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Volumn 6, Issue 2, 2007, Pages 153-168

Potential of active and passive immunizations for the prevention and therapy of transmissible spongiform encephalopathies

Author keywords

Creutzfeldt Jakob disease; IgG; Immunization; Prion; Prophylaxis; Scrapie; sIgA; Therapy; Transmissible spongiform encephalopathies; Vaccination

Indexed keywords

CELL WALL SKELETON; CHOLERA TOXIN; CPG OLIGODEOXYNUCLEOTIDE; DNA VACCINE; FREUND ADJUVANT; HEAT LABILE ENTEROTOXIN; HEAT SHOCK PROTEIN 70; HELIX 1 PEPTIDE; IMS 1313; KEYHOLE LIMPET HEMOCYANIN; LIPOFECTIN; LYSOSOMAL INTEGRAL MEMBRANE PROTEIN 2; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2 BINDING PRION PROTEIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 6H4; MONOCLONAL ANTIBODY 7D9; MONOCLONAL ANTIBODY ICSM35; MONOCLONAL ANTIBODY PRION PROTEIN; MONTANIDE; PHOSPHORYL LIPID A; PRION PROTEIN; RECOMBINANT PRION PROTEIN 132-242; RECOMBINANT PRION PROTEIN 23-230; RECOMBINANT PRION PROTEIN 23-231; RECOMBINANT PRION PROTEIN 25-242; RECOMBINANT PRION PROTEIN 90-231; RECOMBINANT VACCINE; SALMONELLOSIS VACCINE; TREHALOSE DICHORYNOMYCOLATE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 34247234606     PISSN: 14760584     EISSN: 17448395     Source Type: Journal    
DOI: 10.1586/14760584.6.2.153     Document Type: Review
Times cited : (13)

References (99)
  • 1
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 216(4542), 136-144 (1982).
    • (1982) Science , vol.216 , Issue.4542 , pp. 136-144
    • Prusiner, S.B.1
  • 2
    • 26444509890 scopus 로고    scopus 로고
    • The prion gene is associated with human long-term memory
    • Papassotiropoulos A, Wollmer MA, Aguzzi A et al. The prion gene is associated with human long-term memory. Hum. Mol. Genet. 14(15), 2241-2246 (2005).
    • (2005) Hum. Mol. Genet , vol.14 , Issue.15 , pp. 2241-2246
    • Papassotiropoulos, A.1    Wollmer, M.A.2    Aguzzi, A.3
  • 3
    • 0037070220 scopus 로고    scopus 로고
    • Cellular prion protein: On the road for functions
    • Martins VR, Linden R, Prado MA et al. Cellular prion protein: on the road for functions. FEBS Lett. 512(1-3), 25-28 (2002).
    • (2002) FEBS Lett , vol.512 , Issue.1-3 , pp. 25-28
    • Martins, V.R.1    Linden, R.2    Prado, M.A.3
  • 4
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • Bueler H, Aguzzi A, Sailer A et al. Mice devoid of PrP are resistant to scrapie. Cell 73(7), 1339-1347 (1993).
    • (1993) Cell , vol.73 , Issue.7 , pp. 1339-1347
    • Bueler, H.1    Aguzzi, A.2    Sailer, A.3
  • 5
    • 0027491308 scopus 로고
    • Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies
    • Prusiner SB, Groth D, Serban A et al. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc. Natl Acad. Sci. USA 90(22), 10608-10612 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , Issue.22 , pp. 10608-10612
    • Prusiner, S.B.1    Groth, D.2    Serban, A.3
  • 6
    • 0034891027 scopus 로고    scopus 로고
    • Sympathetic innervation of lymphoreticular organs is rate limiting for prion neuroinvasion
    • Glatzel M, Heppner FL, Albers KM, Aguzzi A. Sympathetic innervation of lymphoreticular organs is rate limiting for prion neuroinvasion. Neuron 31(1), 25-34 (2001).
    • (2001) Neuron , vol.31 , Issue.1 , pp. 25-34
    • Glatzel, M.1    Heppner, F.L.2    Albers, K.M.3    Aguzzi, A.4
  • 7
    • 33646000833 scopus 로고    scopus 로고
    • Mabbott NA, Macpherson GG. Prions and their lethal journey to the brain. Nat. Rev. Microbiol. 4(3), 201-211 (2006). •Comprehensive overview of the pathogenesis of transmissible spongiform encephalopathies (TSE).
    • Mabbott NA, Macpherson GG. Prions and their lethal journey to the brain. Nat. Rev. Microbiol. 4(3), 201-211 (2006). •Comprehensive overview of the pathogenesis of transmissible spongiform encephalopathies (TSE).
  • 8
    • 0027332116 scopus 로고
    • Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J et al. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl Acad. Sci. USA 90(23), 10962-10966 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , Issue.23 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3
  • 9
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • McKinley MP, Bolton DC, Prusiner SB. A protease-resistant protein is a structural component of the scrapie prion. Cell 35(1), 57-62 (1983).
    • (1983) Cell , vol.35 , Issue.1 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 10
    • 0028252571 scopus 로고
    • Decontamination studies with the agents of bovine spongiform encephalopathy and scrapie
    • Taylor DM, Fraser H, McConnell I et al. Decontamination studies with the agents of bovine spongiform encephalopathy and scrapie. Arch. Virol. 139(3-4), 313-326 (1994).
    • (1994) Arch. Virol , vol.139 , Issue.3-4 , pp. 313-326
    • Taylor, D.M.1    Fraser, H.2    McConnell, I.3
  • 11
    • 0026031118 scopus 로고
    • Survival of scrapie virus after 3 years' interment
    • Brown P, Gajdusek DC. Survival of scrapie virus after 3 years' interment. Lancet 337(8736), 269-270 (1991).
