8A00

Infectious mouse-adapted ME7 scrapie prion fibril purified from terminally-infected mouse brains

8A00 の概要

• エントリーDOI: 10.2210/pdb8a00/pdb
• EMDBエントリー: 15043
• 分子名称: Major prion protein (1 entity in total)
• 機能のキーワード: prion, protein fibril
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 47329.89

構造登録者

Manka, S.W.,Wenborn, A.,Betts, J.,Joiner, S.,Saibil, H.R.,Collinge, J.,Wadsworth, J.D.F. (登録日: 2022-05-26, 公開日: 2023-01-18, 最終更新日: 2024-11-13)

主引用文献

Manka, S.W.,Wenborn, A.,Betts, J.,Joiner, S.,Saibil, H.R.,Collinge, J.,Wadsworth, J.D.F.
A structural basis for prion strain diversity.
Nat.Chem.Biol., 19:607-613, 2023

PubMed Abstract: 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.

PubMed: 36646960
DOI: 10.1038/s41589-022-01229-7

実験手法

ELECTRON MICROSCOPY (2.6 Å)