Skip directly to site content Skip directly to page options Skip directly to A-Z link Skip directly to A-Z link Skip directly to A-Z link
Volume 19, Number 5—May 2013
Research

Foodborne Transmission of Bovine Spongiform Encephalopathy to Nonhuman Primates

Edgar HolznagelComments to Author , Barbara Yutzy, Walter Schulz-Schaeffer, Carina Kruip, Uwe Hahmann, Pär Bierke, Juan-Maria Torres, Yong-Sun Kim, Achim Thomzig, Michael Beekes, Gerhard Hunsmann, and Johannes Loewer
Author affiliations: Paul-Ehrlich-Institut, Langen, Germany (E. Holznagel, B. Yutzy, C. Kruip, J. Loewer); University of Göttingen, Göttingen, Germany (W. Schulz-Schaeffer); German Primate Centre, Göttingen (U. Hahmann, G. Hunsmann); Swedish Institute for Infectious Disease Control, Solna, Sweden (P. Bierke); Centro de Investigación en Sanidad Animal, Madrid, Spain (J.-M. Torres); Hallym University, Anyang, Gyeonggi-Do, South Korea (Y.-S. Kim); Robert-Koch-Institut, Berlin, Germany (A. Thomzig, M. Beekes)

Main Article

Figure 1

Schematic diagram of the mature nonglycosylated prion protein and below amino acid sequences of the human and the simian prion polypeptide chain. Homology (198/207 aa) between human and simian mature cellular form of prion protein on the amino acid level is 96%. Large and small arrows indicate major and minor, respectively, proteinase K digestion sites (14). Open arrows indicate digestion sites in type 1 fragments; filled arrows indicate digestion sites in type 2 fragments. The epitopes recogniz

Figure 1. . Schematic diagram of the mature nonglycosylated prion protein and below amino acid sequences of the human and the simian prion polypeptide chain. Homology (198/207 aa) between human and simian mature cellular form of prion protein on the amino acid level is 96%. Large and small arrows indicate major and minor, respectively, proteinase K digestion sites (14). Open arrows indicate digestion sites in type 1 fragments; filled arrows indicate digestion sites in type 2 fragments. The epitopes recognized by the used monoclonal antibodies are shown below. OR, octarepeat region; H, α-helical structure; PK, proteinase K; M. fascicularis, Macaca fascicularis. *Swiss-Prot (www.ebi.ac.uk/swissprot/) accession numbers.

