In silico investigation of the prion protein glycosylation profiles in relation to scrapie disease resistance in domestic sheep (Ovis aries)

In this study, the potential N- and O-glycosylation positions of sheep prion protein polymorphisms were analyzed, the secondary and three-dimensional protein structure models were predicted, three-dimensional glycoprotein models were constructed and the role of glycosylation positions in protein interactions was investigated. Here, we found that protein secondary and three-dimensional structures vary among polymorphisms. Moreover, we found wild-type prion and all polymorphic variants show N-glycosylation at Asn184 and Asn200 positions, while O-glycosylation profiles are variant-specific. We also found that structural changes among prion polymorphisms leads to the formation of variant spesific O-glycosylation profiles and these positions are associated with protein interactions. Based on these findings, we suggest that O-glycosylation may be effective on resistance/susceptibility of sheep prion polymorphisms to scrapie disease.Graphical abstract
Source: Molecular and Cellular Probes - Category: Molecular Biology Source Type: research