Caprine PrP variants harboring Asp-146, His-154 and Gln-211 alleles display reduced convertibility upon interaction with pathogenic murine prion protein in scrapie infected cells

REFERENCES

• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136-44; http://dx.doi.org/10.1126/science.6801762
   PubMed Web of Science ®Google Scholar
• Weber P, Giese A, Piening N, Mitteregger G, Thomzig A, Beekes M, Kretzschmar HA. Generation of genuine prion infectivity by serial PMCA. Vet Microbiol 2007; 123:346-57; PMID:17493773; http://dx.doi.org/10.1016/j.vetmic.2007.04.004
   PubMed Web of Science ®Google Scholar
• Makarava N, Kovacs GG, Bocharova O, Savtchenko R, Alexeeva I, Budka H, Rohwer RG, Baskakov IV. Recombinant prion protein induces a new transmissible prion disease in wild-type animals. Acta Neuropathol 2010; 119:177-87; PMID:20052481; http://dx.doi.org/10.1007/s00401-009-0633-x
   PubMed Web of Science ®Google Scholar
• Kim J-I, Cali I, Surewicz K, Kong Q, Raymond GJ, Atarashi R, Race B, Qing L, Gambetti P, Caughey B, et al. Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J Biol Chem 2010; 285:14083-7; PMID:20304915; http://dx.doi.org/10.1074/jbc.C110.113464
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Prions. Proc Natl Acad Sci U S A 1998; 95:13363-83; http://dx.doi.org/10.1073/pnas.95.23.13363
   PubMed Web of Science ®Google Scholar
• Goldmann W. PrP genetics in ruminant transmissible spongiform encephalopathies. Vet Res 2008; 39:30; PMID:18284908; http://dx.doi.org/10.1051/vetres:2008010
   PubMed Web of Science ®Google Scholar
• Hagenaars TJ, Melchior MB, Bossers A, Davidse A, Engel B, van Zijderveld FG. Scrapie prevalence in sheep of susceptible genotype is declining in a population subject to breeding for resistance. BMC Vet Res 2010; 6:25; PMID:20470415; http://dx.doi.org/10.1186/1746-6148-6-25
   PubMed Web of Science ®Google Scholar
• Nodelijk G, van Roermund HJW, van Keulen LJM, Engel B, Vellema P, Hagenaars TJ. Breeding with resistant rams leads to rapid control of classical scrapie in affected sheep flocks. Vet Res 2011; 42:5; PMID:21314971; http://dx.doi.org/10.1186/1297-9716-42-5
   PubMed Web of Science ®Google Scholar
• Babar ME, Abdullah M, Nadeem A, Haq A. U. Prion protein gene polymorphisms in four goat breeds of Pakistan. Mol Biol Rep 2009; 36:141-4; PMID:17934795; http://dx.doi.org/10.1007/s11033-007-9162-7
   PubMed Web of Science ®Google Scholar
• Vaccari G, Panagiotidis CH, Acin C, Peletto S, Barillet F, Acutis P, Bossers A, Langeveld J, van Keulen L, Sklaviadis T, et al. State-of-the-art review of goat TSE in the European Union, with special emphasis on PRNP genetics and epidemiology. Vet Res 2009; 40:48; PMID:19505422; http://dx.doi.org/10.1051/vetres/2009031
   PubMed Web of Science ®Google Scholar
• Bouzalas IG, Dovas CI, Banos G, Papanastasopoulou M, Kritas S, Oevermann A, Papakostaki D, Evangelia C, Papadopoulos O, Seuberlich T, et al. Caprine PRNP polymorphisms at codons 171, 211, 222 and 240 in a Greek herd and their association with classical scrapie. J Gen Virol 2010; 91:1629-34; PMID:20107013; http://dx.doi.org/10.1099/vir.0.017350-0
   PubMed Web of Science ®Google Scholar
• Hussain A, Babar ME, Imran M, Haq IU, Javed MM. Detection of four novel polymorphisms in PrP gene of Pakistani sheep (Damani and Hashtnagri) and goats (Kamori and Local Hairy) breeds. Virol J 2011; 8:246; PMID:21595993; http://dx.doi.org/10.1186/1743-422X-8-246
