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A stretch of residues within the protease-resistant core is not necessary for prion structure and infectivity.
- Source :
-
Prion [Prion] 2017 Jan 02; Vol. 11 (1), pp. 25-30. Date of Electronic Publication: 2017 Feb 08. - Publication Year :
- 2017
-
Abstract
- 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 α-helical domain of the correctly folded protein and turns into a β-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 PrP <superscript>C</superscript> 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 PrP <superscript>C</superscript> nor for the formation of a stable prion structure.
Details
- Language :
- English
- ISSN :
- 1933-690X
- Volume :
- 11
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Prion
- Publication Type :
- Academic Journal
- Accession number :
- 28281924
- Full Text :
- https://doi.org/10.1080/19336896.2016.1274851