| Wednesday, July 13, 2022 Caption: The top image shows a hamster prion; the lower image a mouse prion. These cross-sectional "mugshots" of prion strains show their overall structural similarities, but also their many different details. Each provides a distinct template for prion growth. (Graphic by Bryan Hansen, NIAID) NIAID study reveals, compares different prion strains For decades, scientists have wondered how different strains of prions can propagate when they do not carry their own genes with them as they move from host to host. A new study in Nature Communications from NIAID researchers and colleagues at Case Western Reserve University reveals – in near-atomic detail – how differences in the folding of the primary protein of prions (PrP) can help determine the distinct characteristics of prion strains. Prion diseases are caused by the corruption of the normal form of PrP that is made by all mammals. Multiple strains of prions have been identified in several mammals, with each giving a distinctive array of clinical presentations, molecular features, patterns of damage in the brain, and transmissibility to other species. Thus, deciphering the basis of prion strain diversity is important in understanding the risks posed by prions to which humans and animals are exposed. The research teams are pursuing studies of prion structure to aid in the design and screening of treatments that might slow or prevent the spread of these deadly diseases.  | 
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