Press Release - Prion diseases: new clues in the structure of prion proteins
Carbohydrates of the prion glycoproteins responsible for a group of neurodegenerative diseases were sequenced for the first time thanks to a highly sensitive technique. The paper is now published in PLOS Pathogens and represents another step toward the fully understanding of these fatal disorders |
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Image: Photomicrograph of a neural tissue specimen, harvested from a scrapie affected |
18 February 2021 Prion diseases are a group of rapidly progressive, fatal and infectious neurodegenerative disorders affecting both humans and animals: Bovine Spongiform Encephalopathy (BSE) or ‘mad cow’ disease is one of the most famous since in 1996 scientists found that the agent responsible for the disease in cows, is the same agent responsible for the so-called variant Creutzfeldt-Jakob Disease (vCJD), a disease affecting humans. A new study carried out by SISSA – Scuola Internazionale Superiore di Studi Avanzati in collaboration with other institutions including Genos Glycoscience Research Laboratory from Zagreb, Croatia and Elettra Sincrotrone Trieste, provides important information on the differences in structures of the prions, proteins responsible for diseases that at the state of the art are incurable. The mystery of the strains One of the main unanswered problems revolving around prion diseases is the existence of strains, leading to a wide range of disorders with different symptoms, incubation time, histopathology, etc. “For a better understanding of the mechanism of the diseases and the existence of strains, resolving the structure of the prion protein is necessary” neuroscientist Natali Nakić, first author of the paper “Site-specific analysis of N-glycans from different sheep prion strains”, just published in PLOS Pathogens, says. |
The prion protein is a glycoprotein, meaning polysaccharides called glycans encompass a large part of the protein structure. The new study is the first one of its kind as it focuses on comparing glycan structures from different strains. A step toward the fully understanding “In this study, glycans from two different sheep prion strains were compared” Natali Nakić adds. “After an extensive analysis, no major differences in glycan structures were found between the two strains, suggesting that glycans may not be responsible for the biochemical and neuropathological differences”. A remarkable goal as it represents another step toward the fully understanding of prion glycoproteins and the cellular mechanism of prion diseases.
Press ReviewTriestecafè.it dd 19/02/2021: "Sequenziati a Trieste per la prima volta i carboidrati dei prioni, responsabili di malattie neurodegenerative" |