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Journal of Clinical Microbiology, June 1998, p. 1750-1755, Vol. 36, No. 6
0095-1137/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Monoclonal Antibody F89/160.1.5 Defines
a Conserved Epitope on the Ruminant Prion Protein
Katherine I.
O'Rourke,1,*
Timothy V.
Baszler,2,3
Janice M.
Miller,4
Terry R.
Spraker,5
Ingrid
Sadler-Riggleman,1,
and
Donald P.
Knowles1
Animal Disease Research Unit, Agricultural
Research Service, U.S. Department of Agriculture,
Pullman, Washington 99164-70301;
Department of Veterinary Microbiology and Pathology, Washington
State University, Pullman, Washington
99164-70402;
Washington Animal Disease
Diagnostic Laboratory, Washington State University, Pullman,
Washington 991643;
National Animal
Disease Center, Agricultural Research Service, U.S. Department of
Agriculture, Ames, Iowa 500104;
and
Colorado State Diagnostic Laboratory, College of
Veterinary Medicine, Colorado State University, Fort Collins,
Colorado 805235
Received 19 August 1997/Returned for modification 11 December
1997/Accepted 27 January 1998
The transmissible spongiform encephalopathies are a heterogeneous
group of fatal neurodegenerative disorders occurring in humans, mink,
cats, and ruminant herbivores. The occurrence of novel transmissible
spongiform encephalopathies in cattle in the United Kingdom and Europe
and in mule deer and elk in parts of the United States has emphasized
the need for reliable diagnostic tests with standardized reagents.
Postmortem diagnosis is performed by histologic examination of brain
sections from affected animals. The histopathological criteria for
transmissible spongiform encephalopathies include gliosis,
astrocytosis, neuronal degeneration, and spongiform change. These
lesions vary in intensity and anatomic location depending on the host
species and genetics, stage of disease, and infectious agent source.
Diagnosis by histopathology alone may be ambiguous in hosts with early
cases of disease and impossible if the tissue is autolyzed. Deposition
of the prion protein (an abnormal isoform of a native cellular
sialoglycoprotein) in the central nervous system is a reliable marker
for infection, and immunohistochemical detection of this marker is a
useful adjunct to histopathology. In the present paper we describe
monoclonal antibody (MAb) F89/160.1.5, which reacts with prion protein
in tissues from sheep, cattle, mule deer, and elk with naturally occurring transmissible spongiform encephalopathies. This MAb recognizes a conserved epitope on the prion protein in formalin-fixed, paraffin-embedded sections after hydrated autoclaving. MAb F89/160.1.5 will be useful in diagnostic and pathogenesis studies of the
transmissible spongiform encephalopathies in these ruminant species.
*
Corresponding author. Mailing address: Animal
Disease Research Unit, Agricultural Research Service, U.S. Department
of Agriculture, 337 Bustad Hall, WSU, Pullman, WA 99164-7030. Phone: (509) 335-6020. Fax: (509) 335-8328. E-mail:
korourke{at}vetmed.wsu.edu.

Present address: 560 Quail Ridge, Pullman, WA 99164.
Journal of Clinical Microbiology, June 1998, p. 1750-1755, Vol. 36, No. 6
0095-1137/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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