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Bett et al. Acta Neuropathologica Communications (2017) 5:32 DOI ten.1186/s40478-017-0430-zRESEARCHOpen AccessEnhanced neuroinvasion by smaller, soluble prionsCyrus Bett1,7, Jessica Lawrence1, Timothy D. Kurt1, Christina Orru2, Patricia Aguilar-Calvo1, Anthony E. Kincaid3, Witold K. Surewicz4, Byron Caughey2, Chengbiao Wu5 and Christina J. Sigurdson1,6*AbstractInfectious prion aggregates can propagate from extraneural sites in to the brain with remarkable efficiency, most likely transported by way of peripheral nerves. However not all prions spread in to the brain, and also the physical properties of a prion that is certainly capable of transit within neurons stay unclear. We hypothesized that smaller, diffusible aggregates spread into the CNS Myeloperoxidase/MPO Protein C-10His through peripheral nerves. Here we made use of a structurally diverse panel of prion strains to analyze how the prion conformation impacts transit in to the brain. Two prion strains form fibrils visible ultrastructurally within the brain in situ, whereas 3 strains form diffuse, subfibrillar prion deposits and no visible fibrils. The subfibrillar strains had drastically higher levels of soluble prion aggregates than the fibrillar strains. Major neurons internalized both the subfibrillar and fibril-forming prion strains by macropinocytosis, and each strain forms had been transported from the axon terminal to the cell body in vitro. However.