Cấu trúc đa dạng của prion: sự khác biệt cấu trúc, cơ chế hình thành và vai trò trong rào cản loài

Aguilar-Calvo P, Xiao X, Bett C, Erana H, Soldau K, Castilla J, Nilsson KP, Surewicz WK, Sigurdson CJ (2017) Post-translational modifications in PrP expand the conformational diversity of prions in vivo. Sci Rep 7:43295 Angers RC, Kang HE, Napier D, Browning S, Seward T, Mathiason C, Balachandran A, McKenzie D, Castilla J, Soto C, Jewell J, Graham C, Hoover EA, Telling GC (2010) Prion strain mutation determined by prion protein conformational compatibility and primary structure. Science 328:1154–1158 Asante EA, Linehan JM, Desbruslais M, Joiner S, Gowland I, Wood AL, Welch J, Hill AF, Lloyd SE, Wadsworth JD, Collinge J (2002) BSE prions propagate as either variant CJD-like or sporadic CJD-like prion strains in transgenic mice expressing human prion protein. EMBO J 21:6358–6366 Asante EA, Smidak M, Grimshaw A, Houghton R, Tomlinson A, Jeelani A, Jakubcova T, Hamdan S, Richard-Londt A, Linehan JM, Brandner S, Alpers M, Whitfield J, Mead S, Wadsworth JD, Collinge J (2015) A naturally occurring variant of the human prion protein completely prevents prion disease. Nature 522:478–481 Babelhadj B, Di Bari MA, Pirisinu L, Chiappini B, Gaouar SBS, Riccardi G, Marcon S, Agrimi U, Nonno R, Vaccari G (2018) Prion disease in dromedary camels, Algeria. Emerg Infect Dis 24:1029–1036 Benestad SL, Mitchell G, Simmons M, Ytrehus B, Vikoren T (2016) First case of chronic wasting disease in Europe in a Norwegian free-ranging reindeer. Vet Res 47:88 Benestad SL, Sarradin P, Thu B, Schonheit J, Tranulis MA, Bratberg B (2003) Cases of scrapie with unusual features in Norway and designation of a new type, Nor98. Vet Rec 153:202–208 Berardi VA, Cardone F, Valanzano A, Lu M, Pocchiari M (2006) Preparation of soluble infectious samples from scrapie-infected brain: a new tool to study the clearance of transmissible spongiform encephalopathy agents during plasma fractionation. Transfusion 46:652–658 Beringue V, Herzog L, Jaumain E, Reine F, Sibille P, Le Dur A, Vilotte JL, Laude H (2012) Facilitated cross-species transmission of prions in extraneural tissue. Science 335:472–475 Beringue V, Le Dur A, Tixador P, Reine F, Lepourry L, Perret-Liaudet A, Haik S, Vilotte JL, Fontes M, Laude H (2008a) Prominent and persistent extraneural infection in human PrP transgenic mice infected with variant CJD. PLoS ONE 3:e1419 Beringue V, Tixador P, Andreoletti O, Reine F, Castille J, Lai TL, Le Dur A, Laisne A, Herzog L, Passet B, Rezaei H, Vilotte JL, Laude H (2020) Host prion protein expression levels impact prion tropism for the spleen. PLoS Pathog 16:e1008283 Beringue V, Vilotte JL, Laude H (2008b) Prion agent diversity and species barrier. Vet Res 39:47 Bian J, Khaychuk V, Angers RC, Fernandez-Borges N, Vidal E, Meyerett-Reid C, Kim S, Calvi CL, Bartz JC, Hoover EA, Agrimi U, Richt JA, Castilla J, Telling GC (2017) Prion replication without host adaptation during interspecies transmissions. Proc Natl Acad Sci U S A 114:1141–1146 Bian J, Kim S, Kane SJ, Crowell J, Sun JL, Christiansen J, Saijo E, Moreno JA, DiLisio J, Burnett E, Pritzkow S, Gorski D, Soto C, Kreeger TJ, Balachandran A, Mitchell G, Miller MW, Nonno R, Vikoren T, Vage J, Madslien K, Tran L, Vuong TT, Benestad SL, Telling GC (2021) Adaptive selection of a prion strain conformer corresponding to established North American CWD during propagation of novel emergent Norwegian strains in mice expressing elk or deer prion protein. PLoS Pathog 17:e1009748 