    • (1991) Lancet , vol.337 , Issue.8736 , pp. 269-270
    • Brown, P.1    Gajdusek, D.C.2
  • 12
    • 33747040538 scopus 로고    scopus 로고
    • Iatrogenic Creutzfeldt-Jakob disease: The waning of an era
    • Brown P, Brandel JP, Preece M, Sato T. Iatrogenic Creutzfeldt-Jakob disease: the waning of an era. Neurology 67(3), 389-393 (2006).
    • (2006) Neurology , vol.67 , Issue.3 , pp. 389-393
    • Brown, P.1    Brandel, J.P.2    Preece, M.3    Sato, T.4
  • 13
    • 0342951746 scopus 로고    scopus 로고
    • A new variant of Creutzfeldt-Jakob disease in the UK
    • Will RG, Ironside JW, Zeidler M et al. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347(9006), 921-925 (1996).
    • (1996) Lancet , vol.347 , Issue.9006 , pp. 921-925
    • Will, R.G.1    Ironside, J.W.2    Zeidler, M.3
  • 14
    • 0031588178 scopus 로고    scopus 로고
    • New variant Creutzfeldt-Jakob disease: Neurological features and diagnostic tests
    • Zeidler M, Stewart GE, Barraclough CR et al. New variant Creutzfeldt-Jakob disease: neurological features and diagnostic tests. Lancet 350(9082), 903-907 (1997).
    • (1997) Lancet , vol.350 , Issue.9082 , pp. 903-907
    • Zeidler, M.1    Stewart, G.E.2    Barraclough, C.R.3
  • 15
    • 0029947694 scopus 로고    scopus 로고
    • BSE transmission to macaques
    • Lasmezas CI, Deslys JP, Demaimay R et al. BSE transmission to macaques. Nature 381(6585), 743-744 (1996).
    • (1996) Nature , vol.381 , Issue.6585 , pp. 743-744
    • Lasmezas, C.I.1    Deslys, J.P.2    Demaimay, R.3
  • 16
    • 0030775632 scopus 로고    scopus 로고
    • Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent
    • Bruce ME, Will RG, Ironside JW et al. Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent. Nature 389(6650), 498-501 (1997).
    • (1997) Nature , vol.389 , Issue.6650 , pp. 498-501
    • Bruce, M.E.1    Will, R.G.2    Ironside, J.W.3
  • 18
    • 33745440706 scopus 로고    scopus 로고
    • Kuru in the 21st century - an acquired human prion disease with very long incubation periods
    • Collinge J, Whitfield J, McKintosh E et al. Kuru in the 21st century - an acquired human prion disease with very long incubation periods. Lancet 367(9528), 2068-2074 (2006).
    • (2006) Lancet , vol.367 , Issue.9528 , pp. 2068-2074
    • Collinge, J.1    Whitfield, J.2    McKintosh, E.3
  • 19
    • 14744273321 scopus 로고    scopus 로고
    • Working with transmissible spongiform encephalopathy agents
    • Brown P, Abee CR. Working with transmissible spongiform encephalopathy agents. ILAR J. 46(1), 44-52 (2005).
    • (2005) ILAR J , vol.46 , Issue.1 , pp. 44-52
    • Brown, P.1    Abee, C.R.2
  • 20
    • 30344436691 scopus 로고    scopus 로고
    • Pathological prion protein in muscles of hamsters and mice infected with rodent-adapted BSE or vCJD
    • Thomzig A, Cardone F, Kruger D et al. Pathological prion protein in muscles of hamsters and mice infected with rodent-adapted BSE or vCJD. J. Gen. Virol. 87(Pt 1), 251-254 (2006).
    • (2006) J. Gen. Virol , vol.87 , Issue.PART 1 , pp. 251-254
    • Thomzig, A.1    Cardone, F.2    Kruger, D.3
  • 21
    • 33644554856 scopus 로고    scopus 로고
    • Prions in skeletal muscles of deer with chronic wasting disease
    • Angers RC, Browning SR, Seward TS et al. Prions in skeletal muscles of deer with chronic wasting disease. Science 311(5764), 1117 (2006).
    • (2006) Science , vol.311 , Issue.5764 , pp. 1117
    • Angers, R.C.1    Browning, S.R.2    Seward, T.S.3
  • 22
    • 13844259181 scopus 로고    scopus 로고
    • Chronic lymphocytic inflammation specifies the organ tropism of prions
    • Heikenwalder M, Zeller N, Seeger H et al. Chronic lymphocytic inflammation specifies the organ tropism of prions. Science 307(5712), 1107-1110 (2005).
    • (2005) Science , vol.307 , Issue.5712 , pp. 1107-1110
    • Heikenwalder, M.1    Zeller, N.2    Seeger, H.3
  • 23
    • 33749618609 scopus 로고    scopus 로고
    • Infectious prions in the saliva and blood of deer with chronic wasting disease
    • Mathiason CK, Powers JG, Dahmes SJ et al. Infectious prions in the saliva and blood of deer with chronic wasting disease. Science 314(5796), 133-136 (2006).
    • (2006) Science , vol.314 , Issue.5796 , pp. 133-136
    • Mathiason, C.K.1    Powers, J.G.2    Dahmes, S.J.3
  • 25
    • 0032567088 scopus 로고    scopus 로고
    • The host range of chronic wasting disease is altered on passage in ferrets
    • Bartz JC, Marsh RF, McKenzie DI, Aiken JM. The host range of chronic wasting disease is altered on passage in ferrets. Virology 251(2), 297-301 (1998).
    • (1998) Virology , vol.251 , Issue.2 , pp. 297-301
    • Bartz, J.C.1    Marsh, R.F.2    McKenzie, D.I.3    Aiken, J.M.4
  • 26
    • 2542629820 scopus 로고    scopus 로고
    • Chronic wasting disease and potential transmission to humans
    • Belay ED, Maddox RA, Williams ES et al. Chronic wasting disease and potential transmission to humans. Emerg. Infect. Dis.10(6), 977-984 (2004).
