TY - JOUR AU - Chapuis, Jérôme AU - Moudjou, Mohammed AU - Reine, Fabienne AU - Herzog, Laetitia AU - Jaumain, Emilie AU - Chapuis, Céline AU - Quadrio, Isabelle AU - Boulliat, Jacques AU - Perret-Liaudet, Armand AU - Dron, Michel AU - Laude, Hubert AU - Rezaei, Human AU - Béringue, Vincent PY - 2016 DA - 2016/02/05 TI - Emergence of two prion subtypes in ovine PrP transgenic mice infected with human MM2-cortical Creutzfeldt-Jakob disease prions JO - Acta Neuropathologica Communications SP - 10 VL - 4 IS - 1 AB - Mammalian prions are proteinaceous pathogens responsible for a broad range of fatal neurodegenerative diseases in humans and animals. These diseases can occur spontaneously, such as Creutzfeldt-Jakob disease (CJD) in humans, or be acquired or inherited. Prions are primarily formed of macromolecular assemblies of the disease-associated prion protein PrPSc, a misfolded isoform of the host-encoded prion protein PrPC. Within defined host-species, prions can exist as conformational variants or strains. Based on both the M/V polymorphism at codon 129 of PrP and the electrophoretic signature of PrPSc in the brain, sporadic CJD is classified in different subtypes, which may encode different strains. A transmission barrier, the mechanism of which remains unknown, limits prion cross-species propagation. To adapt to the new host, prions have the capacity to ‘mutate’ conformationally, leading to the emergence of a variant with new biological properties. Here, we transmitted experimentally one rare subtype of human CJD, designated cortical MM2 (129 MM with type 2 PrPSc), to transgenic mice overexpressing either human or the VRQ allele of ovine PrPC. SN - 2051-5960 UR - https://doi.org/10.1186/s40478-016-0284-9 DO - 10.1186/s40478-016-0284-9 ID - Chapuis2016 ER -