Bishop MT, Will RG, Manson JC (2010) Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties. Proc Natl Acad Sci U S A 107:12005–12010 Bruce M, Chree A, McConnell I, Foster J, Pearson G, Fraser H (1994) Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier. Philos Trans R Soc Lond B Biol Sci 343:405–411 Bruce ME, Dickinson AG (1987) Biological evidence that scrapie agent has an independent genome. J Gen Virol 68(Pt 1):79–89 Cancellotti E, Mahal SP, Somerville R, Diack A, Brown D, Piccardo P, Weissmann C, Manson JC (2013) Post-translational changes to PrP alter transmissible spongiform encephalopathy strain properties. EMBO J 32:756–769 Cassard H, Huor A, Espinosa JC, Douet JY, Lugan S, Aron N, Vilette D, Delisle MB, Marin-Moreno A, Peran P, Beringue V, Torres JM, Ironside JW, Andreoletti O (2020) Prions from sporadic Creutzfeldt-Jakob disease patients propagate as strain mixtures. mBio 11 Castilla J, Gonzalez-Romero D, Saa P, Morales R, De Castro J, Soto C (2008a) Crossing the species barrier by PrP(Sc) replication in vitro generates unique infectious prions. Cell 134:757–768 Castilla J, Morales R, Saa P, Barria M, Gambetti P, Soto C (2008b) Cell-free propagation of prion strains. EMBO J 27:2557–2566 Chapuis J, Moudjou M, Reine F, Herzog L, Jaumain E, Chapuis C, Quadrio I, Boulliat J, Perret-Liaudet A, Dron M, Laude H, Rezaei H, Béringue V (2016) Emergence of two prion subtypes in ovine PrP transgenic mice infected with human MM2-cortical Creutzfeldt-Jakob disease prions. Acta Neuropathol Commun 4:10 Choi JK, Cali I, Surewicz K, Kong Q, Gambetti P, Surewicz WK (2016) Amyloid fibrils from the N-terminal prion protein fragment are infectious. Proc Natl Acad Sci U S A 113:13851–13856 Collinge J (2001) Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 24:519–550 Collinge J (2012) Cell biology. The Risk of Prion Zoonoses Science 335:411–413 Collinge J (2016) Mammalian prions and their wider relevance in neurodegenerative diseases. Nature 539:217–226 Collinge J, Clarke AR (2007) A general model of prion strains and their pathogenicity. Science 318:930–936 Collinge J, Palmer MS, Sidle KC, Hill AF, Gowland I, Meads J, Asante E, Bradley R, Doey LJ, Lantos PL (1995) Unaltered susceptibility to BSE in transgenic mice expressing human prion protein. Nature 378:779–783 Collinge J, Sidle KC, Meads J, Ironside J, Hill AF (1996) Molecular analysis of prion strain variation and the aetiology of “new variant” CJD. Nature 383:685–690 Collins SR, Douglass A, Vale RD, Weissman JS (2004) Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol 2:e321 Cronier S, Gros N, Tattum MH, Jackson GS, Clarke AR, Collinge J, Wadsworth JD (2008) Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin. Biochem J 416:297–305 Csermely P, Palotai R, Nussinov R (2010) Induced fit, conformational selection and independent dynamic segments: an extended view of binding events. Trends Biochem Sci 35:539–546 D’Castro L, Wenborn A, Gros N, Joiner S, Cronier S, Collinge J, Wadsworth JD (2010) Isolation of proteinase K-sensitive prions using pronase E and phosphotungstic acid. PLoS ONE 5:e15679 DeArmond SJ, Sanchez H, Yehiely F, Qiu Y, Ninchak-Casey A, Daggett V, Camerino AP, Cayetano J, Rogers M, Groth D, Torchia M, Tremblay P, Scott MR, Cohen FE, Prusiner SB (1997) Selective neuronal targeting in prion disease. Neuron 19:1337–1348 Eghiaian F, Grosclaude J, Lesceu S, Debey P, Doublet B, Treguer E, Rezaei H, Knossow M (2004) Insight into the PrPC– > PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants. Proc Natl