A stretch of residues within the protease-resistant core is not necessary for prion structure and infectivity

Munoz-Montesino, Carola; Sizun, Christina; Moudjou, Mohammed; Herzog, Laetitia; Reine, Fabienne; Igel-Egalon, Angelique; Barbereau, Clement; Chapuis, Jerome; Ciric, Danica; Laude, Hubert; Beringue, Vincent; Rezaei, Human; Dron, Michel


Mapping out regions of PrP influencing prion conversion remains a challenging issue complicated by the lack of prion structure. The portion of PrP associated with infectivity contains the -helical domain of the correctly folded protein and turns into a -sheet-rich insoluble core in prions. Deletions performed so far inside this segment essentially prevented the conversion. Recently we found that deletion of the last C-terminal residues of the helix H2 was fully compatible with prion conversion in the RK13-ovPrP cell culture model, using 3 different infecting strains. This was in agreement with preservation of the overall PrPC structure even after removal of up to one-third of this helix. Prions with internal deletion were infectious for cells and mice expressing the wild-type PrP and they retained prion strain-specific characteristics. We thus identified a piece of the prion domain that is neither necessary for the conformational transition of PrPC nor for the formation of a stable prion structure.

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Título según WOS: ID WOS:000396024200003 Not found in local WOS DB
Título de la Revista: PRION
Volumen: 11
Número: 1
Fecha de publicación: 2017
Página de inicio: 25
Página final: 30


Notas: ISI