    • (2004) Emerg. Infect. Dis , vol.10 , Issue.6 , pp. 977-984
    • Belay, E.D.1    Maddox, R.A.2    Williams, E.S.3
  • 27
    • 0031929887 scopus 로고    scopus 로고
    • Effect of repeated oral infection of hamsters with scrapie
    • Diringer H, Roehmel J, Beekes M. Effect of repeated oral infection of hamsters with scrapie. J. Gen. Virol. 79(Pt 3), 609-612 (1998).
    • (1998) J. Gen. Virol , vol.79 , Issue.PART 3 , pp. 609-612
    • Diringer, H.1    Roehmel, J.2    Beekes, M.3
  • 28
    • 21644458458 scopus 로고    scopus 로고
    • High incidence of scrapie induced by repeated injections of subinfectious prion doses
    • Jacquemot C, Cuche C, Dormont D, Lazarini F. High incidence of scrapie induced by repeated injections of subinfectious prion doses. J. Virol. 79(14), 8904-8908 (2005).
    • (2005) J. Virol , vol.79 , Issue.14 , pp. 8904-8908
    • Jacquemot, C.1    Cuche, C.2    Dormont, D.3    Lazarini, F.4
  • 29
    • 0034797467 scopus 로고    scopus 로고
    • Transepithelial prion transport by M cells
    • Heppner FL, Christ AD, Klein MA et al. Transepithelial prion transport by M cells. Nat. Med. 7(9), 976-977 (2001).
    • (2001) Nat. Med , vol.7 , Issue.9 , pp. 976-977
    • Heppner, F.L.1    Christ, A.D.2    Klein, M.A.3
  • 30
    • 33645887847 scopus 로고    scopus 로고
    • Short-term study of the uptake of PrP(Sc) by the Peyer's patches in hamsters after oral exposure to scrapie
    • Bergstrom AL, Jensen TK, Heegaard PM et al. Short-term study of the uptake of PrP(Sc) by the Peyer's patches in hamsters after oral exposure to scrapie. J. Comp. Pathol. 134(2-3), 126-133 (2006).
    • (2006) J. Comp. Pathol , vol.134 , Issue.2-3 , pp. 126-133
    • Bergstrom, A.L.1    Jensen, T.K.2    Heegaard, P.M.3
  • 31
    • 0030576516 scopus 로고    scopus 로고
    • Epithelial M cells: Gateways for mucosal infection and immunization
    • Neutra MR, Frey A, Kraehenbuhl JP. Epithelial M cells: gateways for mucosal infection and immunization. Cell 86(3), 345-348 (1996).
    • (1996) Cell , vol.86 , Issue.3 , pp. 345-348
    • Neutra, M.R.1    Frey, A.2    Kraehenbuhl, J.P.3
  • 32
    • 0033987269 scopus 로고    scopus 로고
    • Early accumulation of pathological PrP in the enteric nervous system and gut-associated lymphoid tissue of hamsters orally infected with scrapie
    • Beekes M, McBride PA. Early accumulation of pathological PrP in the enteric nervous system and gut-associated lymphoid tissue of hamsters orally infected with scrapie. Neurosci. Lett. 278(3), 181-184 (2000).
    • (2000) Neurosci. Lett , vol.278 , Issue.3 , pp. 181-184
    • Beekes, M.1    McBride, P.A.2
  • 34
    • 0035321325 scopus 로고    scopus 로고
    • Dendritic cells express tight junction proteins and penetrate gut epithelial monolayers to sample bacteria
    • Rescigno M, Urbano M, Valzasina B et al. Dendritic cells express tight junction proteins and penetrate gut epithelial monolayers to sample bacteria. Nat. Immunol. 2(4), 361-367 (2001).
    • (2001) Nat. Immunol , vol.2 , Issue.4 , pp. 361-367
    • Rescigno, M.1    Urbano, M.2    Valzasina, B.3
  • 35
    • 33749623858 scopus 로고    scopus 로고
    • Degradation of scrapie associated prion protein (PrP(Sc)) by the gastrointestinal microbiota of cattle
    • Scherbel C, Pichner R, Groschup MH et al. Degradation of scrapie associated prion protein (PrP(Sc)) by the gastrointestinal microbiota of cattle. Vet. Res. 37(5), 695-703 (2006).
    • (2006) Vet. Res , vol.37 , Issue.5 , pp. 695-703
    • Scherbel, C.1    Pichner, R.2    Groschup, M.H.3
  • 36
    • 10644241804 scopus 로고    scopus 로고
    • Protease-resistant human prion protein and ferritin are cotransported across Caco-2 epithelial cells: Implications for species barrier in prion uptake from the intestine
    • Mishra RS, Basu S, Gu Y et al. Protease-resistant human prion protein and ferritin are cotransported across Caco-2 epithelial cells: implications for species barrier in prion uptake from the intestine. J. Neurosci. 24(50), 11280-11290 (2004).
    • (2004) J. Neurosci , vol.24 , Issue.50 , pp. 11280-11290
    • Mishra, R.S.1    Basu, S.2    Gu, Y.3
  • 37
    • 0242499506 scopus 로고    scopus 로고
    • Positioning of follicular dendritic cells within the spleen controls prion neuroinvasion
    • Prinz M, Heikenwalder M, Junt T et al. Positioning of follicular dendritic cells within the spleen controls prion neuroinvasion. Nature 425(6961), 957-962 (2003).
    • (2003) Nature , vol.425 , Issue.6961 , pp. 957-962
    • Prinz, M.1    Heikenwalder, M.2    Junt, T.3
  • 38
    • 33644836224 scopus 로고    scopus 로고
    • Mucosal vaccines: The promise and the challenge
    • Neutra MR, Kozlowski PA. Mucosal vaccines: the promise and the challenge. Nat. Rev. Immunol. 6(2), 148-158 (2006).
    • (2006) Nat. Rev. Immunol , vol.6 , Issue.2 , pp. 148-158
    • Neutra, M.R.1    Kozlowski, P.A.2
  • 39
    • 0036337774 scopus 로고    scopus 로고
    • Secretory component: A new role in secretory IgA-mediated immune exclusion in vivo
    • Phalipon A, Cardona A, Kraehenbuhl JP et al. Secretory component: a new role in secretory IgA-mediated immune exclusion in vivo. Immunity 17(1), 107-115 (2002).
