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From: TSS ()
Date: March 23, 2006 at 8:57 am PST

In Reply to: Re: SCRAPIE STRAINS IN GOATS LAST 3 YEARS UK posted by TSS on March 23, 2006 at 7:47 am:

Copyright © 2005 Published by Elsevier Ltd.
Immunohistochemical Features of PrPd Accumulation in Natural and Experimental Goat Transmissible Spongiform Encephalopathies

M. Jeffreya, S. Martina, L. Gonzáleza, J. Fosterb, J.P.M. Langeveldc, F.G. van Zijderveldc, J. Grassid and N. Hunterb

aVeterinary Laboratories Agency (VLA-Lasswade), Pentlands Science Park, Bush Loan, Midlothian EH26 0PZ, UK
bInstitute of Animal Health Neuropathogenesis Unit, Edinburgh EH9 3JF, UK
cCentral Institute for Animal Disease Control, Lelystad (CIDC-Lelystad), PO Box 2004, 8203 AA Lelystad, The Netherlands
dCEA Service de Pharmacologie et d'Immunologie, Batiment 136, CEA/Saclay, France

Received 9 June 2005; accepted 30 October 2005. Available online 20 March 2006.

Scrapie is a transmissible spongiform encephalopathy (TSE) or prion disease, which naturally affects sheep and goats. Immunohistochemical epitope mapping of abnormal PrP accumulations (PrPd) in brain can help in characterizing sheep TSE sources or strains and in identifying potential bovine spongiform encephalopathy (BSE) infections of sheep. Natural and experimental TSE infections of goats were examined to determine whether the epitope mapping approach could also be applied to aid recognition of BSE infection in goats. Goats experimentally infected with the SSBP/1 or CH1641 sheep scrapie strains or with cattle BSE, together with four field cases of natural TSE in goats, were examined immunohistochemically with six different antibodies. CH1641 and SSBP/1 infections in goats, as in sheep, showed PrPd accumulations which were mainly intracellular. Some differences in targeting, particularly of Purkinje cells, was evident in inter-species comparisons of CH1641 and SSBP/1. PrPd labelling of goat BSE experimental cases showed extensive intracellular and extracellular accumulations, also similar to those in sheep BSE. Intra-neuronal PrPd in both goat and sheep BSE was labelled only by antibodies recognizing epitopes located C-terminally of residue His99, whereas in natural sheep TSE sources, and in sheep and goat SSBP/1, PrPd was also detected by antibodies to epitopes located between residues Trp93 and His99. Testing of four natural goat TSE samples showed one case in which epitope mapping characteristics and the overall patterns of PrPd accumulation was identical with those of experimental goat BSE. The four natural goat scrapie cases examined showed some degree of immunohistochemical phenotype variability, suggesting that multiple strains exist within the relatively small UK goat population.

Keywords: bovine spongiform encephalopathy; BSE; cattle; goat; prion protein; scrapie; sheep; transmissible spongiform encephalopathy; TSE


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