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ARS Home » Pacific West Area » Pullman, Washington » Animal Disease Research » Research » Publications at this Location » Publication #84392
Title: MONOCLONAL ANTIBODY F89/160.1.5 DEFINES A CONSERVED EPITOPE ON THE RUMINANT PRION PROTEIN

Author
item O'Rourke, Katherine
item BASZLER, TIMOTHY - WASHINGTON STATE UNIV
item Miller, Janice
item SPRAKER, JERRY - COLORADO STATE UNIV
item SADLER-RIGGLEMAN, INGRID - FORMER ARS EMPLOYEE
item Knowles Jr, Donald

Submitted to: Journal of Clinical Microbiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/2/1998
Publication Date: N/A
Citation: N/A

Interpretive Summary: This manuscript characterizes a monoclonal antibody that binds to the prions of scrapie, bovine spongiform encephalopathy and chronic wasting diseases. The utility of this monoclonal antibody is that it binds to prion by immunohistochemistry and western blotting. The development of monoclonal antibodies against the prion diseases is important so that the diagnosis of these diseases can be standarized. The potential uses of this reagent are discussed.

Technical Abstract: 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 an in mule deer and elk in parts of the United States has emphasized the need for reliable diagnostic tests. The histopathological criteria of gliosis, astrocytosis, neuronal degeneration, and spongiform change vary in intensity and anatomic location depending on the host species, host genetics, stage of disease, and infectious agent source. Diagnosis by histopathology alone may be ambiguous in early cases 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 this paper, we describe monoclonal antibody F89/160.1.5, which reacts with prion protein in tissues from sheep, cattle, mule deer, and elk with naturally occurring transmissible spongiform encephalopathy. This monoclonal antibody recognizes a conserved epitope in formalin fixed paraffin 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.