   PubMed Web of Science ®Google Scholar
• Goldmann W, Ryan K, Stewart P, Parnham D, Xicohtencatl R, Fernandez N, Saunders G, Windl O, González L, Bossers A, et al. Caprine prion gene polymorphisms are associated with decreased incidence of classical scrapie in goat herds in the United Kingdom. Vet Res 2011; 42:110; PMID:22040234; http://dx.doi.org/10.1186/1297-9716-42-110
   PubMed Web of Science ®Google Scholar
• Papasavva-Stylianou P, Windl O, Saunders G, Mavrikiou P, Toumazos P, Kakoyiannis C. PrP gene polymorphisms in Cyprus goats and their association with resistance or susceptibility to natural scrapie. Vet J 2011; 187:245-50; PMID:20093056; http://dx.doi.org/10.1016/j.tvjl.2009.10.015
   PubMed Web of Science ®Google Scholar
• Fragkiadaki EG, Vaccari G, Ekateriniadou LV, Agrimi U, Giadinis ND, Chiappini B, Esposito E, Conte M, Nonno R. PRNP genetic variability and molecular typing of natural goat scrapie isolates in a high number of infected flocks. Vet Res 2011; 42:104; PMID:21961834; http://dx.doi.org/10.1186/1297-9716-42-104
   PubMed Web of Science ®Google Scholar
• Acín C, Martín-Burriel I, Monleón E, Lyahyai J, Pitarch JL, Serrano C, Monzón M, Zaragoza P, Badiola JJ. Prion protein gene variability in Spanish goats. Inference through susceptibility to classical scrapie strains and pathogenic distribution of peripheral PrP(sc.). PLoS One 2013; 8:e61118; PMID:23580248; http://dx.doi.org/10.1371/journal.pone.0061118
   PubMed Web of Science ®Google Scholar
• Goldmann W, Martin T. Novel polymorphisms in the caprine PrP gene: a codon 142 mutation associated with scrapie incubation period. J Gen Virol 1996; 77:2885-91; PMID:8922485; http://dx.doi.org/10.1099/0022-1317-77-11-2885
   PubMed Web of Science ®Google Scholar
• Billinis C, Panagiotidis CH, Psychas V, Argyroudis S, Nicolaou A, Leontides S, Papadopoulos O, Sklaviadis T. Prion protein gene polymorphisms in natural goat scrapie. J Gen Virol 2002; 83:713-21; PMID:11842266; http://dx.doi.org/10.1099/0022-1317-83-3-713
   PubMed Web of Science ®Google Scholar
• Papasavva-Stylianou P, Kleanthous M, Toumazos P, Mavrikiou P, Loucaides P. Novel polymorphisms at codons 146 and 151 in the prion protein gene of Cyprus goats, and their association with natural scrapie. Vet J 2007; 173:459-62; PMID:16314132; http://dx.doi.org/10.1016/j.tvjl.2005.09.013
   PubMed Web of Science ®Google Scholar
• Ortiz-Pelaez A, Georgiadou S, Simmons MM, Windl O, Dawson M, Arnold ME, Neocleous P, Papasavva-Stylianou P. Allelic variants at codon 146 in the PRNP gene show significant differences in the risk for natural scrapie in Cypriot goats. Epidemiol Infect 2015; 143:1304-10; PMID:25140573; http://dx.doi.org/10.1017/S0950268814002064
   PubMed Web of Science ®Google Scholar
• Barillet F, Mariat D, Amigues Y, Faugeras R, Caillat H, Moazami-Goudarzi K, Rupp R, Babilliot JM, Lacroux C, Lugan S, et al. Identification of seven haplotypes of the caprine PrP gene at codons 127, 142, 154, 211, 222 and 240 in French Alpine and Saanen breeds and their association with classical scrapie. J Gen Virol 2009; 90:769-76; PMID:19218225; http://dx.doi.org/10.1099/vir.0.006114-0
   PubMed Web of Science ®Google Scholar
• Acutis PL, Bossers A, Priem J, Riina MV, Peletto S, Mazza M, Casalone C, Forloni G, Ru G, Caramelli M. Identification of prion protein gene polymorphisms in goats from Italian scrapie outbreaks. J Gen Virol 2006; 87:1029-33; PMID:16528054; http://dx.doi.org/10.1099/vir.0.81440-0
