A. Maheshwari, M. Fischer, P. Gambetti, A. Parker, A. Ram et al., Recent US Case of Variant Creutzfeldt-Jakob Disease???Global Implications, Emerging Infectious Diseases, vol.21, issue.5, pp.750-925897712, 2015.
DOI : 10.3201/eid2105.142017

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4412247

J. Wilesmith, G. Wells, M. Cranwell, and J. Ryan, Bovine spongiform encephalopathy: epidemiological studies on the origin, Veterinary Record, vol.128, issue.9, pp.638-443218047, 1988.
DOI : 10.1136/vr.128.9.199

A. Aguzzi and M. Polymenidou, Mammalian Prion Biology, Cell, vol.116, issue.2, pp.313-2714744440, 2004.
DOI : 10.1016/S0092-8674(03)01031-6

URL : http://doi.org/10.1016/s0092-8674(03)01031-6

. Anonymous, amending Annexes II, VII, VIII, IX and X to Regulation ( EC ) No 999/2001 of the European Parliament and of the Council laying down rules for the prevention, control and eradication of 176 J. R. Requena et al. certain transmissible spongiform encephalopathies, Off J Eur Union, vol.308, pp.66-79, 1148.

J. Collinge, J. Whitfield, E. Mckintosh, A. Frosh, S. Mead et al., A clinical study of kuru patients with long incubation periods at the end of the epidemic in Papua New Guinea, Philosophical Transactions of the Royal Society B: Biological Sciences, vol.3, issue.9552, pp.3725-3918849289, 2008.
DOI : 10.1016/S0140-6736(06)69835-8

M. Bishop, A. Diack, D. Ritchie, J. Ironside, R. Will et al., Prion infectivity in the spleen of a PRNP heterozygous individual with subclinical variant Creutzfeldt???Jakob disease, Brain, vol.136, issue.4, pp.1139-4523449776, 2013.
DOI : 10.1093/brain/awt032

A. Peden, M. Head, D. Ritchie, J. Bell, and J. Ironside, Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient, The Lancet, vol.364, issue.9433, pp.527-915302196, 2004.
DOI : 10.1016/S0140-6736(04)16811-6

O. Gill, Y. Spencer, A. Richard-loendt, C. Kelly, R. Dabaghian et al., Prevalent abnormal prion protein in human appendixes after bovine spongiform encephalopathy epizootic: large scale survey, BMJ, vol.347, issue.oct15 5, p.567524129059, 2013.
DOI : 10.1136/bmj.f5675

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3805509

J. Douet, S. Zafar, A. Perret-liaudet, C. Lacroux, S. Lugan et al., Detection of Infectivity in Blood of Persons with Variant and Sporadic Creutzfeldt-Jakob Disease, Emerging Infectious Diseases, vol.20, issue.1, pp.114-724377668, 2014.
DOI : 10.3201/eid2001.130353

F. Houston, S. Mccutcheon, W. Goldmann, A. Chong, J. Foster et al., Prion diseases are efficiently transmitted by blood transfusion in sheep, Blood, vol.112, issue.12, pp.4739-4518647958, 2008.
DOI : 10.1182/blood-2008-04-152520

C. Llewelyn, P. Hewitt, R. Knight, K. Amar, S. Cousens et al., Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion, The Lancet, vol.363, issue.9407, pp.417-2114962520, 2004.
DOI : 10.1016/S0140-6736(04)15486-X

T. Konold, G. Bone, A. Vidal-diez, R. Tortosa, A. Davis et al., Pruritus is a common feature in sheep infected with the BSE agent, BMC Veterinary Research, vol.4, issue.1, pp.4-6, 2008.
DOI : 10.1186/1746-6148-4-16

M. Tranulis, S. Benestad, T. Baron, and H. Kretzschmar, Atypical Prion Diseases in Humans and Animals, Top Curr Chem, vol.305, pp.23-5021598097, 2011.
DOI : 10.1007/128_2011_161

