Skip to main content
Log in

BSE immunohistochemical patterns in the brainstem: a comparison between UK and Italian cases

  • Original Paper
  • Published:
Acta Neuropathologica Aims and scope Submit manuscript

Abstract

The continuous monitoring of bovine spongiform encephalopathy (BSE) cases is an integral component of European research and surveillance programmes, to ensure that any changes in the presentation of transmissible spongiform encephalopathies (TSE) in cattle can be detected and defined. Monitoring is generally limited to the brainstem at the level of the obex, for reasons of practicality, safety and cost. Demonstration of disease-specific prion protein (PrPd) by immunohistochemistry is currently the most widely used confirmatory tool for both active and passive surveillance. This study assessed PrPd immunostaining in the brainstems (obex) of cattle with BSE in the UK and Italy. Immunoreactivity ‘profiles’ were created for each case based on the nature of the immunostaining, its relative intensity and precise neuroanatomical location. This study compares the obex immunostaining patterns of Italian cases (only active surveillance) and two UK groups (both active and passive surveillance). The neuroanatomical distribution and relative intensity of PrPd was highly reproducible in all cases. The overall staining intensity varied widely but was generally stronger in the active than in the passive surveillance populations. The conclusion to be drawn from this comparative study is that the pattern of immunopathology in these routine screening samples for BSE diagnosis and surveillance is the same in the UK and Italy, whether or not the animal was displaying typical, or indeed any, clinical signs at the time of sampling. This indicates that the current confirmatory diagnostic strategy remains appropriate for active surveillance applications.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

References

  1. Biacabe A-G, Laplanche J-L, Ryder S, Baron T (2004) Distinct molecular phenotypes in bovine prion diseases. EMBO Rep 2004:1–5

    Google Scholar 

  2. De Bosschere H, Roels S, Vanopdenbosch E (2004) Atypical case of bovine spongiform encephalopathy in an East-Flemish cow. J Appl Res Vet Med 2:52–54

    Google Scholar 

  3. Casalone C, Zanusso GL, Acutis PL, Ferrari S, Capucci L, Tagliavini F, Monaco S, Caramelli M (2004) Identification of a second bovine amyloidotic spongiform encephalopathy: molecular similarities with sporadic Creutzfeldt-Jakob disease. Proc Natl Acad Sci USA 101:3065–3070

    Article  PubMed  CAS  Google Scholar 

  4. Clark WW, Hourrigan JL, Hadlow WJ (1995) Encephalopathy in cattle experimentally infected with the scrapie agent. Am J Vet Res 56:606–612

    PubMed  CAS  Google Scholar 

  5. Cutlip RC, Miller JM, Race RE, Jenny AL, Katz JB, Lehmkuhl HD, DeBey BM, Robinson MM (1994) Intracerebral transmission of scrapie to cattle. J Infect Dis 169:814–820

    PubMed  CAS  Google Scholar 

  6. European Commission (1996) European Union Council Regulation 716/1996/EC. Official J L099:14

    Google Scholar 

  7. European Commission (2001) European Union Council Regulation 999/2001/EC. Official J L147:1

    Google Scholar 

  8. European Commission (2002). European Union Council Regulation 270/2002/EC. Official J L45:4

    Google Scholar 

  9. European Commission (2004) Report on the monitoring and testing of Ruminants for the presence of transmissible spongiform encephalopathy (TSE) in the EU in 2003, including the results of the survey of prion protein genotypes in sheep breeds. http://www.europa.eu.int/comm/food/food/biosafety/bse/annual_reps_en.htm

  10. Hoinville LJ, Wilesmith JW, Richards MS (1995) An investigation of risk factors for cases of bovine spongiform encephalopathy born after the introduction of the ‘feed ban’. Vet Rec 136:312–318

    PubMed  CAS  Google Scholar 

  11. Jeffrey M, Martin S, Gonzalez L (2003) Cell-associated variants of disease-specific prion protein immunolabelling are found in different sources of sheep transmissible spongiform encephalopathy. J Gen Virol 84:1033–1145

    Article  PubMed  CAS  Google Scholar 

  12. Robinson MM, Hadlow WJ, Knowles DP, Huff TP, Lacy PA, Marsh RF, Gorham JR (1995) Experimental infection of cattle with the agents of transmissible mink encephalopathy and scrapie. J Comp Pathol 113:241–251

    Article  PubMed  CAS  Google Scholar 

  13. Ryder SJ, Hawkins SAC, Konold T, Wells GAH (2002) Challenge of cattle with two current sources of British ovine scrapie results in two different disease presentations. In: Proceedings of the international conference on transmissible spongiform encephalopathies, 15–18 September 2002, Edinburgh, p 22

  14. Simmons MM, Harris P, Jeffrey M, Meek S, Blamire IWH, Wells GAH (1996) BSE in Great Britain: consistency of the neurohistological findings in two random annual samples of clinically suspect cases. Vet Rec 146:391–395

    Google Scholar 

  15. Terry LA, Marsh SA, Ryder SJ, Hawkins SAC, Wells GAH, Spencer YI (2003) Detection of disease-specific PrP in the distal ileum of cattle exposed orally to the agent of bovine spongiform encephalopathy. Vet Rec 152:387–92

    PubMed  CAS  Google Scholar 

  16. Wells GAH, Hancock RD, Cooley WA, Richards MS, Higgins RJ, David GP (1989) Bovine spongiform encephalopathy: diagnostic significance of vacuolar change in selected nuclei of the medulla oblongata. Vet Rec 125:521–524

    PubMed  CAS  Google Scholar 

  17. Wells GAH, Hawkins SAC, Green RB, Austin AR, Dexter I, Spencer YI, Chaplin MJ, Stack MJ, Dawson M (1998) Preliminary observations on the pathogenesis of experimental bovine spongiform encephalopathy (BSE): an update. Vet Rec 142:103–106

    PubMed  CAS  Google Scholar 

  18. Wells GAH, Wilesmith JW (1995) The neuropathology and epidemiology of bovine spongiform encephalopathy. Brain Pathol 5:91–103

    Article  PubMed  CAS  Google Scholar 

  19. Yamakawa Y, Hagiwara K, Nohtomi K, Nakamura Y, Nishijima M, Higuchi Y, Sato Y, Sata T (2003) Expert Committee for BSE diagnosis, Ministry of Health, Labour and Welfare of Japan. Atypical proteinase K-resistant prion protein (PrPres) observed an apparently healthy 23-month-old Holstein steer. Jpn J Infect Dis 56:221–222

    PubMed  Google Scholar 

Download references

Acknowledgements

The authors wish to thank the staff of the Pathology Department, VLA-Weybridge, and the CEA, IZS Turin for their excellent technical assistance. This work was funded by Defra (Project SE 0225 to MMS) and the Italian Ministry of Health (IZS PLV 001/01 to CC).

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to M. M. Simmons.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Casalone, C., Caramelli, M., Crescio, M.I. et al. BSE immunohistochemical patterns in the brainstem: a comparison between UK and Italian cases. Acta Neuropathol 111, 444–449 (2006). https://doi.org/10.1007/s00401-005-0012-1

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00401-005-0012-1

Keywords

Navigation