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Abstract
Polymorphisms in the prion protein, PrP C, affect the susceptibility of sheep to scrapie. Three rare polymorphisms, M137T, S138N, and R151C, have been found in Icelandic sheep. Observations suggest that R151C may be associated with lower scrapie susceptibility, whereas S138N is neutral. The effects of the S138N and R151C polymorphisms on the cellular processing of PrP C were examined in a model system consisting of the expression of ovine PrP C-EGFP (green fluorescent protein) chimeras in the mouse neuroblastoma cell line N2a. Chimeras with the haplotypes A 136R 154Q 171 (ARQ), AN 138RQ, and AC 151RQ were compared. The chimeras did not differ regarding their translocation into the secretory system, glycosylation, and transport to the cell surface. However, the AC 151RQ chimera differed from the other chimeras regarding disulfide bonding characteristics; furthermore, a slight difference was detected between AC 151RQ and the other chimeras by limited proteolysis. The processing of the ARQ and AN 138RQ chimeras was identical in the experiments performed consistent with observations that it is neutral.
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