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Article Dans Une Revue Prion Année : 2017

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

Résumé

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.

Dates et versions

hal-01603861 , version 1 (02-10-2017)

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Carola Munoz-Montesino, Christina Sizun, Mohammed Moudjou, Laetitia Herzog, Fabienne Reine, et al.. A stretch of residues within the protease-resistant core is not necessary for prion structure and infectivity. Prion, 2017, 11 (1), pp.25-30. ⟨10.1080/19336896.2016.1274851⟩. ⟨hal-01603861⟩
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