7QIG

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

7QIG の概要

• エントリーDOI: 10.2210/pdb7qig/pdb
• EMDBエントリー: 13989
• 分子名称: Major prion protein (1 entity in total)
• 機能のキーワード: prion, amyloid, prp, prion protein, mouse rml scrapie strain, ex vivo 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: 45870.31

構造登録者

Manka, S.W.,Zhang, W.,Wenborn, A.,Betts, J.,Joiner, S.,Saibil, H.R.,Collinge, J.,Wadsworth, J.D.F. (登録日: 2021-12-14, 公開日: 2022-07-27, 最終更新日: 2025-07-09)

主引用文献

Manka, S.W.,Zhang, W.,Wenborn, A.,Betts, J.,Joiner, S.,Saibil, H.R.,Collinge, J.,Wadsworth, J.D.F.
2.7 angstrom cryo-EM structure of ex vivo RML prion fibrils.
Nat Commun, 13:4004-4004, 2022

PubMed Abstract: Mammalian prions propagate as distinct strains and are composed of multichain assemblies of misfolded host-encoded prion protein (PrP). Here, we present a near-atomic resolution cryo-EM structure of PrP fibrils present in highly infectious prion rod preparations isolated from the brains of RML prion-infected mice. We found that prion rods comprise single-protofilament helical amyloid fibrils that coexist with twisted pairs of the same protofilaments. Each rung of the protofilament is formed by a single PrP monomer with the ordered core comprising PrP residues 94-225, which folds to create two asymmetric lobes with the N-linked glycans and the glycosylphosphatidylinositol anchor projecting from the C-terminal lobe. The overall architecture is comparable to that of recently reported PrP fibrils isolated from the brain of hamsters infected with the 263K prion strain. However, there are marked conformational variations that could result from differences in PrP sequence and/or represent distinguishing features of the distinct prion strains.

PubMed: 35831275
DOI: 10.1038/s41467-022-30457-7

実験手法

ELECTRON MICROSCOPY (2.7 Å)