7ZH7

Cryo-EM structure of ex vivo AA amyloid from renal tissue of a short hair cat deceased in a shelter

7ZH7 の概要

• エントリーDOI: 10.2210/pdb7zh7/pdb
• EMDBエントリー: 14726
• 分子名称: Serum amyloid A protein (1 entity in total)
• 機能のキーワード: aa amyloidosis, cat, serum amyloid a, protein fibril
• 由来する生物種: Felis catus (domestic cat)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 144497.66

構造登録者

Schulte, T.,Chaves-Sanjuan, A.,Ricagno, S. (登録日: 2022-04-05, 公開日: 2022-11-30, 最終更新日: 2024-07-24)

主引用文献

Schulte, T.,Chaves-Sanjuan, A.,Mazzini, G.,Speranzini, V.,Lavatelli, F.,Ferri, F.,Palizzotto, C.,Mazza, M.,Milani, P.,Nuvolone, M.,Vogt, A.C.,Vogel, M.,Palladini, G.,Merlini, G.,Bolognesi, M.,Ferro, S.,Zini, E.,Ricagno, S.
Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter.
Nat Commun, 13:7041-7041, 2022

PubMed Abstract: AA amyloidosis is a systemic disease characterized by deposition of misfolded serum amyloid A protein (SAA) into cross-β amyloid in multiple organs in humans and animals. AA amyloidosis occurs at high SAA serum levels during chronic inflammation. Prion-like transmission was reported as possible cause of extreme AA amyloidosis prevalence in captive animals, e.g. 70% in cheetah and 57-73% in domestic short hair (DSH) cats kept in zoos and shelters, respectively. Herein, we present the 3.3 Å cryo-EM structure of AA amyloid extracted post-mortem from the kidney of a DSH cat with renal failure, deceased in a shelter with extreme disease prevalence. The structure reveals a cross-β architecture assembled from two 76-residue long proto-filaments. Despite >70% sequence homology to mouse and human SAA, the cat SAA variant adopts a distinct amyloid fold. Inclusion of an eight-residue insert unique to feline SAA contributes to increased amyloid stability. The presented feline AA amyloid structure is fully compatible with the 99% identical amino acid sequence of amyloid fragments of captive cheetah.

PubMed: 36396658
DOI: 10.1038/s41467-022-34743-2

実験手法

ELECTRON MICROSCOPY (3.3 Å)