S. Prusiner and . Prions, Nobel Lecture: Prions, Proceedings of the National Academy of Sciences, vol.389, issue.6650, pp.13363-839811807, 1998.
DOI : 10.1038/39097

A. Aguzzi and A. Calella, Prions: Protein Aggregation and Infectious Diseases, Physiological Reviews, vol.89, issue.4, pp.1105-52, 2009.
DOI : 10.1152/physrev.00006.2009

H. Wille, W. Bian, M. Mcdonald, A. Kendall, D. Colby et al., Natural and synthetic prion structure from X-ray fiber diffraction, Proceedings of the National Academy of Sciences, vol.18, issue.24, pp.16990-16995, 2009.
DOI : 10.1074/jbc.M111402200

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2761340

V. Azquez-fern-andez, E. Vos, M. Cebey, L. , R. L. Sevillano et al., Recent advances towards an understanding of the structure of PrPSc, Prion, vol.8, p.6, 2014.

V. Azquez-fern-andez, E. Alonso, J. Pastrana, M. Ramos, A. Stitz et al., Structural Organization of Mammalian Prions as Probed by Limited Proteolysis, PLoS One, vol.7, issue.11e50111, 2012.

J. D. Richardson and . Richardson, Natural ??-sheet proteins use negative design to avoid edge-to-edge aggregation, Proceedings of the National Academy of Sciences, vol.268, issue.4, pp.2754-2763, 2002.
DOI : 10.1006/jmbi.1994.1691

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC122420

A. Bryan, . Jr, J. Starner-kreinbrink, R. Hosur, P. Clark et al., Structure-based prediction reveals capping motifs that inhibit ??-helix aggregation, Proceedings of the National Academy of Sciences, vol.16, issue.4, pp.11099-104, 2011.
DOI : 10.1093/bioinformatics/16.4.404

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3131356

G. Giachin, I. Biljan, G. Ilc, J. Plavec, and G. Legname, Probing Early Misfolding Events in Prion Protein Mutants by NMR Spectroscopy, Molecules, vol.103, issue.8, pp.9451-76, 2013.
DOI : 10.1006/jmbi.2001.5322

URL : http://doi.org/10.3390/molecules18089451

K. Ashe and A. Aguzzi, Prions, prionoids and pathogenic proteins in Alzheimer disease, Prion, vol.17, issue.1, pp.55-64, 2013.
DOI : 10.1038/379339a0

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3609051

M. Jucker and L. Walker, Self-propagation of pathogenic protein aggregates in neurodegenerative diseases, Nature, vol.6, issue.7465, pp.45-51, 2013.
DOI : 10.1038/nature12481

E. Vidal, F. Borges, N. Pintado, B. Ord-o~-nez, M. et al., Exploring the risks of a putative transmission of BSE to new species, Prion, vol.156, issue.6, pp.443-449, 2013.
DOI : 10.1099/vir.0.004754-0

E. Allard, M. Grujic, G. Fisone, and K. Kristensson, Prion formation correlates with activation of translation-regulating protein 4E-BP and neuronal transcription factor Elk1, Neurobiology of Disease, vol.58, pp.116-138, 2013.
DOI : 10.1016/j.nbd.2013.05.014

A. Rouvinski, S. Karniely, M. Kounin, S. Moussa, M. Goldberg et al., in cell-surface, raft-associated amyloid strings and webs, The Journal of Cell Biology, vol.72, issue.3, pp.423-464, 2014.
DOI : 10.1083/jcb.201308028.dv

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3912534

S. Godsave, H. Wille, J. Pierson, S. Prusiner, and P. Peters, Plasma membrane invaginations containing clusters of full-length PrPSc are an early form of prion-associated neuropathology in??vivo, Neurobiology of Aging, vol.34, issue.6, pp.1621-1631, 2013.
DOI : 10.1016/j.neurobiolaging.2012.12.015