Acad Sci U S A 101:10254–10259 Elsen JM, Amigues Y, Schelcher F, Ducrocq V, Andreoletti O, Eychenne F, Khang JV, Poivey JP, Lantier F, Laplanche JL (1999) Genetic susceptibility and transmission factors in scrapie: detailed analysis of an epidemic in a closed flock of Romanov. Arch Virol 144:431–445 Endo T, Groth D, Prusiner SB, Kobata A (1989) Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry 28:8380–8388 Eskandari-Sedighi G, Cortez LM, Yang J, Daude N, Shmeit K, Sim V, Westaway D (2021) Quaternary Structure Changes for PrP(Sc) Predate PrP(C) Downregulation and neuronal death during progression of experimental scrapie disease. Mol Neurobiol 58:375–390 Fediaevsky A, Tongue SC, Noremark M, Calavas D, Ru G, Hopp P (2008) A descriptive study of the prevalence of atypical and classical scrapie in sheep in 20 European countries. BMC Vet Res 4:19 Fernandez-Borges N, Espinosa JC, Marin-Moreno A, Aguilar-Calvo P, Asante EA, Kitamoto T, Mohri S, Andreoletti O, Torres JM (2017) Protective effect of Val129-PrP against bovine spongiform encephalopathy but not variant Creutzfeldt-Jakob disease. Emerg Infect Dis 23:1522–1530 Foliaki ST, Lewis V, Islam AMT, Ellett LJ, Senesi M, Finkelstein DI, Roberts B, Lawson VA, Adlard PA, Collins SJ (2019) Early existence and biochemical evolution characterise acutely synaptotoxic PrPSc. PLoS Pathog 15:e1007712 Gill ON, Spencer Y, Richard-Loendt A, Kelly C, Brown D, Sinka K, Andrews N, Dabaghian R, Simmons M, Edwards P, Bellerby P, Everest DJ, McCall M, McCardle LM, Linehan J, Mead S, Hilton DA, Ironside JW, Brandner S (2020) Prevalence in Britain of abnormal prion protein in human appendices before and after exposure to the cattle BSE epizootic. Acta Neuropathol 139:965–976 Griffith JS (1967) Self-replication and scrapie. Nature 215:1043–1044 Halliez S, Martin-Lanneree S, Passet B, Hernandez-Rapp J, Castille J, Urien C, Chat S, Laude H, Vilotte JL, Mouillet-Richard S, Beringue V (2015) Prion protein localizes at the ciliary base during neural and cardiovascular development, and its depletion affects alpha-tubulin post-translational modifications. Sci Rep 5:17146 Hannaoui S, Triscott E, Duque Velasquez C, Chang SC, Arifin MI, Zemlyankina I, Tang X, Bollinger T, Wille H, McKenzie D, Gilch S (2021) New and distinct chronic wasting disease strains associated with cervid polymorphism at codon 116 of the Prnp gene. PLoS Pathog 17:e1009795 Haybaeck J, Heikenwalder M, Klevenz B, Schwarz P, Margalith I, Bridel C, Mertz K, Zirdum E, Petsch B, Fuchs TJ, Stitz L, Aguzzi A (2011) Aerosols transmit prions to immunocompetent and immunodeficient mice. PLoS Pathog 7:e1001257 Hazards EPoB, Koutsoumanis K, Allende A, Alvarez-Ordonez A, Bolton D, Bover-Cid S, Chemaly M, Davies R, De Cesare A, Herman L, Hilbert F, Lindqvist R, Nauta M, Peixe L, Ru G, Skandamis P, Suffredini E, Andreoletti O, Benestad SL, Comoy E, Nonno R, da Silva Felicio T, Ortiz-Pelaez A, Simmons MM (2019) Update on chronic wasting disease (CWD) III. EFSA J 17 Herzog C, Sales N, Etchegaray N, Charbonnier A, Freire S, Dormont D, Deslys JP, Lasmezas CI (2004) Tissue distribution of bovine spongiform encephalopathy agent in primates after intravenous or oral infection. Lancet 363:422–428 Huor A, Espinosa JC, Vidal E, Cassard H, Douet JY, Lugan S, Aron N, Marin-Moreno A, Lorenzo P, Aguilar-Calvo P, Badiola J, Bolea R, Pumarola M, Benestad SL, Orge L, Thackray AM, Bujdoso R, Torres JM, Andreoletti O (2019) The emergence of classical BSE from atypical/Nor98 scrapie. Proc Natl Acad Sci U S A Igel-Egalon