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Immunological characterization of abnormal prion protein from atypical scrapie cases in sheep using a panel of monoclonal antibodies

¹ Institute for Novel and Emerging Infectious Diseases at the Friedrich-Loeffler-Institut, Boddenblick 5a, 17493 Greifswald-Insel Riems, Germany
² Central Institute for Animal Disease Control, PO Box 2004, 8203 AA Lelystad, The Netherlands

Correspondence
Martin H. Groschup
martin.groschup{at}fli.bund.de

After the implementation of an active surveillance programme for scrapie in sheep in the EU, the number of diagnosed classical scrapie cases rose sharply and a novel kind of so-called atypical scrapie case was discovered. These atypical scrapie cases display unusual features concerning the distribution of the abnormal prion protein (PrP^Sc) in the brain, a distinct electrophoretic profile of PrP^Sc and an inconsistent reaction pattern in the currently used rapid tests. In this report, PrP^Sc of two German atypical sheep scrapie cases was characterized by epitope mapping using a panel of 18 monoclonal antibodies that were directed against epitopes located throughout the prion protein. This analysis suggests that PrP^Sc derived from atypical scrapie cases and treated with proteinase K is largely composed of an 11 kDa fragment (previously referred to as the 12 kDa band) and of polymeric fragments thereof. The 11 kDa band corresponds to a prion protein fragment spanning approximately aa 90–153 and may therefore represent a novel PrP^Sc type.