Z. Marijanovic, A. Caputo, V. Campana, and C. Zurzolo, Identification of an Intracellular Site of Prion Conversion, PLoS Pathogens, vol.38, issue.4, 2009.
DOI : 10.1371/journal.ppat.1000426.s009

URL : https://hal.archives-ouvertes.fr/pasteur-00396879

K. Gousset, E. Schiff, C. Langevin, Z. Marijanovic, A. Caputo et al., Prions hijack tunnelling nanotubes for intercellular spread, Nature Cell Biology, vol.177, issue.3, pp.328-364, 2009.
DOI : 10.1038/nprot.2006.356

URL : https://hal.archives-ouvertes.fr/pasteur-00368712

L. Marzo, K. Gousset, and C. Zurzolo, Multifaceted Roles of Tunneling Nanotubes in Intercellular Communication, Frontiers in Physiology, vol.3, p.7222514537, 2012.
DOI : 10.3389/fphys.2012.00072

URL : https://hal.archives-ouvertes.fr/pasteur-00716379

D. Gavier-wid-en, M. Stack, T. Baron, A. Balachandran, and M. Simmons, Diagnosis of Transmissible Spongiform Encephalopathies in Animals: A Review, Journal of Veterinary Diagnostic Investigation, vol.101, issue.6, pp.509-536, 2005.
DOI : 10.1136/vr.129.11.233

C. Orr-u, J. Wilham, L. Raymond, F. Kuhn, B. Schroeder et al., Prion Disease Blood Test Using Immunoprecipitation and Improved Quaking-Induced Conversion, mBio, vol.2, issue.3, pp.78-1121558432, 2011.
DOI : 10.1128/mBio.00078-11

M. Cramm, M. Schmitz, A. Karch, E. Mitrova, F. Kuhn et al., Stability and Reproducibility Underscore Utility of RT-QuIC for Diagnosis of Creutzfeldt-Jakob Disease, Molecular Neurobiology, vol.51, issue.3, pp.1896-90425823511, 2016.
DOI : 10.1007/s12035-015-9133-2

P. Brown and D. Gajdusek, Survival of scrapie virus after 3 years' interment, The Lancet, vol.337, issue.8736, pp.269-701671114, 1991.
DOI : 10.1016/0140-6736(91)90873-N

B. Maddison, J. Owen, K. Bishop, H. Rees, G. Shaw et al., with Soils Is Influenced by Prion Source and Soil Type, Environmental Science & Technology, vol.44, issue.22, pp.8503-820968294, 2010.
DOI : 10.1021/es101591a

L. Terry, L. Howells, K. Bishop, C. Baker, S. Everest et al., Detection of prions in the faeces of sheep naturally infected with classical scrapie, Veterinary Research, vol.42, issue.1, p.6521592355, 2011.
DOI : 10.1016/j.rvsc.2003.11.007

B. Seidel, A. Thomzig, A. Buschmann, M. Groschup, R. Peters et al., Scrapie Agent (Strain 263K) Can Transmit Disease via the Oral Route after Persistence in Soil over Years, PLoS ONE, vol.279, issue.5, p.43517502917, 2007.
DOI : 10.1371/journal.pone.0000435.t002

C. Maluquer-de-motes, J. Espinosa, A. Esteban, M. Calvo, R. Girones et al., Persistence of the bovine spongiform encephalopathy infectious agent in sewage, Prion stability and infectivity in the environment, pp.1-722776326158, 2009.
DOI : 10.1016/j.envres.2012.06.010

N. Mabbott, Prion pathogenesis and secondary lymphoid organs (SLO), Prion, vol.13, issue.4, pp.322-3322895090, 2012.
DOI : 10.1371/journal.ppat.1001257

