Could immunomodulation be used to prevent prion diseases?

References

• Collee JG, Bradley R. BSE: a decade on. Lancet349, 636–641 (1997).
   PubMed Web of Science ®Google Scholar
• Harman JL, Silva CJ. Bovine spongiform encephalopathy. J. Am. Vet. Med. Assoc.234(1), 59–72 (2009).
   PubMedGoogle Scholar
• Mackay GA, Knight RS, Ironside JW. The molecular epidemiology of variant CJD. Int. J. Mol. Epidemiol. Genet.2(3), 217–227 (2011).
   PubMedGoogle Scholar
• Garske T, Ghani AC. Uncertainty in the tail of the variant Creutzfeldt–Jakob disease epidemic in the UK. PLoS One5(12), e15626 (2010).
   Google Scholar
• Hilton DA, Ghani AC, Conyers L et al. Prevalence of lymphoreticular prion protein accumulation in UK tissue samples. J. Pathol.203(3), 733–739 (2004).
   PubMed Web of Science ®Google Scholar
• Hilton DA. Pathogenesis and prevalence of variant Creutzfeldt–Jakob disease. J. Pathol.208(2), 134–141 (2006).
   PubMed Web of Science ®Google Scholar
• Clewley JP, Kelly CM, Andrews N et al. Prevalence of disease related prion protein in anonymous tonsil specimens in Britain: cross sectional opportunistic survey. Brit. Med. J.338, b1442 (2009).
   PubMed Web of Science ®Google Scholar
• de Marco MF, Linehan J, Gill ON, Clewley JP, Brandner S. Large-scale immunohistochemical examination for lymphoreticular prion protein in tonsil specimens collected in Britain. J. Pathol.222(4), 380–387 (2010).
   PubMedGoogle Scholar
• Brown P, Brandel JP, Preese M, Sato T. Iatrogenic Creutzfeldt–Jakob disease: the waning of an era. Neurology67(3), 389–393 (2006).
   PubMed Web of Science ®Google Scholar
• Ironside JW. Variant Creutzfeldt–Jakob disease. Haemophilia16(Suppl. 5), 175–180 (2010).
   PubMed Web of Science ®Google Scholar
• Brown P. Transmissible spongiform encephalopathy in the 21st century: neuroscience for the clinical neurologist. Neurology70(9), 713–722 (2008).
   PubMed Web of Science ®Google Scholar
• Peden AH, Ritchie DL, Ironside JW. Risks of transmission of variant Creutzfeldt–Jakob disease by blood transfusion. Folia Neuropathol.43(4), 271–278 (2005).
   PubMedGoogle Scholar
• Jones M, Peden AH, Yull H et al. Human platelets as a substrate source for the in vitro amplification of the abnormal prion protein (PrP) associated with variant Creutzfeldt–Jakob disease. Transfusion49(2), 376–384 (2009).
   PubMedGoogle Scholar
• Puopolo M, Ladogana A, Vetrugno V, Pocchiari M. Transmission of sporadic Creutzfeldt–Jakob disease by blood transfusion: risk factor or possible biases. Transfusion51(7), 1556–1566 (2011).
   PubMedGoogle Scholar
• Zaman SM, Hill FG, Palmer B et al. The risk of variant Creutzfeldt–Jakob disease among UK patients with bleeding disorders, known to have received potentially contaminated plasma products. Haemophilia17(6), 931–937 (2011).
   PubMed Web of Science ®Google Scholar
• Edgeworth JA, Farmer M, Sicilia A et al. Detection of prion infection in variant Creutzfeldt–Jakob disease: a blood-based assay. Lancet377(9764), 487–493 (2011).
   PubMed Web of Science ®Google Scholar
• Peden AH, McGuire LI, Appleford NE et al. Sensitive and specific detection of sporadic Creutzfeldt–Jakob disease brain prion protein using real-time quaking induced conversion. J. Gen. Virol. doi: 10.1099/vir.0.033365-0 (2011) (Epub ahead of print).
   PubMedGoogle Scholar
• Bishop MT, Hart P, Aitchison L et al. Predicting susceptibility and incubation time of human-to-human transmission of vCJD. Lancet Neurol.5(5), 393–398 (2006).
