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

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  • Tim Schulte

    (IRCCS Policlinico San Donato)

  • Antonio Chaves-Sanjuan

    (Università degli Studi di Milano
    Università degli Studi di Milano)

  • Giulia Mazzini

    (University of Pavia
    Fondazione IRCCS Policlinico San Matteo)

  • 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
    Fondazione IRCCS Policlinico San Matteo)

  • Mario Nuvolone

    (University of Pavia
    Fondazione IRCCS Policlinico San Matteo)

  • Anne-Cathrine Vogt

    (University of Bern
    University Hospital Bern)

  • Monique Vogel

    (University of Bern
    University Hospital Bern)

  • Giovanni Palladini

    (University of Pavia
    Fondazione IRCCS Policlinico San Matteo)

  • Giampaolo Merlini

    (University of Pavia
    Fondazione IRCCS Policlinico San Matteo)

  • Martino Bolognesi

    (Università degli Studi di Milano
    Università degli Studi di Milano)

  • Silvia Ferro

    (University of Padova)

  • Eric Zini

    (AniCura Istituto Veterinario Novara
    University of Padua
    University of Zurich)

  • Stefano Ricagno

    (IRCCS Policlinico San Donato
    Università degli Studi di Milano)

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.

Suggested Citation

  • Tim Schulte & Antonio Chaves-Sanjuan & Giulia Mazzini & Valentina Speranzini & Francesca Lavatelli & Filippo Ferri & Carlo Palizzotto & Maria Mazza & Paolo Milani & Mario Nuvolone & Anne-Cathrine Vogt, 2022. "Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34743-2
    DOI: 10.1038/s41467-022-34743-2
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    References listed on IDEAS

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    1. Paolo Swuec & Francesca Lavatelli & Masayoshi Tasaki & Cristina Paissoni & Paola Rognoni & Martina Maritan & Francesca Brambilla & Paolo Milani & Pierluigi Mauri & Carlo Camilloni & Giovanni Palladini, 2019. "Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient," Nature Communications, Nature, vol. 10(1), pages 1-9, December.
    2. Akanksha Bansal & Matthias Schmidt & Matthies Rennegarbe & Christian Haupt & Falk Liberta & Sabrina Stecher & Ioana Puscalau-Girtu & Alexander Biedermann & Marcus Fändrich, 2021. "AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
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