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Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter

Veterinary Science

Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter

T. Schulte, A. Chaves-sanjuan, et al.

Discover groundbreaking insights into AA amyloidosis, a systemic disease affecting multiple organs due to misfolded serum amyloid A protein. This research, featuring a 3.3 Å cryo-EM structure of feline AA amyloid, highlights unique architectural features and intriguing similarities with captive cheetah structures. Join the authors, including Tim Schulte and Antonio Chaves-Sanjuan, as they explore these crucial findings.

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Playback language: English
Abstract
AA amyloidosis is a systemic disease characterized by the deposition of misfolded serum amyloid A protein (SAA) into cross-β amyloid in multiple organs. This study presents the 3.3 Å cryo-EM structure of AA amyloid extracted from the kidney of a domestic short hair (DSH) cat with renal failure from a shelter with high disease prevalence. The structure reveals a cross-β architecture with a distinct amyloid fold compared to human and mouse SAA, influenced by a feline-specific eight-residue insert. The feline AA amyloid structure is highly similar to that found in captive cheetahs, suggesting potential implications for prion-like transmission.
Publisher
Nature Communications
Published On
Nov 17, 2022
Authors
Tim Schulte, Antonio Chaves-Sanjuan, Giulia Mazzini, Valentina Speranzini, Francesca Lavatelli, Filippo Ferri, Carlo Palizzotto, Maria Mazza, Paolo Milani, Mario Nuvolone, Anne-Cathrine Vogt, Monique Vogel, Giovanni Palladini, Giampaolo Merlini, Martino Bolognesi, Silvia Ferro, Eric Zini, Stefano Ricagno
Tags
AA amyloidosis
serum amyloid A protein
cryo-EM structure
feline amyloid
prion-like transmission
cross-β architecture
kidney disease

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