A, Bohl J, Moudjou M, Herzog L, Reine F, Rezaei H, Beringue V (2019a) Heterogeneity and architecture of pathological prion protein assemblies: time to revisit the molecular basis of the prion replication process? Viruses 11 Igel-Egalon A, Laferriere F, Moudjou M, Bohl J, Mezache M, Knapple T, Herzog L, Reine F, Jas-Duval C, Doumic M, Rezaei H, Beringue V (2019b) Early stage prion assembly involves two subpopulations with different quaternary structures and a secondary templating pathway. Commun Biol 2:363 Igel-Egalon A, Laferriere F, Tixador P, Moudjou M, Herzog L, Reine F, Torres JM, Laude H, Rezaei H, Beringue V (2020) Crossing species barriers relies on structurally distinct prion assemblies and their complementation. Mol Neurobiol Igel-Egalon A, Moudjou M, Martin D, Busley A, Knapple T, Herzog L, Reine F, Lepejova N, Richard CA, Beringue V, Rezaei H (2017) Reversible unfolding of infectious prion assemblies reveals the existence of an oligomeric elementary brick. PLoS Pathog 13:e1006557 Jaumain E, Quadrio I, Herzog L, Reine F, Rezaei H, Andréoletti O, Laude H, Perret-Liaudet A, Haïk S, Béringue V (2016) Absence of evidence for a causal link between bovine spongiform encephalopathy strain variant L-BSE and known forms of sporadic Creutzfeldt-Jakob disease in human PrP transgenic mice. J Virol 90:10867–10874 Kimberlin RH, Walker CA (1978) Pathogenesis of mouse scrapie: effect of route of inoculation on infectivity titres and dose-response curves. J Comp Pathol 88:39–47 Kimberlin RH, Walker CA (1988) Pathogenesis of experimental scrapie. Ciba Found Symp 135:37–62 Koshland DE Jr (1963) Correlation of structure and function in enzyme action. Science 142:1533–1541 Kraus A, Hoyt F, Schwartz CL, Hansen B, Artikis E, Hughson AG, Raymond GJ, Race B, Baron GS, Caughey B (2021) High-resolution structure and strain comparison of infectious mammalian prions. Mol Cell Laferriere F, Tixador P, Moudjou M, Chapuis J, Sibille P, Herzog L, Reine F, Jaumain E, Laude H, Rezaei H, Beringue V (2013) Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics. PLoS Pathog 9:e1003702 Langevin C, Andreoletti O, Le Dur A, Laude H, Beringue V (2011) Marked influence of the route of infection on prion strain apparent phenotype in a scrapie transgenic mouse model. Neurobiol Dis 41:219–225 Lansbury PT Jr, Caughey B (1995) The chemistry of scrapie infection: implications of the “ice 9” metaphor. Chem Biol 2:1–5 Lasmezas CI, Comoy E, Hawkins S, Herzog C, Mouthon F, Konold T, Auvre F, Correia E, Lescoutra-Etchegaray N, Sales N, Wells G, Brown P, Deslys JP (2005) Risk of oral infection with bovine spongiform encephalopathy agent in primates. Lancet 365:781–783 Lasmezas CI, Fournier JG, Nouvel V, Boe H, Marce D, Lamoury F, Kopp N, Hauw JJ, Ironside J, Bruce M, Dormont D, Deslys JP (2001) Adaptation of the bovine spongiform encephalopathy agent to primates and comparison with Creutzfeldt– Jakob disease: implications for human health. Proc Natl Acad Sci U S A 98:4142–4147 Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 457:1128–1132 Le Dur A, Beringue V, Andreoletti O, Reine F, Lai TL, Baron T, Bratberg B, Vilotte JL, Sarradin P, Benestad SL, Laude H (2005) A newly identified type of scrapie agent can naturally infect sheep with resistant PrP genotypes. Proc Natl Acad Sci U S A 102:16031–16036 Le Dur A, Lai TL, Stinnakre MG, Laisne A, Chenais N, Rakotobe S, Passet B, Reine F, Soulier S, Herzog L, Tilly G, Rezaei H, Beringue V, Vilotte JL, Laude H (2017) Divergent prion strain evolution driven by PrPC