berne, Switzerland; 2Graduate school for Cellular and Biomedical Sciences; University of Berne; Berne, Switzerland; 3neurobiology Division; The roslin institute and r(D)SVS; The University of Edinburgh; Edinburgh, UKIntroduction. In summers 2011 to 2013 in Switzerland, sev-eral brainstem samples from cattle in a severely autolytic stage were reactive with some of the BSE screening tests, but remained unconfirmed. In the Western immunoblot (WB), a truncated form of PrPres type was detected after proteinase K (PK) diges-tion, with a profile distinct from either H-, L- or C-BSE. In order to investigate whether this particular PrP profile was related to the effects of severe autolysis, we compared the PrP species pres-ent in these autolytic samples to those in non-autolytic BSE nega-tive samples and BSE positive samples.Material and methods. Fallen stock autolytic brainstem samples that were initially reactive in the screening laboratory were selected. Freshly prepared control brains were collected at the slaughterhouse. All samples were analyzed with and without PK digestion and deglycosylation respectively using standard Downloaded by [138.102.135.242] at 06:44 12 March 2015 

Transmission of sheep-bovine spongiform encephalopathy in pigs

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Transmission of sheep-bovine spongiform encephalopathy in pigs

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