    • (2002) Immunity , vol.17 , Issue.1 , pp. 107-115
    • Phalipon, A.1    Cardona, A.2    Kraehenbuhl, J.P.3
  • 40
    • 17644371966 scopus 로고    scopus 로고
    • Mucosal immunity and vaccines
    • Holmgren J, Czerkinsky C. Mucosal immunity and vaccines. Nat. Med. 11(Suppl. 4), S45-S53 (2005).
    • (2005) Nat. Med , vol.11 , Issue.SUPPL. 4
    • Holmgren, J.1    Czerkinsky, C.2
  • 41
    • 0035812752 scopus 로고    scopus 로고
    • Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies
    • Heppner FL, Musahl C, Arrighi I et al. Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies. Science 294(5540), 178-182 (2001).
    • (2001) Science , vol.294 , Issue.5540 , pp. 178-182
    • Heppner, F.L.1    Musahl, C.2    Arrighi, I.3
  • 42
    • 0242363656 scopus 로고    scopus 로고
    • Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis
    • Mallucci G, Dickinson A, Linehan J et al. Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Science 302(5646), 871-874 (2003).
    • (2003) Science , vol.302 , Issue.5646 , pp. 871-874
    • Mallucci, G.1    Dickinson, A.2    Linehan, J.3
  • 43
    • 0034856996 scopus 로고    scopus 로고
    • Modulation of proteinase-K resistant prion protein by prion peptide immunization
    • Souan L, Tal Y, Felling Y et al. Modulation of proteinase-K resistant prion protein by prion peptide immunization. Eur. J. Immunol. 31(8), 2338-2346 (2001).
    • (2001) Eur. J. Immunol , vol.31 , Issue.8 , pp. 2338-2346
    • Souan, L.1    Tal, Y.2    Felling, Y.3
  • 44
    • 0036849619 scopus 로고    scopus 로고
    • Induction of antibodies against murine full-length prion protein in wild-type mice
    • Koller MF, Grau T, Christen P. Induction of antibodies against murine full-length prion protein in wild-type mice. J. Neuroimmunol. 132(1-2), 113-116 (2002).
    • (2002) J. Neuroimmunol , vol.132 , Issue.1-2 , pp. 113-116
    • Koller, M.F.1    Grau, T.2    Christen, P.3
  • 45
    • 0036317750 scopus 로고    scopus 로고
    • Sigurdsson EM, Brown DR, Daniels M et al. Immunization delays the onset of prion disease in mice. Am. J. Pathol. 161(1), 13-17 (2002). •Demonstrates that an active systemic immunization is able to prolong the asymptomatic incubation phase after systemic infection with prions.
    • Sigurdsson EM, Brown DR, Daniels M et al. Immunization delays the onset of prion disease in mice. Am. J. Pathol. 161(1), 13-17 (2002). •Demonstrates that an active systemic immunization is able to prolong the asymptomatic incubation phase after systemic infection with prions.
  • 46
    • 4444325310 scopus 로고    scopus 로고
    • Humoral immune response to native eukaryotic prion protein correlates with anti-prion protection
    • Polymenidou M, Heppner FL, Pellicioli EC et al. Humoral immune response to native eukaryotic prion protein correlates with anti-prion protection. Proc. Natl Acad. Sci. USA 101(Suppl. 2), 14670-14676 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.SUPPL. 2 , pp. 14670-14676
    • Polymenidou, M.1    Heppner, F.L.2    Pellicioli, E.C.3
  • 47
    • 0037705352 scopus 로고    scopus 로고
    • Polyclonal anti-PrP auto-antibodies induced with dimeric PrP interfere efficiently with PrPSc propagation in prion-infected cells
    • Gilch S, Wopfner F, Renner-Muller I et al. Polyclonal anti-PrP auto-antibodies induced with dimeric PrP interfere efficiently with PrPSc propagation in prion-infected cells. J. Biol. Chem. 278(20), 18524-18531 (2003).
    • (2003) J. Biol. Chem , vol.278 , Issue.20 , pp. 18524-18531
    • Gilch, S.1    Wopfner, F.2    Renner-Muller, I.3
  • 48
    • 20144371828 scopus 로고    scopus 로고
    • Circumventing tolerance to the prion protein (PrP): Vaccination with PrP-displaying retrovirus particles induces humoral immune responses against the native form of cellular PrP
    • Nikles D, Bach P, Boller K et al. Circumventing tolerance to the prion protein (PrP): vaccination with PrP-displaying retrovirus particles induces humoral immune responses against the native form of cellular PrP. J. Virol. 79(7), 4033-4042 (2005).
    • (2005) J. Virol , vol.79 , Issue.7 , pp. 4033-4042
    • Nikles, D.1    Bach, P.2    Boller, K.3
  • 49
    • 33645118457 scopus 로고    scopus 로고
    • Generation of antibodies against bovine recombinant prion protein in various strains of mice
    • Andrievskaia O, McRae H, Elmgren C et al. Generation of antibodies against bovine recombinant prion protein in various strains of mice. Clin. Vaccine Immunol. 13(1), 98-105 (2006).
    • (2006) Clin. Vaccine Immunol , vol.13 , Issue.1 , pp. 98-105
    • Andrievskaia, O.1    McRae, H.2    Elmgren, C.3
  • 50
    • 33845574428 scopus 로고    scopus 로고
    • Immunization with recombinant bovine but not mouse prion protein delays the onset of disease in mice inoculated with a mouse-adapted prion
    • Ishibashi D, Yamanaka H, Yamaguchi N et al. Immunization with recombinant bovine but not mouse prion protein delays the onset of disease in mice inoculated with a mouse-adapted prion. Vaccine 25(6), 985-992 (2006).
