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From: TSS ()
Subject: Immunohistochemical characteristics of disease-associated PrP are not altered by ...
Date: February 19, 2005 at 9:08 am PST

-------- Original Message --------
Subject: Immunohistochemical characteristics of disease-associated PrP are not altered by host genotype or route of inoculation following infection of sheep with bovine spongiform encephalopathy
Date: Fri, 18 Feb 2005 20:13:33 -0600
From: "Terry S. Singeltary Sr."
Reply-To: Bovine Spongiform Encephalopathy
To: BSE-L@LISTSERV.KALIV.UNI-KARLSRUHE.DE


##################### Bovine Spongiform Encephalopathy #####################

Immunohistochemical characteristics of disease-associated PrP are
not altered by host genotype or route of inoculation following
infection of sheep with bovine spongiform encephalopathy


J Gen Virol 86 (2005), 839-848; DOI 10.1099/vir.0.80364-0

Stuart Martin1, Lorenzo González1, Angela Chong2, Fiona E. Houston3,
Nora Hunter2 and Martin Jeffrey1

1 Veterinary Laboratories Agency (VLA-Lasswade), Pentlands Science Park,
Bush Loan, Penicuik, Midlothian EH26 0PZ, UK
2 Institute for Animal Health Neuropathogenesis Unit, Edinburgh EH9 3JF, UK
3 Institute for Animal Health, Compton, Berkshire RG20 7NN, UK

Correspondence
Martin Jeffrey
m.jeffrey@vla.defra.gsi.gov.uk

It has previously been reported that disease-associated prion protein
(PrPd) derived from natural scrapie and from sheep infected
experimentally with bovine spongiform encephalopathy (BSE) differed in
respect of their immunohistochemical and immunoblotting properties. For
BSE, however, these initial observations were restricted to orally
challenged sheep of the ARQ/ARQ PrP genotype. Here, extended
examinations were performed on 28 sheep that developed neurological
signs after BSE experimental infection by one of three routes.
Intracerebrally infected ARQ/ARQ sheep showed more widespread and
abundant accumulations of PrPd in tissues of the lymphoreticular system
(LRS) than VRQ/VRQ animals, whereas no peripheral PrPd was detected in
ARR/ARR sheep. The intensity and dissemination of PrPd accumulation in
LRS tissues were less than those found previously in orally dosed sheep.
AHQ/AHQ sheep challenged orally and ARQ/AHQ and ARQ/ARQ animals infected
intravenously showed similar LRS-tissue PrPd distributions and levels to
those of ARQ/ARQ sheep infected intracerebrally. The patterns of intra-
and extracellular immunoreactivity to different PrP antibodies in brain
and LRS tissues and the immunoblotting characteristics of PrPres from
brain samples remained constant, irrespective of the route of
inoculation and the PrP genotype, and were the same as described
previously for ARQ/ARQ sheep dosed orally with BSE. These results
suggest that the intracellular truncation of BSE PrPd and the proteinase
K cleavage site of BSE PrPres are not altered by PrP genotype or by
route of inoculation and that, therefore, screening tests based on these
properties can be applied to identify potential sheep BSE cases
occurring naturally.

http://vir.sgmjournals.org/cgi/content/abstract/86/3/839?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&fulltext=prion&searchid=1108778143595_1188&stored_search=&FIRSTINDEX=0&volume=86&issue=3&search_url=http%3A%2F%2Fvir.sgmjournals.org%2Fcgi%2Fsearch

TSS

######### https://listserv.kaliv.uni-karlsruhe.de/warc/bse-l.html ##########






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