   PubMed Web of Science ®Google Scholar
• Clarke P, Will RG, Ghani AC. Is there the potential for an epidemic of variant Creutzfeldt–Jakob disease via blood transfusion in the UK? J. R. Soc. Interface4(15), 675–684 (2007).
   PubMed Web of Science ®Google Scholar
• Tranulis MA, Benestad SL, Baron T, Kretzschmar H. Atypical prion diseases in humans and animals. Top. Curr. Chem.305, 23–50 (2011).
   PubMed Web of Science ®Google Scholar
• Kong Q, Zheng M, Casalone C et al. Evaluation of the human transmission risk of an atypical bovine spongiform encephalopathy prion strain. J. Virol.82(7), 3697–3701 (2008).
   PubMed Web of Science ®Google Scholar
• Casalone C, Zanusso G, Acutis P et al. Identification of a second bovine amyloidotic spongiform encephalopathy: molecular similarities with sporadic Creutzfeldt–Jakob disease. Proc. Natl Acad. Sci. USA101(9), 3065–3070 (2004).
   PubMed Web of Science ®Google Scholar
• Biacabe AG, Jacobs JG, Bencsik A, Langeveld JP, Baron TG. H-type bovine spongiform encephalopathy: complex molecular features and similarities with human prion diseases. Prion1(1), 61–68 (2007).
   PubMed Web of Science ®Google Scholar
• Comoy EE, Casalone C, Lescoutra-Etchegaray N et al. Atypical BSE (BASE) transmitted from asymptomatic aging cattle to a primate. PLoS One3(8), e3017 (2008).
   PubMed Web of Science ®Google Scholar
• Beringue V, Herzog L, Reine F et al. Transmission of atypical bovine prions to mice transgenic for human prion protein. Emerg. Infect. Dis.14(12), 1898–1901 (2008).
   PubMed Web of Science ®Google Scholar
• Williams ES. Chronic wasting disease. Vet. Pathol.42(5), 530–549 (2005).
   PubMed Web of Science ®Google Scholar
• Aguzzi A, Sigurdson CJ. Antiprion immunotherapy: to suppress or to stimulate? Nat. Rev. Immunol.4(9), 725–736 (2004).
   PubMed Web of Science ®Google Scholar
• Sigurdson CJ. A prion disease of cervids: chronic wasting disease. Vet. Res.39(4), 41 (2008).
   PubMed Web of Science ®Google Scholar
• Gilch S, Chitoor N, Taguchi Y, Stuart M, Jewell JE, Schatzl HM. Chronic wasting disease. Top. Curr. Chem.305, 51–77 (2011).
   PubMed Web of Science ®Google Scholar
• Williams ES, Young S. Chronic wasting disease of captive mule deer: a spongiform encephalopathy. J. Wildl. Dis.16(1), 89–98 (1980).
   PubMed Web of Science ®Google Scholar
• Williams ES, Young S. Spongiform encephalopathy of Rocky Mountain elk. J. Wildl. Dis.18(4), 465–471 (1982).
   PubMed Web of Science ®Google Scholar
• Beekes M, McBride PA. The spread of prions through the body in naturally acquired transmissible spongiform encephalopathies. FEBS J.274(3), 588–605 (2007).
   PubMed Web of Science ®Google Scholar
• Safar JG, Lessard P, Tamguney G et al. Transmission and detection of prions in feces. J. Infect. Dis.198(1), 81–89 (2008).
   PubMed Web of Science ®Google Scholar
• Belay ED, Maddox RA, Williams ES, Miller MW, Gambetti P, Schonberger LB. Chronic wasting disease and potential transmission to humans. Emerg. Infect. Dis.10, 977–984 (2004).
   PubMed Web of Science ®Google Scholar
• Liberski PP, Guiroy DC, Williams ES, Walis A, Budka H. Deposition patterns of disease-associated prion protein in captive mule deer brains with chronic wasting disease. Acta Neuropathol.102(5), 496–500 (2001).
   PubMed Web of Science ®Google Scholar
• Marsh RF, Kincaid AE, Bessen RA, Bartz JC. Interspecies transmission of chronic wasting disease prions to squirrel monkeys (Saimiri sciureus). J. Virol.79(21), 13794–13796 (2005).
   PubMed Web of Science ®Google Scholar
• Race B, Meade-White KD, Miller MW et al. Susceptibilities of nonhuman primates to chronic wasting disease. Emerg. Infect. Dis.15(9), 1366–1376 (2009).
   PubMed Web of Science ®Google Scholar
• Hamir AN, Kunkle RA, Cutlip RC et al. Experimental transmission of chronic wasting disease agent from mule deer to cattle by the intracerebral route. J. Vet. Diagn. Invest.17(3), 276–281 (2005).
   PubMed Web of Science ®Google Scholar
• Hamir AN, Kunkle RA, Cutlip RC, Miller JM, Williams ES, Richt JA. Transmission of chronic wasting disease of mule deer to Suffolk sheep following intracerebral inoculation. J. Vet. Diagn. Invest.18(6), 558–565 (2006).
   PubMed Web of Science ®Google Scholar
• Heisey DM, Mickelsen NA, Schneider JR et al. Chronic wasting disease (CWD) susceptibility of several North American rodents that are sympatric with cervid CWD epidemics. J. Virol.84(1), 210–215 (2010).
   PubMed Web of Science ®Google Scholar
• Kurt TD, Seelig DM, Schneider JR et al. Alteration of the chronic wasting disease species barrier by in vitro prion amplification. J. Virol.85(17), 8528–8537 (2011).
   PubMedGoogle Scholar
• Hamir AN, Greenlee JJ, Nicholson EM et al. Experimental transmission of chronic wasting disease (CWD) from elk and white-tailed deer to fallow deer by intracerebral route: final report. Can. J. Vet. Res.75(2), 152–156 (2011).
   PubMed Web of Science ®Google Scholar
• Krumm CE, Conner MM, Hobbs NT, Hunter DO, Miller MW. Mountain lions prey selectively on prion-infected mule deer. Biol. Lett.6(2), 209–211 (2010).
   PubMedGoogle Scholar
• Kong Q, Huang S, Zou W et al. Chronic wasting disease of elk: transmissibility to humans examined by transgenic mouse models. J. Neurosci.25(35), 7944–7949 (2005).
   PubMed Web of Science ®Google Scholar
• Tamguney G, Giles K, Bouzamondo-Bernstein E et al. Transmission of elk and deer prions to transgenic mice. J. Virol.80(18), 9104–9114 (2006).
   PubMed Web of Science ®Google Scholar
• Sandberg M, Al-Doujaily H, Sigurdson C et al. Chronic wasting disease prions are not transmissible to transgenic mice over-expressing human prion protein. J. Gen. Virol.91(10), 2651–2657 (2010).
   PubMed Web of Science ®Google Scholar
• Angers RC, Kang HE, Napier D et al. Prion strain mutation determined by prion protein conformational compatibility and primary structure. Science328(5982), 1154–1158 (2010).
   PubMed Web of Science ®Google Scholar
• Collinge J. Prion strain mutation and selection. Science328, 1111–1112 (2010).
   PubMed Web of Science ®Google Scholar
• Johnson CJ, Herbst A, Duque-Velasquez C et al. Prion protein polymorphisms affect chronic wasting disease progression. PLoS One6(3), e17450 (2011).
   PubMed Web of Science ®Google Scholar
• Angers RC, Browning SR, Seward TS et al. Prions in skeletal muscles of deer with chronic wasting disease. Science311(5764), 1117 (2006).
   PubMed Web of Science ®Google Scholar
• Mathiason CK, Powers JG, Dahmes SJ et al. Infectious prions in the saliva and blood of deer with chronic wasting disease. Science314(5796), 133–136 (2006).
   PubMed Web of Science ®Google Scholar
• Mathiason CK, Hayes-Klug J, Hays SA et al. B cells and platelets harbor prion infectivity in the blood of deer infected with chronic wasting disease. J. Virol.84(10), 5097–5107 (2010).
   PubMed Web of Science ®Google Scholar
• Race B, Meade-White K, Race R, Chesebro B. Prion infectivity in fat of deer with chronic wasting disease. J. Virol.83(18), 9608–9610 (2009).