   PubMed Web of Science ®Google Scholar
• Corbière F, Perrin-Chauvineau C, Lacroux C, Costes P, Thomas M, Bremaud I, Martin S, Lugan S, Chartier C, Schelcher F, et al. PrP-associated resistance to scrapie in five highly infected goat herds. J Gen Virol 2013; 94:241-5; PMID:23100359; http://dx.doi.org/10.1099/vir.0.047225-0
   PubMed Web of Science ®Google Scholar
• Eiden M, Soto EO, Mettenleiter TC, Groschup MH. Effects of polymorphisms in ovine and caprine prion protein alleles on cell-free conversion. Vet Res 2011; 42:30; PMID:21324112; http://dx.doi.org/10.1186/1297-9716-42-30
   PubMed Web of Science ®Google Scholar
• Aguilar-Calvo P, Espinosa JC, Pintado B, Gutiérrez-Adán A, Alamillo E, Miranda A, Prieto I, Bossers A, Andreoletti O, Torres JM. Role of the Goat K222-PrPC Polymorphic Variant in Prion Infection Resistance. J Virol 2014; 88:2670-6; PMID:24352451; http://dx.doi.org/10.1128/JVI.02074-13
   PubMed Web of Science ®Google Scholar
• Lacroux C, Perrin-Chauvineau C. Genetic resistance to scrapie infection in experimentally challenged goats. J Virol 2014; 88:2406-13. Available from: PMID:24284317; http://dx.doi.org/10.1128/JVI.02872-13
   PubMed Web of Science ®Google Scholar
• Acutis P, Martucci F, D'Angelo A, Peletto S. Resistance to classical scrapie in experimentally challenged goats carrying mutation K222 of the prion protein gene. Vet Res 2012; 43:8; PMID:22296670; http://dx.doi.org/10.1186/1297-9716-43-8
   PubMed Web of Science ®Google Scholar
• White S, Reynolds J, Waldron D. Extended scrapie incubation time in goats singly heterozygous for PRNP S146 or K222. Gene 2012; 501:49-51; PMID:22516690; http://dx.doi.org/10.1016/j.gene.2012.03.068
   PubMed Web of Science ®Google Scholar
• Harmeyer S, Pfaff E, Groschup MH. Synthetic peptide vaccines yield monoclonal antibodies to cellular and pathological prion proteins of ruminants. J Gen Virol 1998; 79:937-45; PMID:9568991; http://dx.doi.org/10.1099/0022-1317-79-4-937
   PubMed Web of Science ®Google Scholar
• Haire LF, Whyte SM, Vasisht N, Gill AC, Verma C, Dodson EJ, Dodson GG, Bayley PM. The crystal structure of the globular domain of sheep prion protein. J Mol Biol 2004; 336:1175-83; PMID:15037077; http://dx.doi.org/10.1016/j.jmb.2003.12.059
   PubMed Web of Science ®Google Scholar
• Konold T, Moore SJ, Bellworthy SJ, Terry LA, Thorne L, Ramsay A, Salguero FJ, Simmons MM, Simmons HA. Evidence of effective scrapie transmission via colostrum and milk in sheep. BMC Vet Res 2013; 9:99; PMID:23651710; http://dx.doi.org/10.1186/1746-6148-9-99
   PubMed Web of Science ®Google Scholar
• Konold T, Simmons HA, Webb PR, Bellerby PJ, Hawkins SAC, González L. Transmission of classical scrapie via goat milk. Vet Rec 2013; 172:455; PMID:23625249; http://dx.doi.org/10.1136/vr.f2613
   PubMed Web of Science ®Google Scholar
• Schneider DA, Madsen-Bouterse SA, Zhuang D, Truscott TC, Dassanayake RP, O'Rourke KI. The placenta shed from goats with classical scrapie is infectious to goat kids and lambs. J Gen Virol 2015; 96:2464-9; PMID:25888622; http://dx.doi.org/10.1099/vir.0.000151
   PubMed Web of Science ®Google Scholar
• Gough KC, Maddison BC. Prion transmission: Prion excretion and occurrence in the environment. Prion 2010; 4:275-82; PMID:20948292; http://dx.doi.org/10.4161/pri.4.4.13678
   PubMed Web of Science ®Google Scholar
