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

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 and Stefano Ricagno ()
Additional contact information
Tim Schulte: IRCCS Policlinico San Donato
Antonio Chaves-Sanjuan: Università degli Studi di Milano
Giulia Mazzini: University of Pavia
Valentina Speranzini: Università degli Studi di Milano
Francesca Lavatelli: University of Pavia
Filippo Ferri: AniCura Istituto Veterinario Novara
Carlo Palizzotto: AniCura Istituto Veterinario Novara
Maria Mazza: Istituto Zooprofilattico Sperimentale del Piemonte Liguria e Valle d’Aosta, S.C. Diagnostica Specialistica
Paolo Milani: University of Pavia
Mario Nuvolone: University of Pavia
Anne-Cathrine Vogt: University of Bern
Monique Vogel: University of Bern
Giovanni Palladini: University of Pavia
Giampaolo Merlini: University of Pavia
Martino Bolognesi: Università degli Studi di Milano
Silvia Ferro: University of Padova
Eric Zini: AniCura Istituto Veterinario Novara
Stefano Ricagno: IRCCS Policlinico San Donato

Nature Communications, 2022, vol. 13, issue 1, 1-9

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-34743-2

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