The Effects of Glycosylation on Prion Protein Conversion

Abstract

Glycosylation of the prion protein may be experimentally altered through expression in different insect cell lines. The presence or absence of several terminal sugars may or may not have an effect on the conversion efficiency of the prion protein into its infectious form. The main focus of this research was to characterize the prion protein as it is produced in two varying insect cell lines that are able to glycosylate proteins to different extents. Glycosidase treatment demonstrated that the expressed prion protein was glycosylated. Lectin blotting was used to assess the presence or absence of terminal sugar moieties existing on the prion protein. The differentially glycosylated prion proteins produced will allow insight into the effect of terminal glycosylation on prion protein conversion. This research may provide valuable insight into the still unknown prion interconversion process and disease transmission dynamics, and may have implications for human based prion disease.