• Johnson CJ, Phillips KE, Schramm PT, McKenzie D, Aiken JM, Pedersen JA. Prions adhere to soil minerals and remain infectious. PLoS Pathog 2006; 2:e32; PMID:16617377; http://dx.doi.org/10.1371/journal.ppat.0020032
   PubMed Web of Science ®Google Scholar
• Ermonval M, Mouillet-Richard S, Codogno P, Kellermann O, Botti J. Evolving views in prion glycosylation: functional and pathological implications. Biochimie 2003; 85:33-45; PMID:12765773; http://dx.doi.org/10.1016/S0300-9084(03)00040-3
   PubMed Web of Science ®Google Scholar
• Grassmann A, Wolf H, Hofmann J, Graham J, Vorberg I. Cellular aspects of prion replication in vitro. Viruses 2013; 5:374-405; PMID:23340381; http://dx.doi.org/10.3390/v5010374
   PubMed Web of Science ®Google Scholar
• Linden R, Martins V. Physiology of the prion protein. Physiol Rev 2008; 88:673-728; PMID:18391177; http://dx.doi.org/10.1152/physrev.00007.2007
   PubMed Web of Science ®Google Scholar
• Veith NM, Plattner H, Stuermer CAO, Schulz-Schaeffer WJ, Bürkle A. Immunolocalisation of PrPSc in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy; PMID:18834644
   PubMedGoogle Scholar
• Noinville S, Chich JF, Rezaei H. Misfolding of the prion protein: Linking biophysical and biological approaches. Vet Res 2008; 39; PMID:18533092; http://dx.doi.org/10.1051/vetres:2008025
   PubMed Web of Science ®Google Scholar
• Hagiwara K, Hara H, Hanada K. Species-barrier phenomenon in prion transmissibility from a viewpoint of protein science. J Biochem 2013; 153:139-45; PMID:23284000; http://dx.doi.org/10.1093/jb/mvs148
   PubMed Web of Science ®Google Scholar
• Horiuchi M, Priola SA, Chabry J, Caughey B. Interactions between heterologous forms of prion protein: binding, inhibition of conversion, and species barriers. Proc Natl Acad Sci U S A 2000; 97:5836-41; PMID:10811921; http://dx.doi.org/10.1073/pnas.110523897
   PubMed Web of Science ®Google Scholar
• Priola SA, Chesebro B. A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells. J Virol 1995; 69:7754-8; PMID:7494285
   PubMed Web of Science ®Google Scholar
• Prigent S, Rezaei H. PrP assemblies: Spotting the responsible regions in Prion propagation. Prion 2011; 5:69-75; PMID:21788728; http://dx.doi.org/10.4161/pri.5.2.16383
   PubMed Web of Science ®Google Scholar
• Sigurdson C. A molecular switch controls interspecies prion disease transmission in mice. J Clin Invest 2010; 120:2590-9; PMID:20551516; http://dx.doi.org/10.1172/JCI42051
   PubMed Web of Science ®Google Scholar
• Bett C, Fernández-Borges N, Kurt TD, Lucero M, Nilsson KPR, Castilla J, Sigurdson CJ. Structure of the β2-α2 loop and interspecies prion transmission. FASEB J 2012; 26:2868-76; PMID:22490928; http://dx.doi.org/10.1096/fj.11-200923
   PubMed Web of Science ®Google Scholar
• Vorberg I, Groschup M, Pfaff E, Priola S. Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform. J Virol 2003; 77:2003-9; PMID:12525634; http://dx.doi.org/10.1128/JVI.77.3.2003-2009.2003
   PubMed Web of Science ®Google Scholar
• Mallik S, Yang W, Norstrom EM, Mastrianni JA. Live cell fluorescence resonance energy transfer predicts an altered molecular association of heterologous PrPSc with PrPC. J Biol Chem 2010; 285:8967-75; PMID:20086009; http://dx.doi.org/10.1074/jbc.M109.058107
   PubMed Web of Science ®Google Scholar
