Document Type

Thesis - University Access Only

Award Date

2008

Degree Name

Doctor of Philosophy (PhD)

Department / School

Veterinary and Biomedical Sciences

First Advisor

Alan Young

Abstract

Transmissible spongiform encephalopathies (TS Es) are fatal, neurodegenerative diseases caused by a variant form of a normal cellular protein (PrPc) that is conformationally altered into a disease-causing form (PrPct). TSEs include scrapie in sheep and goats as well as chronic wasting disease (CWD) in deer, elk, and moose. TSEs pose a significant challenge to study due to their similarity to the normal cellular protein as well as the lack of a typical immune response. In this study we were the first laboratory to examine the deposition patterns of scrapie and CWD in early infection. First, a novel method of antigen retrieval was developed to be used in prion immunohistochemistry. This antigen retrieval technique allowed staining of sheep immune cells as well as PrPsc within lymph nodes and increased the sensitivity of immunohistochemical techniques used in prion detection. This new technique will enable the use of many monoclonal antibodies with consistent and reliable results and allow the detection of small amounts of PrPsc in lymph nodes of sheep infected with scrapie.

Library of Congress Subject Headings

Scarpie -- Pathogenesis
Prion diseases in animals
Chronic wasting disease
Immunohistochemistry

Publisher

South Dakota State University

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Rights Statement

In Copyright