   PubMed Web of Science ®Google Scholar
• Haley NJ, Seelig DM, Zabel MD, Telling GC, Hoover EA. Detection of CWD prions in urine and saliva of deer by transgenic mouse bioassay. PLoS One4(3), e4848 (2009).
   PubMed Web of Science ®Google Scholar
• Tamguney G, Miller MW, Wolfe LL et al. Asymptomatic deer excrete infectious prions in faeces. Nature461(7263), 529–532 (2009).
   PubMed Web of Science ®Google Scholar
• Angers RC, Seward TS, Napier D et al. Chronic wasting disease prions in elk antler velvet. Emerg. Infect. Dis.15(5), 696–703 (2009).
   PubMed Web of Science ®Google Scholar
• Barria MA, Telling GC, Gambetti P, Mastrianni JA, Soto C. Generation of a new form of human PrP(Sc) in vitro by interspecies transmission from cervid prions. J. Biol. Chem.286(9), 7490–7495 (2011).
   PubMed Web of Science ®Google Scholar
• Collinge J, Whitfield J, McKintosh E et al. Kuru in the 21st century – an acquired human prion disease with very long incubation periods. Lancet367(9528), 2068–2074 (2006).
   PubMed Web of Science ®Google Scholar
• Smith CB, Booth CJ, Pedersen JA. Fate of prions in soil: a review. J. Environ. Qual.40(2), 449–461 (2011).
   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.2(4), e32 (2006).
   PubMed Web of Science ®Google Scholar
• Saunders SE, Bartz JC, Vercauteren KC, Bartelt-Hunt SL. Enzymatic digestion of chronic wasting disease prions bound to soil. Environ. Sci. Technol.44(11), 4129–4135 (2010).
   PubMed Web of Science ®Google Scholar
• Nichols TA, Pulford B, Wyckoff AC et al. Detection of protease-resistant cervid prion protein in water from a CWD-endemic area. Prion3(3), 171–183 (2009).
   PubMed Web of Science ®Google Scholar
• Johnson CJ, Pedersen JA, Chappell RJ, McKenzie D, Aiken JM. Oral transmissibility of prion disease is enhanced by binding to soil particles. PLoS Pathog.3(7), e93 (2007).
   PubMed Web of Science ®Google Scholar
• Abrams JY, Maddox RA, Harvey AR, Schonberger LB, Belay ED. Travel history, hunting, and venison consumption related to prion disease exposure, 2006–2007 FoodNet population survey. J. Am. Diet. Assoc.111(6), 858–863 (2011).
   PubMedGoogle Scholar
• Denkers ND, Seelig DM, Telling GC, Hoover EA. Aerosol and nasal transmission of chronic wasting disease in cervidized mice. J. Gen. Virol.91(Pt 6), 1651–1658 (2010).
   PubMed Web of Science ®Google Scholar
• Haybaeck J, Heikenwalder M, Klevenz B et al. Aerosols transmit prions to immunocompetent and immunodeficient mice. PLoS Pathog.7(1), e1001257 (2011).
   PubMed Web of Science ®Google Scholar
• Aguzzi A, Heikenwalder M. Prions, cytokines, and chemokines: a meeting in lymphoid organs. Immunity22(2), 145–154 (2005).
   PubMed Web of Science ®Google Scholar
• Aucouturier P, Carp RI, Carnaud C, Wisniewski T. Prion diseases and the immune system. Clin. Immunol.96, 79–85 (2000).
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Goni F. Immunomodulation for prion and prion related diseases. Expert Rev. Vaccines9(12), 1441–1452 (2010).
   PubMed Web of Science ®Google Scholar
• Bremer J, Heikenwalder M, Haybaeck J et al. Repetitive immunization enhances the susceptibility of mice to peripherally administered prions. PLoS One4(9), e7160 (2009).
   Web of Science ®Google Scholar
• Brown KL, Ritchie DL, McBride PA, Bruce ME. Detection of PrP in extraneural tissues. Microscopy Res. Tech.50(1), 40–45 (2000).
   PubMed Web of Science ®Google Scholar
• Mabbott NA, MacPherson GG. Prions and their lethal journey to the brain. Nat. Rev. Microbiol.4(3), 201–211 (2006).