expression level in transgenic mice. Nat Commun 8:14170 Legname G, Baskakov IV, Nguyen HO, Riesner D, Cohen FE, DeArmond SJ, Prusiner SB (2004) Synthetic mammalian prions. Science 305:673–676 Mahal SP, Jablonski J, Suponitsky-Kroyter I, Oelschlegel AM, Herva ME, Oldstone M, Weissmann C (2012) Propagation of RML prions in mice expressing PrP devoid of GPI anchor leads to formation of a novel, stable prion strain. PLoS Pathog 8:e1002746 Makarava N, Baskakov IV (2013) The evolution of transmissible prions: the role of deformed templating. PLoS Pathog 9:e1003759 Makarava N, Kovacs GG, Savtchenko R, Alexeeva I, Budka H, Rohwer RG, Baskakov IV (2011) Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease. PLoS Pathog 7:e1002419 Makarava N, Savtchenko R, Alexeeva I, Rohwer RG, Baskakov IV (2016) New molecular insight into mechanism of evolution of mammalian synthetic prions. Am J Pathol 186:1006–1014 Manka SW, Zhang W, Wenborn A, Betts J, Joiner S, Saibil HR, Collinge J, Wadsworth JDF (2022) 2.7 A cryo-EM structure of ex vivo RML prion fibrils. Nat Commun 13:4004 Marin B, Otero A, Lugan S, Espinosa JC, Marin-Moreno A, Vidal E, Hedman C, Romero A, Pumarola M, Badiola JJ, Torres JM, Andreoletti O, Bolea R (2021) Classical BSE prions emerge from asymptomatic pigs challenged with atypical/Nor98 scrapie. Sci Rep 11:17428 Martin D, Reine F, Herzog L, Igel-Egalon A, Aron N, Michel C, Moudjou M, Fichet G, Quadrio I, Perret-Liaudet A, Andreoletti O, Rezaei H, Beringue V (2021) Prion potentiation after life-long dormancy in mice devoid of PrP. Brain Commun 3:fcab092 Mays CE, Kim C, Haldiman T, van der Merwe J, Lau A, Yang J, Grams J, Di Bari MA, Nonno R, Telling GC, Kong Q, Langeveld J, McKenzie D, Westaway D, Safar JG (2014) Prion disease tempo determined by host-dependent substrate reduction. J Clin Invest 124:847–858 Moazami-Goudarzi K, Andreoletti O, Vilotte JL, Beringue V (2021) Review on PRNP genetics and susceptibility to chronic wasting disease of Cervidae. Vet Res 52:128 Moroncini G, Kanu N, Solforosi L, Abalos G, Telling GC, Head M, Ironside J, Brockes JP, Burton DR, Williamson RA (2004) Motif-grafted antibodies containing the replicative interface of cellular PrP are specific for PrPSc. Proc Natl Acad Sci U S A 101:10404–10409 Moudjou M, Castille J, Passet B, Herzog L, Reine F, Vilotte JL, Rezaei H, Beringue V, Igel-Egalon A (2020) Improving the predictive value of prion inactivation validation methods to minimize the risks of iatrogenic transmission with medical instruments. Front Bioeng Biotechnol 8:591024 Moudjou M, Chapuis J, Mekrouti M, Reine F, Herzog L, Sibille P, Laude H, Vilette D, Andreoletti O, Rezaei H, Dron M, Beringue V (2016) Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification. Sci Rep 6:29116 Moudjou M, Sibille P, Fichet G, Reine F, Chapuis J, Herzog L, Jaumain E, Laferriere F, Richard CA, Laude H, Andreoletti O, Rezaei H, Beringue V (2014) Highly infectious prions generated by a single round of microplate-based protein misfolding cyclic amplification. Mbio 5:e00829-e1813 Mouillet-Richard S, Ghazi A, Laurent-Puig P (2021) The cellular prion protein and the hallmarks of cancer. Cancers (Basel) 13 Nakaoke R, Sakaguchi S, Atarashi R, Nishida N, Arima K, Shigematsu K, Katamine S (2000) Early appearance but lagged accumulation of detergent-insoluble prion protein in the brains of mice inoculated with a mouse-adapted Creutzfeldt-Jakob disease agent. Cell Mol Neurobiol 20:717–730 Nakic N, Tran TH, Novokmet M, Andreoletti O, Lauc G, Legname G (2021) Site-specific