Main Article

References
  1. Will  RG, Ironside  JW, Zeidler  M, Cousens  SN, Estibeiro  K, Alperovitch  A, A new variant of Creutzfeldt-Jakob disease in the UK. Lancet. 1996;347:9215. DOIPubMed
  2. Collinge  J, Sidle  KCL, Meads  J, Ironside  J, Hill  AF. Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD. Nature. 1996;383:68590. DOIPubMed
  3. Bruce  ME, Will  RG, Ironside  JW, McConnell  I, Drummond  D, Suttie  A, Transmissions to mice indicate that ‘new variant’ CJD is caused by the BSE agent. Nature. 1997;389:498501. DOIPubMed
  4. Lasmézas  CI, Comoy  E, Hawkins  S, Herzog  C, Mouthon  F, Konold  T, Risk of oral infection with bovine spongiform encephalopathy agent in primates. Lancet. 2005;365:7813 .PubMed
  5. Valleron  AJ, Boelle  PY, Will  R, Cesbron  J-Y. Estimation of epidemic size and incubation time based on age characteristics of vCJD in the United Kingdom. Science. 2001;294:17268. DOIPubMed
  6. Gravenor  MB, Stallard  N, Curnow  R, McLean  AR. Repeated challenge with prion disease: the risk of infection and impact on incubation period. Proc Natl Acad Sci U S A. 2003;100:109605. DOIPubMed
  7. Andrews  NJ. Incidence of variant Creutzfeldt-Jakob disease diagnoses and death in the U.K. 2011. The National Creutzfeldt-Jakob Disease Research & Surveillance Unit [cited 2013 Feb 28]. http://www.cjd.ed.ac.uk/documents/cjdq72.pdf
  8. Hunsmann  G. Hahmann U, Motzkus D, Bierke P, Dormont D, Lazmezas CI, et al. BSE transmission through food and blood products: a study in primates to assess the risk for humans. 5th Framework Programme [cited 2013 Feb 28]. ftp://ftp.cordis.europa.eu/pub/fp7/kbbe/docs/tse_ok-web.pdf
  9. Mead  S, Poulter  M, Uphill  J, Beck  J, Whitfield  J, Webb  TEF, Genetic risk factors for variant Creutzfeldt-Jakob disease: a genome-wide association study. Lancet Neurol. 2009;8:5766. DOIPubMed
  10. Mercier  G, Dieterlen  F, Lucotte  G. Population distribution of the methionine allele at the PRNP codon 129 polymorphism in Europe and the Middle East. Hum Biol. 2008;80:18190. DOIPubMed
  11. Ironside  JW, Bishop  MT, Connolly  K, Hegazy  D, Lowrie  S, Le Grice  M, Variant Creutzfeldt-Jakob disease: prion protein genotype analysis of positive appendix tissue samples from a retrospective prevalence study. BMJ. 2006;332:11868. DOIPubMed
  12. Kaski  D, Mead  S, Hyare  H, Cooper  S, Jampana  R, Overell  J, Variant CJD in an individual heterozygous for PRNP codon 129. Lancet. 2009;374:2128. DOIPubMed
  13. Diringer  H, Roehmel  J, Beekes  M. Effect of repeated oral infection of hamsters with scrapie. J Gen Virol. 1998;79:60912 .PubMed
  14. Yull  HM, Ritchie  DL, Langeveld  JPM, van Zijderveld  FG, Bruce  ME, Ironside  JW, Detection of type 1 prion protein in variant Creutzfeldt-Jakob disease. Am J Pathol. 2006;168:1517. DOIPubMed
  15. Parchi  P, Zou  W, Wang  W, Brown  P, Capellari  S, Ghetti  B, Genetic influence on the structural variations of the abnormal prion protein. Proc Natl Acad Sci U S A. 2000;97:1016872. DOIPubMed
  16. Parchi  P, Giese  A, Capellari  S, Brown  P, Schulz-Schaeffer  W, Windl  O, Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects. Ann Neurol. 1999;46:22433. DOIPubMed
  17. Cali  I, Castellani  R, Yuan  J, Al-Shekhlee  A, Cohen  ML, Xiao  X, Classification of sporadic Creutzfeldt-Jakob disease revisited. Brain. 2006;129:226677. DOIPubMed
  18. Polymenidou  M, Stoeck  K, Glatzel  M, Vey  M, Bellon  A, Aguzzi  A. Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease. Lancet Neurol. 2005;4:80514. DOIPubMed
  19. Cali  I, Castellani  R, Alshekhlee  A, Cohen  Y, Blevins  J, Yuan  J, Co-existence of scrapie prion protein types 1 and 2 in sporadic Creutzfeldt-Jakob disease: its effect on the phenotype and prion-type characteristics. Brain. 2009;132:264358. DOIPubMed
  20. Zou  W-Q, Capellari  S, Parchi  P, Sy  M-S, Gambetti  P, Chen  SG. Identification of novel proteinase K–resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease. J Biol Chem. 2003;278:4042936. DOIPubMed
  21. Notari  S, Strammiello  R, Capellari  S, Giese  A, Cescatti  M, Grassi  J, Characterization of truncated forms of abnormal prion protein in Creutzfeldt-Jakob disease. J Biol Chem. 2008;283:3055765. DOIPubMed
  22. Yutzy  B, Holznagel  E, Coulibaly  C, Stuke  A, Hahmann  U, Deslys  J-P, Time-course studies of 14–3-3 protein isoforms in cerebrospinal fluid and brain of primates after oral or intracerebral infection with bovine spongiform encephalopathy agent. J Gen Virol. 2007;88:346978. DOIPubMed
  23. Castilla  J, Gutierrez  A, Pintado  B, Ramirez  MA, Parra  B, Doyle  D, Early detection of PrPres in BSE-infected bovine transgenic mice. Arch Virol. 2003;148:67791 . DOIPubMed
  24. Schulz-Schaeffer  WJ, Tschoke  S, Kranefuss  N, Drose  W, Hause-Reitner  D, Giese  A, The paraffin-embedded tissue blot detects PrP(Sc) early in the incubation time in prion diseases. Am J Pathol. 2000;156:516. DOIPubMed
  25. Holznagel  E, Yutzy  B, Schulz-Schaeffer  WJ, Hanschman  K-M, Stuke  A, Hahmann  U, Increase in CD230 (cellular prion protein) fluorescence on blood lymphocytes in bovine spongiform encephalopathy–infected nonhuman primates. Transfusion. 2010;50:45266. DOIPubMed
  26. Choi  J-K, Park  S-J, Jun  Y-C, Oh  J-M, Jeong  B-H, Lee  H-P, Generation of monoclonal antibody recognized by the GXXXG motif (glycine zipper) of prion protein. Hybridoma (Larchmt). 2006;25:2717. DOIPubMed
  27. 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. 2010;222:3807. DOIPubMed
  28. Hilton  DA, Ghani  AC, Conyers  L, Edwards  P, McCardle  L, Ritchie  D, Prevalence of lymphoreticular prion protein accumulation in UK tissue samples. J Pathol. 2004;203:7339. DOIPubMed
  29. Nishida  N, Katamine  S, Manuelidis  L. Reciprocal interference between specific CJD and scrapie agents in neural cell cultures. Science. 2005;310:4936. DOIPubMed
  30. Shikiya  RA, Ayers  JI, Schutt  CR, Kincaid  AE, Bartz  JC. Coinfecting prion strains compete for a limiting cellular resource. J Virol. 2010;84:570614. DOIPubMed
  31. Lindwall  G, Cole  D. Phosphorylation affects the ability of tau protein to promote microtubule assembly. J Biol Chem. 1984;259:53015 .PubMed
  32. Race  B, Mead-White  KD, Miller  MW, Barbian  KD, Rubenstein  R, LaFauci  G, Susceptibilities of nonhuman primates to chronic wasting disease. Emerg Infect Dis. 2009;15:136676. DOIPubMed

Main Article

Page created: April 24, 2013
Page updated: April 24, 2013
Page reviewed: April 24, 2013
The conclusions, findings, and opinions expressed by authors contributing to this journal do not necessarily reflect the official position of the U.S. Department of Health and Human Services, the Public Health Service, the Centers for Disease Control and Prevention, or the authors' affiliated institutions. Use of trade names is for identification only and does not imply endorsement by any of the groups named above.
file_external