   PubMed Web of Science ®Google Scholar
• Kitamoto T, Muramoto T, Mohri S, Doh-ura K, Tateishi J. Abnormal isoform of prion protein accumulates in follicular dendritic cells in mice with Creutzfeldt–Jakob disease. J. Virol.65(11), 6292–6295 (1991).
   PubMed Web of Science ®Google Scholar
• Aucouturier P, Geissmann F, Damotte D et al. Infected dendritic cells are sufficient for prion transmission to the CNS in mouse scrapie. J. Clin. Invest.108, 703–708 (2001).
   PubMed Web of Science ®Google Scholar
• Langevin C, Gousset K, Costanzo M, Richard-Le GO, Zurzolo C. Characterization of the role of dendritic cells in prion transfer to primary neurons. Biochem. J.431(2), 189–198 (2010).
   PubMedGoogle Scholar
• Sigurdsson EM, Wisniewski T. Promising developments in prion immunotherapy. Expert Rev. Vaccines4, 607–610 (2005).
   PubMed Web of Science ®Google Scholar
• Goni F, Prelli F, Schreiber F et al. High titers of mucosal and systemic anti-PrP antibodies abrogates oral prion infection in mucosal vaccinated mice. Neuroscience153, 679–686 (2008).
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Chabalgoity JA, Goni F. Is vaccination against transmissible spongiform encephalopathies feasible? OIE Sci. Tech. Rev.26(1), 243–251 (2007).
   PubMed Web of Science ®Google Scholar
• Bartz JC, DeJoia C, Tucker T, Kincaid AE, Bessen RA. Extraneural prion neuroinvasion without lymphoreticular system infection. J. Virol.79(18), 11858–11863 (2005).
   PubMed Web of Science ®Google Scholar
• Bessen RA, Martinka S, Kelly J, Gonzalez D. Role of the lymphoreticular system in prion neuroinvasion from the oral and nasal mucosa. J. Virol.83(13), 6435–6445 (2009).
   PubMed Web of Science ®Google Scholar
• Siso S, Gonzalez L, Jeffrey M. Neuroinvasion in Prion diseases: the roles of ascending neural infection and blood dissemination. Interdiscip. Perspect. Infect. Dis.2010, 747892 (2010).
   PubMedGoogle Scholar
• Selkoe DJ. Resolving controversies on the path to Alzheimer’s therapeutics. Nat. Med.17(9), 1060–1065 (2011).
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Boutajangout A. Immunotherapeutic approaches for Alzheimer’s disease in transgenic mouse models. Brain Struct. Funct.214, 201–218 (2010).
   PubMedGoogle Scholar
• Wisniewski T, Sigurdsson EM. Murine models of Alzheimer’s disease and their use in developing immunotherapies. Biochim. Biophys. Acta Mol. Basis Dis.1802(10), 847–859 (2010).
   PubMed Web of Science ®Google Scholar
• Brody DL, Holtzman DM. Active and passive immunotherapy for neurodegenerative diseass. Annu. Rev. Neurosci.31, 175–193 (2008).
   PubMed Web of Science ®Google Scholar
• Rinne JO, Brooks DJ, Rossor MN et al. (11)C-PiB PET assessment of change in fibrillar amyloid-β load in patients with Alzheimer’s disease treated with bapineuzumab: a Phase 2, double-blind, placebo-controlled, ascending-dose study. Lancet Neurol.9(4), 363–372 (2010).
   PubMed Web of Science ®Google Scholar
• Ostrowitzki S, Deptula D, Thurfjell L et al. Mechanism of amyloid removal in patients with alzheimer disease treated with gantenerumab. Arch. Neurol. doi:10.1001/archneurol.2011.1538 (2011) (Epub ahead of print).
   PubMedGoogle Scholar
• Selkoe DJ. Alzheimer’s disease. Cold Spring Harb. Perspect. Biol.3(7), pii: a004457 (2011).
   Google Scholar
• Morgan D. Immunotherapy for Alzheimer’s disease. J. Intern. Med.269, 54–63 (2011).
   PubMed Web of Science ®Google Scholar
• Boutajangout A, Sigurdsson EM, Krishnamurthy PK. τ as A therapeutic target for Alzheimer’s disease. Curr. Alzheimer Res.8(6), 666–677 (2011).