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3609058

A. Aguzzi, M. Nuvolone, and C. Zhu, The Immunobiology of Prion Diseases, Transfusion Alternatives in Transfusion Medicine, vol.390, issue.s2, pp.888-90224189576, 2013.
DOI : 10.1126/science.1063093

N. Mabbott, F. Mackay, F. Minns, and M. Bruce, Temporary inactivation of follicular dendritic cells delays neuroinvasion of scrapie, Nature Medicine, vol.6, issue.7, pp.719-2010888894, 2000.
DOI : 10.1038/77401

F. Montrasio, R. Frigg, M. Glatzel, M. Klein, F. Mackay et al., Impaired Prion Replication in Spleens of Mice Lacking Functional Follicular Dendritic Cells, Science, vol.288, issue.5469, pp.1257-910818004, 2000.
DOI : 10.1126/science.288.5469.1257

N. Mabbott, Prospects for safe and effective vaccines against prion diseases, Expert Review of Vaccines, vol.14, issue.1, pp.1-4, 2015.
DOI : 10.1586/14760584.2015.965691

M. Eloit, K. Adjou, M. Coulpier, J. Fontaine, R. Hamel et al., BSE agent signatures in a goat, Veterinary Record, vol.156, issue.16, pp.523-527, 2005.
DOI : 10.1136/vr.156.16.523-b

J. Spiropoulos, R. Lockey, R. Sallis, L. Terry, L. Thorne et al., Isolation of Prion with BSE Properties from Farmed Goat, Emerging Infectious Diseases, vol.17, issue.12, pp.2253-61, 2011.
DOI : 10.3201/eid1712.110333

L. Mcculloch, K. Brown, and N. Mabbott, , specifically on follicular dendritic cells has no effect on their maturation or function, Immunology, vol.207, issue.3, pp.246-57, 2013.
DOI : 10.1111/imm.12031

M. Prinz, G. Huber, A. Macpherson, F. Heppner, M. Glatzel et al., Oral Prion Infection Requires Normal Numbers of Peyer's Patches but Not of Enteric Lymphocytes, The American Journal of Pathology, vol.162, issue.4, pp.1103-1114, 2003.
DOI : 10.1016/S0002-9440(10)63907-7

D. Donaldson, K. Else, and N. Mabbott, ABSTRACT, Journal of Virology, vol.89, issue.18, pp.9532-9579, 2015.
DOI : 10.1128/JVI.01544-15

M. Klein, P. Kaeser, P. Schwarz, H. Weyd, I. Xenarios et al., Complement facilitates early prion pathogenesis, Nature Medicine, vol.7, issue.4, pp.488-92, 2001.
DOI : 10.1038/86567

N. Mabbott, M. Bruce, M. Botto, M. Walport, and M. Pepys, Temporary depletion of complement component 178, J. R. Requena et al

B. Michel, A. Ferguson, T. Johnson, H. Bender, C. Meyerett-reid et al., Genetic Depletion of Complement Receptors CD21/35 Prevents Terminal Prion Disease in a Mouse Model of Chronic Wasting Disease, The Journal of Immunology, vol.189, issue.9, pp.4520-4527, 2012.
DOI : 10.4049/jimmunol.1201579

O. Connor, T. Frei, N. Sponarova, J. Schwarz, P. Heikenwalder et al., Lymphotxin, but not TNF, is required for prion invasion of lymph nodes, PLoS Pathog, vol.8, 2012.