analysis of N-glycans from different sheep prion strains. PLoS Pathog 17:e1009232 Nonno R, Di Bari MA, Cardone F, Vaccari G, Fazzi P, Dell’Omo G, Cartoni C, Ingrosso L, Boyle A, Galeno R, Sbriccoli M, Lipp HP, Bruce M, Pocchiari M, Agrimi U (2006) Efficient transmission and characterization of Creutzfeldt-Jakob disease strains in bank voles. PLoS Pathog 2:e12 Nonno R, Notari S, Di Bari MA, Cali I, Pirisinu L, d’Agostino C, Cracco L, Kofskey D, Vanni I, Lavrich J, Parchi P, Agrimi U, Gambetti P (2019) Variable protease-sensitive prionopathy transmission to bank voles. Emerg Infect Dis 25:73–81 Notari S, Appleby BS, Gambetti P (2018) Variably protease-sensitive prionopathy. Handb Clin Neurol 153:175–190 Owen JP, Maddison BC, Whitelam GC, Gough KC (2007) Use of thermolysin in the diagnosis of prion diseases. Mol Biotechnol 35:161–170 Parchi P, Giese A, Capellari S, Brown P, Schulz-Schaeffer W, Windl O, Zerr I, Budka H, Kopp N, Piccardo P, Poser S, Rojiani A, Streichemberger N, Julien J, Vital C, Ghetti B, Gambetti P, Kretzschmar H (1999) Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects. Ann Neurol 46:224–233 Pastrana MA, Sajnani G, Onisko B, Castilla J, Morales R, Soto C, Requena JR (2006) Isolation and characterization of a proteinase K-sensitive PrPSc fraction. Biochemistry 45:15710–15717 Pirisinu L, Di Bari MA, D’Agostino C, Marcon S, Riccardi G, Poleggi A, Cohen ML, Appleby BS, Gambetti P, Ghetti B, Agrimi U, Nonno R (2016) Gerstmann-Straussler-Scheinker disease subtypes efficiently transmit in bank voles as genuine prion diseases. Sci Rep 6:20443 Piro JR, Harris BT, Nishina K, Soto C, Morales R, Rees JR, Supattapone S (2009) Prion protein glycosylation is not required for strain-specific neurotropism. J Virol 83:5321–5328 Polymenidou M, Stoeck K, Glatzel M, Vey M, Bellon A, Aguzzi A (2005) Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease. Lancet Neurol 4:805–814 Prusiner SB (1982) Novel proteinaceous infectious particles cause scrapie. Science 216:136–144 Prusiner SB (1998) Prions. Proc Natl Acad Sci U S A 95:13363–13383 Race B, Phillips K, Meade-White K, Striebel J, Chesebro B (2015) Increased infectivity of anchorless mouse scrapie prions in transgenic mice overexpressing human prion protein. J Virol 89:6022–6032 Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wuthrich K (1996) NMR structure of the mouse prion protein domain PrP(121–231). Nature 382:180–182 Riesner D, Kellings K, Post K, Wille H, Serban H, Groth D, Baldwin MA, Prusiner SB (1996) Disruption of prion rods generates 10-nm spherical particles having high alpha-helical content and lacking scrapie infectivity. J Virol 70:1714–1722 Rudd PM, Merry AH, Wormald MR, Dwek RA (2002) Glycosylation and prion protein. Curr Opin Struct Biol 12:578–586 Saborio GP, Permanne B, Soto C (2001) Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411:810–813 Safar J, Wille H, Itri V, Groth D, Serban H, Torchia M, Cohen FE, Prusiner SB (1998) Eight prion strains have PrP(Sc) molecules with different conformations. Nat Med 4:1157–1165 Salamat MK, Dron M, Chapuis J, Langevin C, Laude H (2011) Prion propagation in cells expressing PrP glycosylation mutants. J Virol 85:3077–3085 Sarradin P, Viglietta C, Limouzin C, Andreoletti O, Daniel-Carlier N, Barc C, Leroux-Coyau M, Berthon P, Chapuis J, Rossignol C, Gatti JL, Belghazi M, Labas V, Vilotte JL, Beringue V, Lantier F, Laude H, Houdebine LM (2015) Transgenic rabbits expressing ovine PrP are susceptible to scrapie. PLoS Pathog 11:e1005077 Scott M, Foster