• Abalos GC, Cruite JT, Bellon A, Hemmers S, Akagi J, Mastrianni JA, Williamson RA, Solforosi L. Identifying key components of the PrPC-PrPSc replicative interface. J Biol Chem 2008; 283:34021-8; PMID:18826953; http://dx.doi.org/10.1074/jbc.M804475200
   PubMed Web of Science ®Google Scholar
• Norstrom EM, Mastrianni JA. The AGAAAAGA palindrome in PrP is required to generate a productive PrPSc-PrPC complex that leads to prion propagation. J Biol Chem 2005; 280:27236-43; PMID:15917252; http://dx.doi.org/10.1074/jbc.M413441200
   PubMed Web of Science ®Google Scholar
• Taguchi Y, Schätzl HM. Identifying critical sites of PrPc -PrPSc interaction in prion-infected cells by dominant-negative inhibition. Prion 2013; 7:452-456; PMID:24401595; http://dx.doi.org/10.4161/pri.27500
   PubMed Web of Science ®Google Scholar
• Hara H, Okemoto-Nakamura Y, Shinkai-Ouchi F, Hanada K, Yamakawa Y, Hagiwara K. Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrP(C) to PrP(Sc) in prion-infected neuroblastoma cells. J Virol 2012; 86:5626-36; PMID:22398286; http://dx.doi.org/10.1128/JVI.06606-11
   PubMed Web of Science ®Google Scholar
• Chen J, Thirumalai D. Helices 2 and 3 are the initiation sites in the PrP C→ PrP SC transition. Biochemistry 2012; 52:310-319; PMID:23256626; http://dx.doi.org/10.1021/bi3005472
   PubMed Web of Science ®Google Scholar
• Norstrom EM, Mastrianni JA. The charge structure of helix 1 in the prion protein regulates conversion to pathogenic PrPSc. J Virol 2006; 80:8521-9; PMID:16912302; http://dx.doi.org/10.1128/JVI.00366-06
   PubMed Web of Science ®Google Scholar
• Safar J, Wille H, Itri V, Groth D, Serban H, Torchia M, Cohen FE, Prusiner SB. Eight prion strains have PrP(Sc) molecules with different conformations. Nat Med 1998; 4:1157-65; PMID:9771749; http://dx.doi.org/10.1038/2654
   PubMed Web of Science ®Google Scholar
• Collinge J, Clarke A. A general model of prion strains and their pathogenicity. Science 2007; 318:930-6; PMID:17991853; http://dx.doi.org/10.1126/science.1138718
   PubMed Web of Science ®Google Scholar
• Solforosi L, Milani M, Mancini N, Clementi M, Burioni R. A closer look at prion strains: Characterization and important implications. Prion 2013; 7:99-108; PMID:23357828; http://dx.doi.org/10.4161/pri.23490
   PubMed Web of Science ®Google Scholar
• Béringue V, Vilotte J, Laude H. Prion agent diversity and species barrier. Vet Res 2008; 39:47; PMID:18519020; http://dx.doi.org/10.1051/vetres:2008024
   PubMed Web of Science ®Google Scholar
• Baron GS, Hughson AG, Raymond GJ, Offerdahl DK, Barton KA, Raymond LD, Dorward DW, Caughey B. Effect of Glycans and GPI Anchor on Strain Dependent Conformations of Scrapie Prion Protein: Improved Purifications and IR Spectra. Biochemistry 2011; 50:4479-90; PMID:21539311; http://dx.doi.org/10.1021/bi2003907
   PubMed Web of Science ®Google Scholar
• Atarashi R, Sim VL, Nishida N, Caughey B, Katamine S. Prion strain-dependent differences in conversion of mutant prion proteins in cell culture. J Virol 2006; 80:7854-62; PMID:16873242; http://dx.doi.org/10.1128/JVI.00424-06
   PubMed Web of Science ®Google Scholar
• Morel N, Andréoletti O. Absolute and relative quantification of sheep brain prion protein (PrP) allelic variants by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 2007; 21:4093-100; PMID:18008391; http://dx.doi.org/10.1002/rcm.3317
   PubMed Web of Science ®Google Scholar
