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

Schulte, Tim; Chaves-Sanjuan, Antonio; Mazzini, Giulia; Speranzini, Valentina; Lavatelli, Francesca; Ferri, Filippo; Palizzotto, Carlo; Mazza, Maria; Milani, Paolo; Nuvolone, Mario; Vogt, Anne-Cathrine; Vogel, Monique; Palladini, Giovanni; Merlini, Giampaolo; Bolognesi, Martino; Ferro, Silvia; Zini, Eric; Ricagno, Stefano

doi:10.1038/s41467-022-34743-2

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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. (2022). Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter. Nature Communications, 13(1), 7041. https://doi.org/10.1038/s41467-022-34743-2

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