species and strain glycosylation patterns of prpsc物种和应变朊蛋白的糖基化模式.pdfVIP

Species and Strain Glycosylation Patterns of PrPSc 1 2 3 4 Konstantinos Xanthopoulos , Magdalini Polymenidou , Sue J. Bellworthy , Sylvie L. Benestad , Theodoros Sklaviadis1,5* 1 Laboratory of Pharmacology, Department of Pharmacy, Aristotle University of Thessaloniki, Thessaloniki, Greece, 2 Ludwig Institute for Cancer Research, and the Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, California, United States of America, 3 Pathology Department, Veterinary Laboratories Agency-Weybridge, Addlestone, Surrey, United Kingdom, 4 Department of Pathology, National Veterinary Institute, Oslo, Norway, 5 Institute of Agrobiotechnology, Centre for Research and Technology, Thermi, Greece Abstract Background: A key event in transmissible spongiform encephalopathies (TSEs) is the conversion of the soluble, protease- C sensitive glycosylated prion protein (PrP ) to an abnormally structured, aggregated and partially protease-resistant isoform (PrPSc). Both PrP isoforms bear two potential glycosylation sites and thus in a typical western blot with an anti-PrP antibody three distinct bands appear, corresponding to the di-, mono- or unglycosylated forms of the protein. The relative intensity and electrophoretic mobility of the three bands are characteristic of each TSE strain and have been used to discriminate between them. Methodology/Principal Findings: In the present study we used lectin-based western blotting to evaluate possible variations in composition within sugar chains carried by PrPSc purified from subjects affected with different TSEs. Our findings indicate