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From: TSS (
Subject: Identification and Characterization of the First U.S. Bovine Spongiform Encephalopathy Case Authors
Date: November 7, 2004 at 6:44 pm PST

-------- Original Message --------
Subject: Identification and Characterization of the First U.S. Bovine Spongiform Encephalopathy Case Authors
Date: Sun, 07 Nov 2004 20:46:58 -0600
From: "Terry S. Singeltary Sr."

Research >

Title: Identification and Characterization of the First U.S. Bovine
Spongiform Encephalopathy Case Authors
item Richt, Juergen

item Kluge, John - NVSL, APHIS, AMES, IA
item Alt, David

item Kunkle, Robert - bob

item Hamir, Amirali

item Czub, Stefanie - NATL BSE REF LAB, CANADA
item Davis, Arthur - NVSL, APHIS, AMES, IA
item Hall, S Mark - NVSL, APHIS, AMES, IA
Submitted to: Meeting Abstract
Publication Acceptance Date: January 2, 2004
Publication Date: January 4, 2004
Citation: Richt, J.A., Kluge, J.P., Alt, D.P., Kunkle, R.A., Hamir,
A.N., Czub, S., Davis, A.J., Hall, S. 2004. Identification And
Characterization Of The First U.S. Bovine Spongiform Encephalopathy
Case. Poster Created For Use By The USDA At A Meeting With The Office Of
International Epizootics. Technical Abstract: Bovine spongiform
encephalopathy (BSE) is a transmissible spongiform encephalopathy of
cattle, first detected in 1986 in the U.K. and subsequently in other
countries. BSE may have arisen either from the infectious agent scrapie,
which causes a similar disease in sheep and goats, or from a germline
mutation in the protein-coding region of the prion protein (PrP) gene of
affected cattle. Here, we report on the prion protein polypeptide
profile and genotype from the first identified case of BSE in the State
of Washington in the United States. The six-year old Holstein cow was
nonambulatory at slaughter and the formalin-fixed obex area of the
brainstem was found to contain spongiform changes and vacuolated neurons
by histopathology and the abnormal form of the prion protein, PrPBSE, by
immunohistochemistry. Species determination was made on the
formalin-fixed tissue. Extensive PrPBSE deposition in the obex was
confirmed by Western blot analyses and enzyme-linked immunosorbent assay
using brainstem and cerebellum derived from fresh tissue from the
suspect animal. The PrPBSE polypeptide profile from the U.S. BSE case
was characterized by (i) a lower molecular mass of the unglycosylated
PrPBSE polypeptide fragment compared to samples from sheep with scrapie
and deer with chronic wasting disease, (ii) good immunoreactivity with
monoclonal antibody 6H4 directed against the central region of the PrP,
but a lack of staining with monoclonal antibody P4, which recognizes the
protease-resistant N-terminal end of the PrP; and (iii) a glycoform
profile with a high proportion of the diglycosylated PrPBSE isoform.
Comparison of the U.S. BSE isolate to the recent Canadian and European
BSE isolates revealed similar sized PrPBSE polypeptide fragments using
anti-PrP antibody 6H4. The PrP gene from the U.S. BSE case was amplified
from both, fresh and formalin-fixed brain material and found to be of
bovine origin with a normal, rather unremarkable cattle PrP sequence.
This cow had a synonymous polymorphism at codon 192, and both alleles
contained the six-copy octapeptide repeat region. We conclude from these
studies that (i) the PrPBSE profile from the first U.S. BSE case showed
similar molecular properties to the typical PrPBSE pattern described for
the Canadian and European BSE isolates, and (ii) a germline mutation in
the bovine PrP gene is not likely the etiological cause in this case.
This information is consistent with the hypothesis that the U.S. BSE
case - similar to the one in Canada - was most likely exposed to
contaminated feed.

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