• Jacobs JG, Bossers A , Rezaei H, van Keulen LJM, McCutcheon S, Sklaviadis T, Lantier I, Berthon P, Lantier F, van Zijderveld FG, et al. Proteinase K-Resistant Material in ARR/VRQ Sheep Brain Affected with Classical Scrapie Is Composed Mainly of VRQ Prion Protein. J Virol 2011; 85:12537-46; PMID:21917981; http://dx.doi.org/10.1128/JVI.00448-11
   PubMed Web of Science ®Google Scholar
• Khan M, Sweeting B. Prion disease susceptibility is affected by β-structure folding propensity and local side-chain interactions in PrP. Proc Natl Acad Sci U S A 2010; 107:19808-13; PMID:21041683; http://dx.doi.org/10.1073/pnas.1005267107
   PubMed Web of Science ®Google Scholar
• Kirby L, Agarwal S, Graham JF, Goldmann W, Gill AC. Inverse correlation of thermal lability and conversion efficiency for five prion protein polymorphic variants. Biochemistry 2010; 49:1448-59; PMID:20085368; http://dx.doi.org/10.1021/bi901855z
   PubMed Web of Science ®Google Scholar
• Bujdoso R, Burke DF, Thackray AM. Structural differences between allelic variants of the ovine prion protein revealed by molecular dynamics simulations. Proteins 2005; 61:840-9; PMID:16252284; http://dx.doi.org/10.1002/prot.20755
   PubMed Web of Science ®Google Scholar
• Gill AC, Agarwal S, Pinheiro TJT, Graham JF. Structural requirements for efficient prion protein conversion: cofactors may promote a conversion-competent structure for PrP(C). Prion 2010; 4:235-42; PMID:20864807; http://dx.doi.org/10.4161/pri.4.4.13394
   PubMed Web of Science ®Google Scholar
• Pastore A, Zagari A. A structural overview of the vertebrate prion proteins. Prion 2007; 1:185-97; PMID:19164911; http://dx.doi.org/10.4161/pri.1.3.5281
   PubMed Web of Science ®Google Scholar
• Chakroun N, Prigent S, Dreiss CA, Noinville S, Chapuis C, Fraternali F, Rezaei H. The oligomerization properties of prion protein are restricted to the H2H3 domain. FASEB J 2010; 24:3222-31; PMID:20410442; http://dx.doi.org/10.1096/fj.09-153924
   PubMed Web of Science ®Google Scholar
• Rezaei H, Choiset Y, Eghiaian F, Treguer E, Mentre P, Debey P, Grosclaude J, Haertle T. Amyloidogenic Unfolding Intermediates Differentiate Sheep Prion Protein Variants. J Mol Biol 2002; 322:799-814; PMID:12270715; http://dx.doi.org/10.1016/S0022-2836(02)00856-2
   PubMed Web of Science ®Google Scholar
• Kanata E, Humphreys-Panagiotidis C, Giadinis ND, Papaioannou N, Arsenakis M, Sklaviadis T. Perspectives of a scrapie resistance breeding scheme targeting Q211, S146 and K222 caprine PRNP alleles in Greek goats. Vet Res 2014; 45:43; PMID:24717012; http://dx.doi.org/10.1186/1297-9716-45-43
   PubMed Web of Science ®Google Scholar
• Salta E, Kanata E, Ouzounis C, Gilch S, Schätzl H, Sklaviadis T. Assessing Proteinase K Resistance of Fish Prion Proteins in a Scrapie-Infected Mouse Neuroblastoma Cell Line. Viruses 2014; 6:4398-421; PMID:25402173; http://dx.doi.org/10.3390/v6114398
   PubMed Web of Science ®Google Scholar
• Nishida N, Harris DA, Vilette D, Laude H, Frobert Y, Grassi J, Casanova D, Milhavet O, Lehmann S. Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein. J Virol 2000; 74:320-5; PMID:10590120; http://dx.doi.org/10.1128/JVI.74.1.320-325.2000
   PubMed Web of Science ®Google Scholar
• Vorberg I, Buschmann A, Harmeyer S, Saalmüller A, Pfaff E, Groschup MH. A novel epitope for the specific detection of exogenous prion proteins in transgenic mice and transfected murine cell lines. Virology 1999; 255:26-31; PMID:10049818; http://dx.doi.org/10.1006/viro.1998.9561
   PubMed Web of Science ®Google Scholar