   PubMed Web of Science ®Google Scholar
• Gu J, Sigurdsson EM. Immunotherapy for tauopathies. J. Mol. Neurosci.45(3), 690–695 (2011).
   PubMedGoogle Scholar
• Come JH, Fraser PE, Lansbury PT Jr. A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proc. Natl Acad. Sci. USA90(13), 5959–5963 (1993).
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science216, 136–144 (1982).
   PubMed Web of Science ®Google Scholar
• Sigurdson CJ, Nilsson KP, Hornemann S et al.De novo generation of a transmissible spongiform encephalopathy by mouse transgenesis. Proc. Natl Acad. Sci. USA106(1), 304–309 (2009).
   PubMed Web of Science ®Google Scholar
• Sigurdson CJ, Nilsson KP, Hornemann S et al. A molecular switch controls interspecies prion disease transmission in mice. J. Clin. Invest.120(7), 2590–2599 (2010).
   PubMed Web of Science ®Google Scholar
• Sigurdson CJ, Joshi-Barr S, Bett C et al. Spongiform encephalopathy in transgenic mice expressing a point mutation in the {β}2-{α}2 loop of the Prion protein. J. Neurosci.31(39), 13840–13847 (2011).
   PubMed Web of Science ®Google Scholar
• Gabizon R, McKinley MP, Groth D, Prusiner SB. Immunoaffinity purification and neutralization of scrapie prion infectivity. Proc. Natl Acad. Sci. USA85(18), 6617–6621 (1988).
   PubMed Web of Science ®Google Scholar
• 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. USA98(16), 9295–9299 (2001).
   PubMed Web of Science ®Google Scholar
• Peretz D, Williamson RA, Kaneko K et al. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature412(6848), 739–743 (2001).
   PubMed Web of Science ®Google Scholar
• Kim CL, Umetani A, Matsui T, Ishiguro N, Shinagawa M, Horiuchi M. Antigenic characterization of an abnormal isoform of prion protein using a new diverse panel of monoclonal antibodies. Virology320(1), 40–51 (2004).
   PubMed Web of Science ®Google Scholar
• Kim CL, Karino A, Ishiguro N, Shinagawa M, Sato M, Horiuchi M. Cell-surface retention of PrPC by anti-PrP antibody prevents protease-resistant PrP formation. J. Gen. Virol.85(Pt 11), 3473–3482 (2004).
   PubMed Web of Science ®Google Scholar
• Pankiewicz J, Prelli F, Sy MS et al. Clearance and prevention of prion infection in cell culture by anti-PrP antibodies. Eur. J. Neurosci.24, 2635–2647 (2006).
   Web of Science ®Google Scholar
• Westergard L, Turnbaugh JA, Harris DA. A nine amino acid domain is essential for mutant prion protein toxicity. J. Neurosci.31(39), 14005–14017 (2011).
   PubMedGoogle Scholar
• Petsch B, Muller-Schiffmann A, Lehle A et al. Biological effects and use of PrPSc- and PrP-specific antibodies generated by immunization with purified full-length native mouse prions. J. Virol.85(9), 4538–4546 (2011).
   PubMed Web of Science ®Google Scholar
• Sigurdsson EM, Sy MS, Li R et al. Anti-PrP antibodies for prophylaxis following prion exposure in mice. Neurosci. Lett.336, 185–187 (2003).
   PubMed Web of Science ®Google Scholar
• White AR, Enever P, Tayebl M et al. Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature422, 80–83 (2003).
   PubMed Web of Science ®Google Scholar
• Sadowski MJ, Pankiewicz J, Prelli F et al. Anti-PrP Mab 6D11 suppresses PrPSc replication in prion infected myeloid precursor line FDC-P1/22L and in the lymphoreticular system in vivo. Neurobiol. Dis.34, 267–278 (2009).
   PubMed Web of Science ®Google Scholar
• Song CH, Furuoka H, Kim CL et al. Effect of intraventricular infusion of anti-prion protein monoclonal antibodies on disease progression in prion-infected mice. J. Gen. Virol.89(Pt 6), 1533–1544 (2008).
   PubMed Web of Science ®Google Scholar
• Solforosi L, Criado JR, McGavern DB et al. Cross-linking cellular prion protein triggers neuronal apoptosis in vivo. Science303(5663), 1514–1516 (2004).