    • (2006) Vaccine , vol.25 , Issue.6 , pp. 985-992
    • Ishibashi, D.1    Yamanaka, H.2    Yamaguchi, N.3
  • 51
    • 2142706520 scopus 로고    scopus 로고
    • Breaking immune tolerance to the prion protein using prion protein peptides plus oligodeoxynucleotide-CpG in mice
    • Rosset MB, Ballerini C, Gregoire S et al. Breaking immune tolerance to the prion protein using prion protein peptides plus oligodeoxynucleotide-CpG in mice. J. Immunol. 172(9), 5168-5174 (2004).
    • (2004) J. Immunol , vol.172 , Issue.9 , pp. 5168-5174
    • Rosset, M.B.1    Ballerini, C.2    Gregoire, S.3
  • 52
    • 27744463376 scopus 로고    scopus 로고
    • The murine B cell repertoire is severely selected against endogenous cellular prion protein
    • Gregoire S, Bergot AS, Feraudet C et al. The murine B cell repertoire is severely selected against endogenous cellular prion protein. J. Immunol. 175(10), 6443-6449 (2005).
    • (2005) J. Immunol , vol.175 , Issue.10 , pp. 6443-6449
    • Gregoire, S.1    Bergot, A.S.2    Feraudet, C.3
  • 53
    • 12244259034 scopus 로고    scopus 로고
    • Complete Freund's adjuvant immunization prolongs survival in experimental prion disease in mice
    • Tal Y, Souan L, Cohen IR et al. Complete Freund's adjuvant immunization prolongs survival in experimental prion disease in mice. J. Neurosci. Res. 71(2), 286-290 (2003).
    • (2003) J. Neurosci. Res , vol.71 , Issue.2 , pp. 286-290
    • Tal, Y.1    Souan, L.2    Cohen, I.R.3
  • 54
    • 34247214020 scopus 로고    scopus 로고
    • Antibodies to a nonconjugated prion protein peptide 95-123 interfere with PrP(Sc) propagation in prion-infected cells
    • DOI: 10.1007/s10571-006- 9108-y , Epub ahead of print
    • Oboznaya MB, Gilch S, Titova MA et al. Antibodies to a nonconjugated prion protein peptide 95-123 interfere with PrP(Sc) propagation in prion-infected cells. Cell. Mol. Neurobiol. DOI: 10.1007/s10571-006- 9108-y (2007) (Epub ahead of print).
    • (2007) Cell. Mol. Neurobiol
    • Oboznaya, M.B.1    Gilch, S.2    Titova, M.A.3
  • 55
    • 0142195845 scopus 로고    scopus 로고
    • Generation of antibodies against prion protein in wild-type mice via helix 1 peptide immunization
    • Arbel M, Lavie V, Solomon B. Generation of antibodies against prion protein in wild-type mice via helix 1 peptide immunization. J. Neuroimmunol. 144(1-2), 38-45 (2003).
    • (2003) J. Neuroimmunol , vol.144 , Issue.1-2 , pp. 38-45
    • Arbel, M.1    Lavie, V.2    Solomon, B.3
  • 56
    • 3543034084 scopus 로고    scopus 로고
    • Multiple antigenic peptides facilitate generation of anti-prion antibodies
    • Bainbridge J, Jones N, Walker B. Multiple antigenic peptides facilitate generation of anti-prion antibodies. Clin. Exp. Immunol. 137(2), 298-304 (2004).
    • (2004) Clin. Exp. Immunol , vol.137 , Issue.2 , pp. 298-304
    • Bainbridge, J.1    Jones, N.2    Walker, B.3
  • 57
    • 0141782730 scopus 로고    scopus 로고
    • Schwarz A, Kratke O, Burwinkel M et al.. Immunisation with a synthetic prion protein-derived peptide prolongs survival times of mice orally exposed to the scrapie agent. Neurosci. Lett. 350(3), 187-189 (2003). •Demonstrates that an active systemic immunization can have a prophylactic effect on oral acquisition of TSE.
    • Schwarz A, Kratke O, Burwinkel M et al.. Immunisation with a synthetic prion protein-derived peptide prolongs survival times of mice orally exposed to the scrapie agent. Neurosci. Lett. 350(3), 187-189 (2003). •Demonstrates that an active systemic immunization can have a prophylactic effect on oral acquisition of TSE.
  • 58
    • 20144377217 scopus 로고    scopus 로고
    • Decrease in pathology and progression of scrapie after immunisation with synthetic prion protein peptides in hamsters
    • Magri G, Clerici M, Dall'ara P et al. Decrease in pathology and progression of scrapie after immunisation with synthetic prion protein peptides in hamsters. Vaccine 23(22), 2862-2868 (2005).
    • (2005) Vaccine , vol.23 , Issue.22 , pp. 2862-2868
    • Magri, G.1    Clerici, M.2    Dall'ara, P.3
  • 59
    • 14944352532 scopus 로고    scopus 로고
    • Testing the possibility to protect bovine PrPC transgenic Swiss mice against bovine PrPSc infection by DNA vaccination using recombinant plasmid vectors harboring and expressing the complete or partial cDNA sequences of bovine PrPC
    • Muller S, Kehm R, Handermann M et al. Testing the possibility to protect bovine PrPC transgenic Swiss mice against bovine PrPSc infection by DNA vaccination using recombinant plasmid vectors harboring and expressing the complete or partial cDNA sequences of bovine PrPC. Virus Genes 30(2), 279-296 (2005).
    • (2005) Virus Genes , vol.30 , Issue.2 , pp. 279-296
    • Muller, S.1    Kehm, R.2    Handermann, M.3
  • 60
    • 33749483690 scopus 로고    scopus 로고
    • DNA vaccination can break immunological tolerance to PrP in wild-type mice and attenuates prion disease after intracerebral challenge
    • Fernandez-Borges N, Brun A, Whitton JL et al. DNA vaccination can break immunological tolerance to PrP in wild-type mice and attenuates prion disease after intracerebral challenge. J. Virol. 80(20), 9970-9976 (2006).
