Master's Theses

Department

Biology

Degree Name

Master of Science (MS)

Abstract

Prion diseases are a group of infectious, incurable, fatal neurodegenerative disorders, including scrapie in sheep, chronic wasting disease in deer, and Creutzfeldt-Jakob disease (CJD) in humans. A key event in prion disease is the conformational transition of the cellular prion protein (PrPC) into the pathogenic isoform (PrPSC). Prion disease occurrence depends mainly on the interaction between the host prion protein (PrPC) and the prion strain (PrPSC). It was hypothesized that prion gene polymorphisms correlate with an organism’s susceptibility to prion disease, which may be related to the overall stability of the α-helical domain of the protein. Prion gene polymorphisms are also related to the species barrier between different mammalian species. The closer the three-dimensional conformation of the prion proteins in donor and recipient animals, the easier it is to transmit prion diseases between the two. Interestingly, some animal species are considered resistant to prion diseases, such as pigs, rabbits, and dogs, since no single case of naturally-occurring disease has been reported in them. In this research, I looked for polymorphisms in the PrPC gene by comparing wild pig sequences to each other, as well as other susceptible and resistant species. There are several regions in the nucleotide sequence in the PrPC gene of all pigs that are highly conserved. Key polymorphisms seem to reside at position 224 and position 230. These polymorphisms might be used as a prediction tool of the animal susceptibility for prion diseases using the amino acid sequence.

Keywords

protein aggregation, PRNP, species barrier, β-sheet, amyloid

Advisor

Dr. Eric Gillock

Date of Award

Spring 2019

Document Type

Thesis

Rights

© The Author(s)

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