P. Kujala, C. Raymond, M. Romeijn, S. Godsave, S. Van-kasteren et al., Prion Uptake in the Gut: Identification of the First Uptake and Replication Sites, PLoS Pathogens, vol.24, issue.12, 2011.
DOI : 10.1371/journal.ppat.1002449.s013

M. Prinz, M. Heikenwalder, T. Junt, P. Schwarz, M. Glatzel et al., Positioning of follicular dendritic cells within the spleen controls prion neuroinvasion, Nature, vol.425, issue.6961, pp.957-62, 2003.
DOI : 10.1038/nature02072

C. Langevin, K. Gousset, M. Costanzo, R. Goff, O. Zurzolo et al., Characterization of the role of dendritic cells in prion transfer to primary neurons, Biochemical Journal, vol.71, issue.2, pp.189-98, 2010.
DOI : 10.1016/j.febslet.2009.03.065

URL : https://hal.archives-ouvertes.fr/hal-00521557

M. Klein, R. Frigg, E. Flechsig, A. Raeber, U. Kalinke et al., A crucial role for B cells in neuroinvasive scrapie, Nature, vol.390, pp.687-919414161, 1997.

M. Heikenwalder, N. Zeller, H. Seeger, M. Prinz, P. Kl?-ohn et al., Chronic Lymphocytic Inflammation Specifies the Organ Tropism of Prions, Science, vol.307, issue.5712, pp.1107-1117, 2005.
DOI : 10.1126/science.1106460

H. Seeger, M. Heikenwalder, N. Zeller, J. Kranich, P. Schwarz et al., Coincident Scrapie Infection and Nephritis Lead to Urinary Prion Excretion, Science, vol.310, issue.5746, pp.324-330, 2005.
DOI : 10.1126/science.1118829

C. Ligios, M. Cancedda, A. Carta, C. Santucciu, C. Maestrale et al., Sheep with Scrapie and Mastitis Transmit Infectious Prions through the Milk, Journal of Virology, vol.85, issue.2, pp.1136-1145, 2011.
DOI : 10.1128/JVI.02022-10

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3020009

T. Konold, S. Moore, S. Bellworthy, L. Terry, L. Thorne et al., Evidence of effective scrapie transmission via colostrum and milk in sheep, BMC Veterinary Research, vol.9, issue.1, p.99, 2013.
DOI : 10.1186/1746-6148-4-16

T. Konold, H. Simmons, P. Webb, P. Bellerby, and S. Hawkins, Gonz alez L. Transmission of classical scrapie via goat milk, Vet Rec, vol.172, p.455, 2013.

T. Konold, S. Moore, S. Bellworthy, and H. Simmons, Evidence of scrapie transmission via milk PMID:18397513, BMC Vet Res, vol.4, pp.141746-6148, 2008.
DOI : 10.1186/1746-6148-4-14

URL : http://doi.org/10.1186/1746-6148-4-14

M. Bruce, R. Will, J. Ironside, I. Mcconnell, D. Drummond et al., Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent, Nature, vol.389, issue.6650, pp.498-5019333239, 1997.
DOI : 10.1038/39057

C. Donnelly, N. Ferguson, A. Ghani, M. Woolhouse, C. Watt et al., The epidemiology of BSE in cattle herds in Great Britain. I. Epidemiological processes, demography of cattle and approaches to control by culling, Philosophical Transactions of the Royal Society B: Biological Sciences, vol.352, issue.1355, pp.781-8010062, 1997.
DOI : 10.1098/rstb.1997.0062

P. Boelle, J. Cesbron, and A. Valleron, Epidemiological evidence of higher susceptibility to vCJD in the young, BMC Infectious Diseases, vol.25, issue.1, pp.26153041991471-2334, 2004.
DOI : 10.1097/00004836-199709000-00017

URL : https://hal.archives-ouvertes.fr/inserm-00088568

K. Brown, G. Wathne, J. Sales, M. Bruce, and N. Mabbott, The Effects of Host Age on Follicular Dendritic Cell Status Dramatically Impair Scrapie Agent Neuroinvasion in Aged Mice, The Journal of Immunology, vol.183, issue.8, pp.5199-207, 2009.
DOI : 10.4049/jimmunol.0802695

K. Brown, A. Gossner, S. Mok, and N. Mabbott, The effects of host age on the transport of complementbound complexes to the spleen and the pathogenesis of intravenous scrapie infection, J Virol, vol.86, pp.1228-1265, 2012.

