An aggregation-specific enzyme-linked immunosorbent assay: detection of conformational differences between recombinant PrP protein dimers and PrP(Sc) aggregates.

The conversion of the normal cellular prion protein, PrP(C), into the protease-resistant, scrapie PrP(Sc) aggregate is the cause of prion diseases. We developed a novel enzyme-linked immunosorbent assay (ELISA) that is specific for PrP aggregate by screening 30 anti-PrP monoclonal antibodies (MAbs) for their ability to react with recombinant mouse, ovine, bovine, or human PrP dimers. One MAb that reacts with all four recombinant PrP dimers also reacts with PrP(Sc) aggregates in ME7-, 139A-, or 22L-infected mouse brains.

Photographic detection of retinopathy in insulin-treated diabetes. A population study in the city of Tartu, Estonia.

Purpose: To perform a cross-sectional baseline investigation of diabetic retinopathy prevalence and metabolic control.

Methods: Using a register of insulin-dependent diabetes mellitus in Tartu (pop. 104,791), 175 patients were invited to fundus photography; 149 (89%) participated, 99 of them diagnosed with diabetes before the age of thirty.