D, Mirenda C, Serban D, Coufal F, Walchli M, Torchia M, Groth D, Carlson G, DeArmond SJ, Westaway D, Prusiner SB (1989) Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 59:847–857 Sevillano AM, Aguilar-Calvo P, Kurt TD, Lawrence JA, Soldau K, Nam TH, Schumann T, Pizzo DP, Nystrom S, Choudhury B, Altmeppen H, Esko JD, Glatzel M, Nilsson KPR, Sigurdson CJ (2020) Prion protein glycans reduce intracerebral fibril formation and spongiosis in prion disease. J Clin Invest 130:1350–1362 Shorter J, Lindquist S (2006) Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol Cell 23:425–438 Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, Hayes SF, Caughey B (2005) The most infectious prion protein particles. Nature 437:257–261 Solforosi L, Bellon A, Schaller M, Cruite JT, Abalos GC, Williamson RA (2007) Toward molecular dissection of PrPC-PrPSc interactions. J Biol Chem 282:7465–7471 Somerville RA, Ritchie LA (1990) Differential glycosylation of the protein (PrP) forming scrapie-associated fibrils. J Gen Virol 71(Pt 4):833–839 Stahl N, Baldwin MA, Burlingame AL, Prusiner SB (1990) Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein. Biochemistry 29:8879–8884 Taylor DM, McConnell I, Fraser H (1996) Scrapie infection can be established readily through skin scarification in immunocompetent but not immunodeficient mice. J Gen Virol 77:1595–1599 Thackray AM, Andreoletti O, Bujdoso R (2018) Mammalian prion propagation in PrP transgenic Drosophila. Brain 141:2700–2710 Tixador P, Herzog L, Reine F, Jaumain E, Chapuis J, Le Dur A, Laude H, Beringue V (2010) The physical relationship between infectivity and prion protein aggregates is strain-dependent. PLoS Pathog 6:e1000859 Tsai CJ, Kumar S, Ma B, Nussinov R (1999) Folding funnels, binding funnels, and protein function. Protein Sci 8:1181–1190 Turnbaugh JA, Unterberger U, Saa P, Massignan T, Fluharty BR, Bowman FP, Miller MB, Supattapone S, Biasini E, Harris DA (2012) The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc). J Neurosci 32:8817–8830 Tuzi NL, Cancellotti E, Baybutt H, Blackford L, Bradford B, Plinston C, Coghill A, Hart P, Piccardo P, Barron RM, Manson JC (2008) Host PrP glycosylation: a major factor determining the outcome of prion infection. PLoS Biol 6:e100 Uro-Coste E, Cassard H, Simon S, Lugan S, Bilheude JM, Perret-Liaudet A, Ironside JW, Haik S, Basset-Leobon C, Lacroux C, Peoch K, Streichenberger N, Langeveld J, Head MW, Grassi J, Hauw JJ, Schelcher F, Delisle MB, Andreoletti O (2008) Beyond PrP9res) type 1/type 2 dichotomy in Creutzfeldt-Jakob disease. PLoS Pathog 4:e1000029 Velasquez CD, Kim C, Haldiman T, Kim C, Herbst A, Aiken J, Safar JG, McKenzie D (2020) Chronic wasting disease (CWD) prion strains evolve via adaptive diversification of conformers in hosts expressing prion protein polymorphisms. J Biol Chem 295:4985–5001 Wadsworth JD, Asante EA, Desbruslais M, Linehan JM, Joiner S, Gowland I, Welch J, Stone L, Lloyd SE, Hill AF, Brandner S, Collinge J (2004) Human prion protein with valine 129 prevents expression of variant CJD phenotype. Science 306:1793–1796 Watts JC, Giles K, Patel S, Oehler A, DeArmond SJ, Prusiner SB (2014) Evidence that bank vole PrP is a universal acceptor for prions. PLoS Pathog 10:e1003990 Weissmann C, Li J, Mahal SP, Browning S (2011) Prions on the move. EMBO Rep 12:1109–1117 Wiseman FK, Cancellotti E, Piccardo P, Iremonger K, Boyle A, Brown D, Ironside JW, Manson JC, Diack AB (2015) The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between species. J Virol 89:4738–4747