A. Kobayashi, D. Donaldson, C. Erridge, T. Kanaya, I. Williams et al., The functional maturation of M cells is dramatically reduced in the Peyer???s patches of aged mice, Mucosal Immunology, vol.51, issue.5, pp.1027-1064, 2013.
DOI : 10.1038/mi.2012.141

K. Brown and N. Mabbott, Evidence of subclinical prion disease in aged mice following exposure to bovine spongiform encephalopathy, Journal of General Virology, vol.95, issue.Pt_1, pp.231-274, 2014.
DOI : 10.1099/vir.0.058958-0

G. Wathne and N. Mabbott, The diverse roles of mononuclear phagocytes in prion disease pathogenesis, Prion, vol.161, issue.2, pp.124-157, 2012.
DOI : 10.1016/0166-0934(89)90023-2

F. Heppner, A. Christ, M. Klein, M. Prinz, M. Fried et al., Transepithelial prion transport by M cells, Nature Medicine, vol.7, issue.9, pp.976-983, 2001.
DOI : 10.1038/nm0901-976

D. Donaldson, A. Kobayashi, H. Ohno, H. Yagita, I. Williams et al., M cell-depletion blocks oral prion disease pathogenesis, Mucosal Immunology, vol.13, issue.2, pp.216-241, 2012.
DOI : 10.1016/0166-0934(89)90023-2

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3282432

C. Raymond, P. Aucouturier, and N. Mabbott, In Vivo Depletion of CD11c+ Cells Impairs Scrapie Agent Neuroinvasion from the Intestine, The Journal of Immunology, vol.179, issue.11, pp.7758-66, 2007.
DOI : 10.4049/jimmunol.179.11.7758

M. Beekes and P. Mcbride, The spread of prions through the body in naturally acquired transmissible spongiform encephalopathies, FEBS Journal, vol.82, issue.10, pp.588-605, 2007.
DOI : 10.1111/j.1742-4658.2007.05631.x

P. Mcbride, W. Schulz-shaeffer, M. Donaldson, M. Bruce, H. Diringer et al., Early Spread of Scrapie from the Gastrointestinal Tract to the Central Nervous System Involves Autonomic Fibers of the Splanchnic and Vagus Nerves, Journal of Virology, vol.75, issue.19, pp.9320-79320, 2001.
DOI : 10.1128/JVI.75.19.9320-9327.2001

M. Glatzel, F. Heppner, K. Albers, and A. Aguzzi, Sympathetic Innervation of Lymphoreticular Organs Is Rate Limiting for Prion Neuroinvasion, Neuron, vol.31, issue.1, pp.25-34, 2001.
DOI : 10.1016/S0896-6273(01)00331-2

F. Heppner, C. Musahl, I. Arrighi, M. Klein, T. Oesch et al., Prevention of Scrapie Pathogenesis by Transgenic Expression of Anti-Prion Protein Antibodies, Science, vol.294, issue.5540, pp.178-82, 2001.
DOI : 10.1126/science.1063093

A. White, P. Enever, M. Tayebi, R. Mushens, J. Linehan et al., Monoclonal antibodies inhibit prion replication and delay the development of prion disease, Nature, vol.358, issue.6927, pp.80-83, 2003.
DOI : 10.1038/nature01457

F. Go~-ni, E. Knudsen, F. Schreiber, H. Scholtzova, J. Pankiewicz et al., Mucosal vaccination delays or prevents prion infection via an oral route, Neuroscience, vol.133, issue.2, pp.413-434, 2005.
DOI : 10.1016/j.neuroscience.2005.02.031

T. Sonati, R. Reimann, J. Falsig, P. Baral, O. Connor et al., The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein, Nature, vol.66, issue.7465, pp.102-108, 2013.
DOI : 10.1038/nature12402