   PubMed Web of Science ®Google Scholar
• Lefebvre-Roque M, Kremmer E, Gilch S et al. Toxic effects of intracerebral PrP antibody administration during the course of BSE infection in mice. Prion1(3), 198–206 (2007).
   PubMed Web of Science ®Google Scholar
• Mallucci GR, White MD, Farmer M et al. Targeting cellular prion protein reverses early cognitive deficits and neurophysiological dysfunction in prion-infected mice. Neuron53(3), 325–335 (2007).
   PubMed Web of Science ®Google Scholar
• Verity NC, Mallucci GR. Rescuing neurons in prion disease. Biochem. J.433(1), 19–29 (2011).
   PubMedGoogle Scholar
• Morgan D, Diamond DM, Gottschall PE et al. Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer’s disease. Nature408, 982–985 (2000).
   PubMed Web of Science ®Google Scholar
• Janus C, Pearson J, McLaurin J et al. Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer’s disease. Nature408, 979–982 (2000).
   PubMed Web of Science ®Google Scholar
• Sigurdsson EM, Knudsen EL, Asuni A et al. An attenuated immune response is sufficient to enhance cognition in an Alzheimer’s disease mouse model immunized with amyloid-β derivatives. J. Neurosci.24, 6277–6282 (2004).
   PubMed Web of Science ®Google Scholar
• Asuni A, Boutajangout A, Scholtzova H et al. Aβ derivative vaccination in alum adjuvant prevents amyloid deposition and does not cause brain microhemorrhages in Alzheimer’s model mice. Eur. J. Neurosci.24, 2530–2542 (2006).
   PubMed Web of Science ®Google Scholar
• Goni F, Prelli F, Ji Y et al. Immunomodulation targeting abnormal protein conformation reduces pathology in a mouse model of Alzheimer’s disease. PLoS One5(10), e13391 (2010).
   PubMed Web of Science ®Google Scholar
• Bard F, Cannon C, Barbour R et al. Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat. Med.6(8), 916–919 (2000).
   PubMed Web of Science ®Google Scholar
• Gilman S, Koller M, Black RS et al. Clinical effects of Aβ immunization (AN1792) in patients with AD in an interupted trial. Neurology64, 1553–1562 (2005).
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Frangione B. Immunological and anti-chaperone therapeutic approaches for Alzheimer’s disease. Brain Pathol.15, 72–77 (2005).
   PubMed Web of Science ®Google Scholar
• Wisniewski T. Commentary on “Clinical effects of Aβ immunization (AN1792) in patients with AD in an interrupted trial.” Nat. Clin. Prac. Neurol.64, 1553–1562 (2005).
   Google Scholar
• Hock C, Konietzko U, Straffer JR et al. Antibodies against β-amyloid slow cognitive decline in Alzheimer’s disease. Neuron38, 547–554 (2003).
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Boutajangout A. Vaccination as a therapeutic approach for Alzheimer’s disease. Mount Sinai J. Med.77, 17–31 (2010).
   PubMedGoogle Scholar
• Boche D, Donald J, Love S et al. Reduction of aggregated τ in neuronal processes but not in the cell bodies after Aβ42 immunisation in Alzheimer’s disease. Acta Neuropathol.120, 13–20 (2010).
   PubMed Web of Science ®Google Scholar
• Holmes C, Boche D, Wilkinson D et al. Long-term effects of Aβ42 immunisation in Alzheimer’s disease: follow-up of a randomised, placebo-controlled Phase 1 trial. Lancet372(9634), 216–223 (2008).
   PubMed Web of Science ®Google Scholar
• Weiner HL, Frenkel D. Immunology and immunotherapy of Alzheimer’s disease. Nat. Rev. Immunol.6(5), 404–416 (2006).
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Konietzko U. Amyloid-β immunization for Alzheimer’s disease. Lancet Neurol.7(9), 805–811 (2008).
   PubMed Web of Science ®Google Scholar
• Lemere CA, Masliah E. Can Alzheimer disease be prevented by amyloid-β immunotherapy? Nat. Rev. Neurol.6(2), 108–119 (2010).