    • (2006) J. Virol , vol.80 , Issue.20 , pp. 9970-9976
    • Fernandez-Borges, N.1    Brun, A.2    Whitton, J.L.3
  • 61
    • 21144432949 scopus 로고    scopus 로고
    • Goni F, Knudsen E, Schreiber F et al. Mucosal vaccination delays or prevents prion infection via an oral route. Neuroscience 133(2), 413-421 (2005). •Demonstrates that an active mucosal immunization can protect against TSE.
    • Goni F, Knudsen E, Schreiber F et al. Mucosal vaccination delays or prevents prion infection via an oral route. Neuroscience 133(2), 413-421 (2005). •Demonstrates that an active mucosal immunization can protect against TSE.
  • 62
    • 32344443856 scopus 로고    scopus 로고
    • Bade S, Baier M, Boetel T, Frey A. Intranasal immunization of Balb/c mice against prion protein attenuates orally acquired transmissible spongiform encephalopathy. Vaccine 24(9), 1242-1253 (2006). •Demonstrates that an active mucosal immunization attenuates the disease and that the stability of the prion protein (PrP) antigen is crucial for the induction of anti-PrP antibodies via a mucosal vaccination.
    • Bade S, Baier M, Boetel T, Frey A. Intranasal immunization of Balb/c mice against prion protein attenuates orally acquired transmissible spongiform encephalopathy. Vaccine 24(9), 1242-1253 (2006). •Demonstrates that an active mucosal immunization attenuates the disease and that the stability of the prion protein (PrP) antigen is crucial for the induction of anti-PrP antibodies via a mucosal vaccination.
  • 63
    • 0037813124 scopus 로고    scopus 로고
    • Prion diseases: Infectious and lethal doses following oral challenge
    • Baier M, Norley S, Schultz J et al. Prion diseases: infectious and lethal doses following oral challenge. J. Gen. Virol. 84(Pt 7), 1927-1929 (2003).
    • (2003) J. Gen. Virol , vol.84 , Issue.PART 7 , pp. 1927-1929
    • Baier, M.1    Norley, S.2    Schultz, J.3
  • 64
    • 33644886008 scopus 로고    scopus 로고
    • Enhanced mucosal immunogenicity of prion protein following fusion with B subunit of Escherichia coli heat-labile enterotoxin
    • Yamanaka H, Ishibashi D, Yamaguchi N et al. Enhanced mucosal immunogenicity of prion protein following fusion with B subunit of Escherichia coli heat-labile enterotoxin. Vaccine 24(15), 2815-2823 (2006).
    • (2006) Vaccine , vol.24 , Issue.15 , pp. 2815-2823
    • Yamanaka, H.1    Ishibashi, D.2    Yamaguchi, N.3
  • 65
    • 0037461583 scopus 로고    scopus 로고
    • Anti-prion antibodies for prophylaxis following prion exposure in mice
    • Sigurdsson EM, Sy MS, Li R et al. Anti-prion antibodies for prophylaxis following prion exposure in mice. Neurosci. Lett. 336(3), 185-187 (2003).
    • (2003) Neurosci. Lett , vol.336 , Issue.3 , pp. 185-187
    • Sigurdsson, E.M.1    Sy, M.S.2    Li, R.3
  • 66
    • 33744478405 scopus 로고    scopus 로고
    • Clearance and prevention of prion infection in cell culture by anti-PrP antibodies
    • Pankiewicz J, Prelli F, Sy MS et al. Clearance and prevention of prion infection in cell culture by anti-PrP antibodies. Eur. J. Neurosci. 23(10), 2635-2647 (2006).
    • (2006) Eur. J. Neurosci , vol.23 , Issue.10 , pp. 2635-2647
    • Pankiewicz, J.1    Prelli, F.2    Sy, M.S.3
  • 67
    • 0037422133 scopus 로고    scopus 로고
    • White AR, Enever P, Tayebi M et al. Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature 422(6927), 80-83 (2003). •Demonstrates that repeated passive immunizations with high doses of anti-PrP antibodies can clear the infection and protect from disease.
    • White AR, Enever P, Tayebi M et al. Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature 422(6927), 80-83 (2003). •Demonstrates that repeated passive immunizations with high doses of anti-PrP antibodies can clear the infection and protect from disease.
  • 68
    • 0023499868 scopus 로고
    • Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins
    • Kascsak RJ, Rubenstein R, Merz PA et al. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J. Virol. 61(12), 3688-3693 (1987).
    • (1987) J. Virol , vol.61 , Issue.12 , pp. 3688-3693
    • Kascsak, R.J.1    Rubenstein, R.2    Merz, P.A.3
  • 69
    • 14844339706 scopus 로고    scopus 로고
    • Protein conformation significantly influences immune responses to prion protein
    • Khalili-Shirazi A, Quaratino S, Londei M et al. Protein conformation significantly influences immune responses to prion protein. J. Immunol. 174(6), 3256-3263 (2005).
    • (2005) J. Immunol , vol.174 , Issue.6 , pp. 3256-3263
    • Khalili-Shirazi, A.1    Quaratino, S.2    Londei, M.3
  • 70
    • 25144445863 scopus 로고    scopus 로고
    • Inhibition of prion propagation in scrapie-infected mouse neuroblastoma cell lines using mouse monoclonal antibodies against prion protein
    • Miyamoto K, Nakamura N, Aosasa M et al. Inhibition of prion propagation in scrapie-infected mouse neuroblastoma cell lines using mouse monoclonal antibodies against prion protein. Biochem. Biophys. Res. Commun. 335(1), 197-204 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.335 , Issue.1 , pp. 197-204
    • Miyamoto, K.1    Nakamura, N.2    Aosasa, M.3
  • 71
    • 0030613755 scopus 로고    scopus 로고
    • Prion (PrPSc)-specific epitope defined by a monoclonal antibody
    • Korth C, Stierli B, Streit P et al. Prion (PrPSc)-specific epitope defined by a monoclonal antibody. Nature 390(6655), 74-77 (1997).
