Prions cause diseases such as mad cow disease or Creutzfeldt-Jakob The study, recently published in the prestigious scientific journal PLOS Pathogens, has finally solved the structure of an infectious prion. The data obtained contradict many of the theoretical models of prion structure proposed so far and allow the formulation of the molecular mechanisms existing behind the replication of prions in mammals with transmissible spongiform encephalopathies.Prions are unconventional infectious agents causing disease in both humans and animals, such as Creutzfeldt-Jakob disease or mad cow disease. Unlike viruses or bacteria, prions have no genome because they are composed entirely of protein. To understand their behavior and pathogenesis the key is in their structure, the way in which these proteins fold.IRTA-CReSA collaborated in this study by helping to demonstrate that the prion that was finally analyzed was, indeed, infectious. This was done through neuropathological and immunohistochemical studies of the brains of mice inoculated with the same purified protein that had been used to determine the structure. These experiments were carried out in the laboratory PRIOCAT located inside the biocontainment level 3 unit of IRTA-CReSA. A laboratory equipped with the necessary biosafety conditions to work with these pathogens.For more information you can read about this study entry in the blog CReSA and the city, "Elucidation of the structure of an infectious prion."The study:The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy Ester Vázquez-Fernández, Matthijn R. Vos, Pavel Afanasyev, Lino Cebey, Alejandro M. Sevillano, Enric Vidal, Isaac Rosa, Ludovic Renault, Adriana Ramos, Peter J. Peters, José Jesús Fernández, Marin van Heel, Howard S. Young,Jesús R. Requena, Holger Wille PLOS Pathogens 2016
