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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,dagger 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.

dagger 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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