Caprine PRNP polymorphisms N146S and Q222K are associated with proteolytic cleavage of PrPC

Sally A Madsen-Bouterse, Paula Stewart, Helen Williamson, David A Schneider, Wilfred Goldmann

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Expression of the cellular prion protein (PrPC) is crucial for the development of prion diseases. Amino acid changes in PrPC or a reduced amount of PrPC may modulate disease resistance. The relative abundance of C1, a natural α-cleavage fragment of PrPC, was previously found to be associated with a resistant PRNP genotype in sheep. Goats are another small ruminant where classical scrapie susceptibility is under strong genetic control. In this study, we assessed PrPC in goats for the existence of similar associations between PrPC fragments and genotype. Brain tissue homogenates from scrapie-free goats with wild type PRNP or polymorphisms (I142M, H143R, N146S, or Q222K) were deglycosylated prior to immunoblot for assessment of the relative abundance of the C1 fragment of PrPC. The presence of K222 or S146 alleles demonstrated significantly different relative levels of C1 compared to that observed in wild type goats, which suggests that the genotype association with C1 is neither unique to sheep nor exclusive to the ovine Q171R dimorphism.

Original languageEnglish
Article number52
JournalGenetics Selection Evolution
Volume53
Issue number1
DOIs
Publication statusPublished - 19 Jun 2021

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