ArticleNature communications2022
Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Serum amyloid A kinetics predicts outcomes to PD-1 inhibitors in patients with recurrent or metastatic nasopharyngeal carcinoma.BMC cancer · 2026Article
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Structural characterization of atrial natriuretic peptide amyloid fibrils from patients with atrial fibrillation.Nature communications · 2025Article
- Surveillance of amyloid A deposits in commercial beef liver and assessment of food hygiene risks.The Journal of veterinary medical science · 2025Article
- Polymorphisms in SAA alter intrarenal amyloid distribution of AA amyloidosis in cats.Scientific reports · 2025Article
- Serum Amyloid A Binding to Glycosaminoglycans is Synergistic with Amyloid Formation: Therapeutic Targeting in the Inflammation-linked Amyloidosis.Journal of molecular biology · 2025Article
- Elucidating the Mechanism of Recognition and Binding of Heparin to Amyloid Fibrils of Serum Amyloid A.Biochemistry · 2025Article
- Cryo-EM structure of a lysozyme-derived amyloid fibril from hereditary amyloidosis.Nature communications · 2024Article
- Investigation of serum amyloid a within animal species focusing on the 1-25 amino acid region.The veterinary quarterly · 2023Article
- AA-amyloidosis in cats (Felis catus) housed in shelters.PloS one · 2023Article
- Histological evaluation of the distribution of systemic AA-amyloidosis in nine domestic shorthair cats.PloS one · 2023Article
- Renal amyloid-A amyloidosis in cats: Characterization of proteinuria and biomarker discovery, and associations with kidney histology.Journal of veterinary internal medicineArticle
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Authors and funding
18 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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