Incomplete glycosylation during prion infection unmasks a prion protein epitope that facilitates prion detection and strain discrimination.

ABSTRACT: The causative factors underlying conformational conversion of cellular prion protein (PrP^C) into its infectious counterpart (PrP^Sc) during prion infection remain undetermined, in part because of a lack of monoclonal antibodies (mAbs) that can distinguish these conformational isoforms. Here we show that the anti-PrP mAb PRC7 recognizes an epitope that is shielded from detection when glycans are attached to Asn-196. We observed that whereas PrP^C is predisposed to full glycosylation and is therefore refractory to PRC7 detection, prion infection leads to diminished PrP^Sc glycosylation at Asn-196, resulting in an unshielded PRC7 epitope that is amenable to mAb recognition upon renaturation. Detection of PRC7-reactive PrP^Sc in experimental a

SUBMITTER: Kang HE 

PROVIDER: S-EPMC7383396 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature