A structural basis for prion strain diversity.
Journal
Nature chemical biology
ISSN: 1552-4469
Titre abrégé: Nat Chem Biol
Pays: United States
ID NLM: 101231976
Informations de publication
Date de publication:
05 2023
05 2023
Historique:
received:
21
06
2022
accepted:
18
11
2022
medline:
4
5
2023
pubmed:
17
1
2023
entrez:
16
1
2023
Statut:
ppublish
Résumé
Recent cryogenic electron microscopy (cryo-EM) studies of infectious, ex vivo, prion fibrils from hamster 263K and mouse RML prion strains revealed a similar, parallel in-register intermolecular β-sheet (PIRIBS) amyloid architecture. Rungs of the fibrils are composed of individual prion protein (PrP) monomers that fold to create distinct N-terminal and C-terminal lobes. However, disparity in the hamster/mouse PrP sequence precludes understanding of how divergent prion strains emerge from an identical PrP substrate. In this study, we determined the near-atomic resolution cryo-EM structure of infectious, ex vivo mouse prion fibrils from the ME7 prion strain and compared this with the RML fibril structure. This structural comparison of two biologically distinct mouse-adapted prion strains suggests defined folding subdomains of PrP rungs and the way in which they are interrelated, providing a structural definition of intra-species prion strain-specific conformations.
Identifiants
pubmed: 36646960
doi: 10.1038/s41589-022-01229-7
pii: 10.1038/s41589-022-01229-7
pmc: PMC10154210
doi:
Substances chimiques
Prions
0
Amyloid
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
607-613Subventions
Organisme : Medical Research Council
ID : MC_U123192748
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_UU_00024/5
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_U12316055
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_U123160655
Pays : United Kingdom
Informations de copyright
© 2023. The Author(s).
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