   PubMed Web of Science ®Google Scholar
• Manuelidis L. Vaccination with an attenuated Creutzfeldt–Jakob disease strain prevents expression of a virulent agent. Proc. Natl Acad. Sci. USA95(5), 2520–2525 (1998).
   PubMed Web of Science ®Google Scholar
• Sigurdsson EM, Brown DR, Daniels M et al. Vaccination delays the onset of prion disease in mice. Am. J. Pathol.161, 13–17 (2002).
   PubMed Web of Science ®Google Scholar
• 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.101(Suppl. 2), 14670–14676 (2004).
   PubMed Web of Science ®Google Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• 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. Vaccine23(22), 2862–2868 (2005).
   PubMed Web of Science ®Google Scholar
• Schwarz A, Kratke O, Burwinkel M et al. Immunization with a synthetic prion protein-derived peptide prolongs survival times of mice orally exposed to the scrapie agent. Neurosci. Lett.350, 187–189 (2003).
   PubMed Web of Science ®Google Scholar
• Pilon J, Loiacono C, Okeson D et al. Anti-prion activity generated by a novel vaccine formulation. Neurosci. Lett.429(2–3), 161–164 (2007).
   PubMed Web of Science ®Google Scholar
• Mastroeni P, Chabalgoity JA, Dunstan SJ, Maskell DJ, Dougan G. Salmonella: immune responses and vaccines. Vet. J.161(2), 132–164 (2001).
   PubMed Web of Science ®Google Scholar
• Moreno M, Kramer MG, Yim L, Chabalgoity JA. Salmonella as live trojan horse for vaccine development and cancer gene therapy. Curr. Gene Ther.10(1), 56–76 (2010).
   PubMed Web of Science ®Google Scholar
• Tacket CO, Sztein MB, Wasserman SS et al. Phase 2 clinical trial of attenuated Salmonella enterica serovar Typhi oral live vector vaccine CVD 908-htrA in U.S. volunteers. Infect. Immun.68(3), 1196–1201 (2000).
   PubMed Web of Science ®Google Scholar
• Kirkpatrick BD, McKenzie R, O’Neill JP et al. Evaluation of Salmonella enterica serovar Typhi (Ty2 aroC-ssaV-) M01ZH09, with a defined mutation in the Salmonella pathogenicity island 2, as a live, oral typhoid vaccine in human volunteers. Vaccine24(2), 116–123 (2006).
   PubMed Web of Science ®Google Scholar
• Villarreal-Ramos B, Manser J, Collins RA, Dougan G, Chatfield SN, Howard CJ. Immune responses in calves immunised orally or subcutaneously with a live Salmonella Typhimurium aro vaccine. Vaccine16(1), 45–54 (1998).
   PubMed Web of Science ®Google Scholar
• Chabalgoity JA, Moreno M, Carol H, Dougan G, Hormaeche CE. A dog-adapted Salmonella Typhimurium strain as a basis for a live oral Echinococcus granulosus vaccine. Vaccine19, 460–469 (2000).
   PubMed Web of Science ®Google Scholar
• Heppner FL, Christ AD, Klein MA et al. Transepithelial prion transport by M cells. Nat. Med.7(9), 976–977 (2001).
   PubMed Web of Science ®Google Scholar
• Goni F, Knudsen EL, Schreiber F et al. Mucosal vaccination delays or prevents prion infection via an oral route. Neuroscience133, 413–421 (2005).
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Mathiason C, Wong V et al. Specific anti-PrP mucosal and systemic responses in white tail deer vaccinated with attenuated Salmonella expressing deer PrP. Alz. Dementia7(4 Suppl. 1), S687–S688 (2011).
   Google Scholar
• Zou WQ, Cashman NR. Acidic pH and detergents enhance in vitro conversion of human brain PrPC to a PrPSc-like form. J. Biol. Chem.277(46), 43942–43947 (2002).
   PubMedGoogle Scholar
• 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).
   PubMed Web of Science ®Google Scholar
• Hedlin PD, Cashman NR, Li L et al. Design and delivery of a cryptic PrP(C) epitope for induction of PrP(Sc)-specific antibody responses. Vaccine28(4), 981–988 (2010).
   PubMed Web of Science ®Google Scholar