    • (1997) Nature , vol.390 , Issue.6655 , pp. 74-77
    • Korth, C.1    Stierli, B.2    Streit, P.3
  • 72
    • 0035979274 scopus 로고    scopus 로고
    • Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody
    • Enari M, Flechsig E, Weissmann C. Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc. Natl Acad. Sci. USA 98(16), 9295-9299 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , Issue.16 , pp. 9295-9299
    • Enari, M.1    Flechsig, E.2    Weissmann, C.3
  • 73
    • 1942519718 scopus 로고    scopus 로고
    • Anti-PrP antibodies block PrPSc replication in prion-infected cell cultures by accelerating PrPC degradation
    • Perrier V, Solassol J, Crozet C et al. Anti-PrP antibodies block PrPSc replication in prion-infected cell cultures by accelerating PrPC degradation. J. Neurochem. 89(2), 454-463 (2004).
    • (2004) J. Neurochem , vol.89 , Issue.2 , pp. 454-463
    • Perrier, V.1    Solassol, J.2    Crozet, C.3
  • 74
    • 1542270865 scopus 로고    scopus 로고
    • Antigenic characterization of an abnormal isoform of prion protein using a new diverse panel of monoclonal antibodies
    • Kim CL, Umetani A, Matsui T et al. Antigenic characterization of an abnormal isoform of prion protein using a new diverse panel of monoclonal antibodies. Virology 320(1), 40-51 (2004).
    • (2004) Virology , vol.320 , Issue.1 , pp. 40-51
    • Kim, C.L.1    Umetani, A.2    Matsui, T.3
  • 75
    • 7444235958 scopus 로고    scopus 로고
    • Cell-surface retention of PrPC by anti-PrP antibody prevents protease-resistant PrP formation
    • Kim CL, Karino A, Ishiguro N et al. Cell-surface retention of PrPC by anti-PrP antibody prevents protease-resistant PrP formation. J. Gen. Virol. 85(Pt 11), 3473-3482 (2004).
    • (2004) J. Gen. Virol , vol.85 , Issue.PART 11 , pp. 3473-3482
    • Kim, C.L.1    Karino, A.2    Ishiguro, N.3
  • 76
    • 15744401372 scopus 로고    scopus 로고
    • Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells
    • Feraudet C, Morel N, Simon S et al. Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells. J. Biol. Chem. 280(12), 11247-11258 (2005).
    • (2005) J. Biol. Chem , vol.280 , Issue.12 , pp. 11247-11258
    • Feraudet, C.1    Morel, N.2    Simon, S.3
  • 77
    • 4544359288 scopus 로고    scopus 로고
    • PrPSc binding antibodies are potent inhibitors of prion replication in cell lines
    • Beringue V, Vilette D, Mallinson G et al. PrPSc binding antibodies are potent inhibitors of prion replication in cell lines. J. Biol. Chem. 279(38), 39671-39676 (2004).
    • (2004) J. Biol. Chem , vol.279 , Issue.38 , pp. 39671-39676
    • Beringue, V.1    Vilette, D.2    Mallinson, G.3
  • 78
    • 0029587683 scopus 로고
    • The immunogenicity of the 7E3 murine monoclonal Fab antibody fragment variable region is dramatically reduced in humans by substitution of human for murine constant regions
    • Knight DM, Wagner C, Jordan R et al. The immunogenicity of the 7E3 murine monoclonal Fab antibody fragment variable region is dramatically reduced in humans by substitution of human for murine constant regions. Mol. Immunol. 32(16), 1271-1281 (1995).
    • (1995) Mol. Immunol , vol.32 , Issue.16 , pp. 1271-1281
    • Knight, D.M.1    Wagner, C.2    Jordan, R.3
  • 79
    • 0035899413 scopus 로고    scopus 로고
    • Antibodies inhibit prion propagation and clear cell cultures of prion infectivity
    • Peretz D, Williamson RA, Kaneko K et al. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412(6848), 739-743 (2001).
    • (2001) Nature , vol.412 , Issue.6848 , pp. 739-743
    • Peretz, D.1    Williamson, R.A.2    Kaneko, K.3
  • 80
    • 12144291519 scopus 로고    scopus 로고
    • Cross-linking cellular prion protein triggers neuronal apoptosis in vivo
    • Solforosi L, Criado JR, McGavern DB et al. Cross-linking cellular prion protein triggers neuronal apoptosis in vivo. Science 303(5663), 1514-1516 (2004).
    • (2004) Science , vol.303 , Issue.5663 , pp. 1514-1516
    • Solforosi, L.1    Criado, J.R.2    McGavern, D.B.3
  • 81
    • 20744448499 scopus 로고    scopus 로고
    • Paracrine inhibition of prion propagation by anti-PrP single-chain Fv miniantibodies
    • Donofrio G, Heppner FL, Polymenidou M, Musahl C, Aguzzi A. Paracrine inhibition of prion propagation by anti-PrP single-chain Fv miniantibodies. J. Virol. 79(13), 8330-8338 (2005).
    • (2005) J. Virol , vol.79 , Issue.13 , pp. 8330-8338
    • Donofrio, G.1    Heppner, F.L.2    Polymenidou, M.3    Musahl, C.4    Aguzzi, A.5
  • 82
    • 12844260131 scopus 로고    scopus 로고
    • Trapping prion protein in the endoplasmic reticulum impairs PrPC maturation and prevents PrPSc accumulation
    • Cardinale A, Filesi I, Vetrugno V et al. Trapping prion protein in the endoplasmic reticulum impairs PrPC maturation and prevents PrPSc accumulation. J. Biol. Chem. 280(1), 685-694 (2005).