S. Gilch, N. Chitoor, Y. Taguchi, M. Stuart, and J. Jewell, Chronic Wasting Disease, Top Curr Chem, vol.305, pp.51-77, 2011.
DOI : 10.1007/128_2011_159

C. Sigurdson, A prion disease of cervids: Chronic wasting disease, Veterinary Research, vol.39, issue.4, p.41, 2008.
DOI : 10.1051/vetres:2008018

URL : https://hal.archives-ouvertes.fr/hal-00902927

A. Steve, H. Hawkins, K. Simmons, B. Gough, and . Maddison, Persistence of ovine scrapie infectivity in a farm environment following cleaning and decontamination, Vet Rec, vol.176, p.499, 2015.

E. S. Report, Protocol for further laboratory investigations into the distribution of infectivity of Atypical BSE, EFSA J, vol.12, p.3798, 2014.

F. Moda, P. Gambetti, S. Notari, L. Concha-marambio, M. Catania et al., Prions in the Urine of Patients with Variant Creutzfeldt???Jakob Disease, New England Journal of Medicine, vol.371, issue.6, pp.530-539, 2014.
DOI : 10.1056/NEJMoa1404401

C. Lacroux, E. Comoy, M. Moudjou, A. Perret-liaudet, S. Lugan et al., Preclinical Detection of Variant CJD and BSE Prions in Blood, PLoS Pathogens, vol.2, issue.4, p.1004202, 2014.
DOI : 10.1371/journal.ppat.1004202.s001

O. Andr-eoletti, C. Litaise, H. Simmons, F. Corbi-ere, S. Lugan et al., Highly efficient prion transmission by blood transfusion, PLoS Pathog, vol.8, issue.6, 2012.

P. Parchi, A. Giese, S. Capellari, P. Brown, W. Schulz-schaeffer et al., Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects, :AID- ANA12%3e3.0.CO, pp.224-331531, 1999.

P. Parchi, L. De-boni, D. Saverioni, M. Cohen, I. Ferrer et al., Consensus classification of human prion disease histotypes allows reliable identification of molecular subtypes: an inter-rater study among surveillance centres in Europe and USA, Acta Neuropathologica, vol.68, issue.4, pp.517-529, 2012.
DOI : 10.1007/s00401-012-1002-8

E. Uro-coste, H. Cassard, S. Simon, S. Lugan, J. Bilheude et al., Beyond PrP res type 1/type 2 dichotomy in Creutzfeldt-Jakob disease, PLoS Pathog PMID:AMBIGUOUS, vol.4, issue.3, 2008.
DOI : 10.1371/journal.ppat.1000029

URL : https://hal.archives-ouvertes.fr/inserm-00421129

P. Gambetti, Z. Dong, J. Yuan, X. Xiao, M. Zheng et al., A novel human disease with abnormal prion protein sensitive to protease, Annals of Neurology, vol.3, issue.6
DOI : 10.1002/ana.21420

E. Mitrov-a, D. Kosorinov-a, M. Gajdo-s, and K. Sebekov-a, A pilot study of a genetic CJD risk factor (E200K) in the general Slovak population, European Journal of Epidemiology, vol.65, issue.7, pp.595-602, 2014.
DOI : 10.1007/s10654-014-9937-9

T. Seuberlich, M. Gsponer, C. Dr?-ogem?-uller, M. Polak, S. Mccutcheon et al., Novel Prion Protein in BSE-affected Cattle, Switzerland, Emerging Infectious Diseases, vol.18, issue.1, pp.158-167, 2012.
DOI : 10.3201/eid1801.111225

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3310124

C. Sala, E. Morignat, N. Oussa?-id, E. Gay, D. Abrial et al., Individual factors associated with L- and H-type Bovine Spongiform Encephalopathy in France, BMC Veterinary Research, vol.8, issue.1, p.74, 2012.
DOI : 10.1016/j.prevetmed.2004.10.004

URL : http://doi.org/10.1186/1746-6148-8-74