    • (2005) J. Biol. Chem , vol.280 , Issue.1 , pp. 685-694
    • Cardinale, A.1    Filesi, I.2    Vetrugno, V.3
  • 83
    • 27844578208 scopus 로고    scopus 로고
    • KDEL-tagged anti-prion intrabodies impair PrP lysosomal degradation and inhibit scrapie infectivity
    • Vetrugno V, Cardinale A, Filesi I et al. KDEL-tagged anti-prion intrabodies impair PrP lysosomal degradation and inhibit scrapie infectivity. Biochem. Biophys. Res. Commun. 338(4), 1791-1797 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.338 , Issue.4 , pp. 1791-1797
    • Vetrugno, V.1    Cardinale, A.2    Filesi, I.3
  • 84
    • 0034907372 scopus 로고    scopus 로고
    • Omalizumab, anti-IgE recombinant humanized monoclonal antibody, for the treatment of severe allergic asthma
    • Busse W, Corren J, Lanier BQ et al. Omalizumab, anti-IgE recombinant humanized monoclonal antibody, for the treatment of severe allergic asthma. J. Allergy Clin. Immunol. 108(2), 184-190 (2001).
    • (2001) J. Allergy Clin. Immunol , vol.108 , Issue.2 , pp. 184-190
    • Busse, W.1    Corren, J.2    Lanier, B.Q.3
  • 85
    • 0038717543 scopus 로고    scopus 로고
    • A prion protein epitope selective for the pathologically misfolded conformation
    • Paramithiotis E, Pinard M, Lawton T et al. A prion protein epitope selective for the pathologically misfolded conformation. Nat. Med. 9(7), 893-899 (2003).
    • (2003) Nat. Med , vol.9 , Issue.7 , pp. 893-899
    • Paramithiotis, E.1    Pinard, M.2    Lawton, T.3
  • 86
    • 0031710237 scopus 로고    scopus 로고
    • Mapping the prion protein using recombinant antibodies
    • Williamson RA, Peretz D, Pinilla C et al. Mapping the prion protein using recombinant antibodies. J. Virol. 72(11), 9413-9418 (1998).
    • (1998) J. Virol , vol.72 , Issue.11 , pp. 9413-9418
    • Williamson, R.A.1    Peretz, D.2    Pinilla, C.3
  • 87
    • 33744954409 scopus 로고    scopus 로고
    • Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay
    • Novitskaya V, Makarava N, Bellon A et al. Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay. J. Biol. Chem. 281(22), 15536-15545 (2006).
    • (2006) J. Biol. Chem , vol.281 , Issue.22 , pp. 15536-15545
    • Novitskaya, V.1    Makarava, N.2    Bellon, A.3
  • 88
    • 13144256747 scopus 로고    scopus 로고
    • Prion protein expression in different species: Analysis with a panel of new mAbs
    • Zanusso G, Liu D, Ferrari S et al. Prion protein expression in different species: analysis with a panel of new mAbs. Proc. Natl Acad. Sci. USA 95(15), 8812-8816 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , Issue.15 , pp. 8812-8816
    • Zanusso, G.1    Liu, D.2    Ferrari, S.3
  • 89
    • 0034682866 scopus 로고    scopus 로고
    • Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus
    • Li R, Liu T, Wong BS et al. Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus. J. Mol. Biol. 301(3), 567-573 (2000).
    • (2000) J. Mol. Biol , vol.301 , Issue.3 , pp. 567-573
    • Li, R.1    Liu, T.2    Wong, B.S.3
  • 90
    • 4444356433 scopus 로고    scopus 로고
    • Epitope scanning reveals gain and loss of strain specific antibody binding epitopes associated with the conversion of normal cellular prion to scrapie prion
    • Pan T, Li R, Kang SC et al. Epitope scanning reveals gain and loss of strain specific antibody binding epitopes associated with the conversion of normal cellular prion to scrapie prion. J. Neurochem. 90(5), 1205-1217 (2004).
    • (2004) J. Neurochem , vol.90 , Issue.5 , pp. 1205-1217
    • Pan, T.1    Li, R.2    Kang, S.C.3
  • 91
    • 11144247721 scopus 로고    scopus 로고
    • Biochemical fingerprints of prion infection: Accumulations of aberrant full-length and N-terminally truncated PrP species are common features in mouse prion disease
    • Pan T, Wong P, Chang B et al. Biochemical fingerprints of prion infection: accumulations of aberrant full-length and N-terminally truncated PrP species are common features in mouse prion disease. J. Virol. 79(2), 934-943 (2005).
    • (2005) J. Virol , vol.79 , Issue.2 , pp. 934-943
    • Pan, T.1    Wong, P.2    Chang, B.3
  • 92
    • 0042823437 scopus 로고    scopus 로고
    • Regional heterogeneity of cellular prion protein isoforms in the mouse brain
    • Beringue V, Mallinson G, Kaisar M et al. Regional heterogeneity of cellular prion protein isoforms in the mouse brain. Brain 126(Pt 9), 2065-2073 (2003).
    • (2003) Brain , vol.126 , Issue.PART 9 , pp. 2065-2073
    • Beringue, V.1    Mallinson, G.2    Kaisar, M.3
  • 93
    • 34247201097 scopus 로고    scopus 로고
    • Number of cases of BSE reported in the UK
    • World organization for animal health OIE
    • World organization for animal health (OIE). Number of cases of BSE reported in the UK www.oie.int/eng/info/en_esbru.htm
  • 94
    • 0008780284 scopus 로고    scopus 로고
    • World organization for animal health OIE
    • World organization for animal health (OIE). Number of reported cases of BSE worldwide www.oie.int/eng/info/en_esbmonde.htm
    • Number of reported cases of BSE worldwide
  • 95
    • 34247191326 scopus 로고    scopus 로고
    • EUROPA. Food safety. Biological safety of Food - BSE ec.europa.eu/food/ food/biosafety/bse/index_en.htm
  • 96
    • 34247223250 scopus 로고    scopus 로고
    • Risk assessment on BSE in cattle in Canada
    • Canadian Food Inspection Agency
    • Canadian Food Inspection Agency. Risk assessment on BSE in cattle in Canada. Part C: risk estimation www.inspection.gc.ca/english/sci/ahra/bseris/ bserisc2e.shtml
    • Part C: Risk estimation
  • 99
    • 34247196192 scopus 로고    scopus 로고
    • World organization for animal health OIE
    • World organization for animal health (OIE) www.oie.int


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