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TitleCryo-EM reveals structural variability of apolipoprotein A-I amyloid fibrils across organs, mutations, and clinical presentations.
Journal, issue, pagesNat Commun, Year 2026
Publish dateApr 17, 2026
AuthorsBinh An Nguyen / Maria Del Carmen Fernandez-Ramirez / Parker Bassett / Virender Singh / Preeti Singh / Maja Pękała / Layla Villalon / Yasmin Ahmed / Andrew Lemoff / Bret Evers / Christian Lopez / Barbara Kluve-Beckerman / Lorena Saelices /
PubMed AbstractHereditary apolipoprotein A-I (AApoA‑I) amyloidosis is a rare systemic disease caused by the deposition of amyloid fibrils formed by apolipoprotein A‑I in multiple organs, leading to severe ...Hereditary apolipoprotein A-I (AApoA‑I) amyloidosis is a rare systemic disease caused by the deposition of amyloid fibrils formed by apolipoprotein A‑I in multiple organs, leading to severe clinical outcomes. With no available therapies or diagnostic tools, defining the structure of AApoA‑I fibrils is crucial to understanding disease mechanisms and guiding intervention. Here we use cryo-electron microscopy to analyze AApoA‑I fibrils from the heart, kidney, liver, and spleen of patients carrying G26R, L90P, and R173P mutations. G26R fibrils, regardless of organ, exhibits untwisted morphologies and cannot be resolved structurally. Conversely, L90P and R173P fibrils display a compact diabolo-shaped conformation in all organs analyzed. Their high-resolution maps enable visualization of cis-Proline 66, which may represent a potential conformational switch during fibril formation. Our findings suggest that mutation-driven polymorphism may influence organ tropism and clinical presentation. This work advances our understanding of AApoA‑I fibril assembly and provides insights toward developing targeted clinical tools.
External linksNat Commun / PubMed:41991931
MethodsEM (helical sym.)
Resolution2.15 - 2.9 Å
Structure data

71896

9pvy

EMDB-71896, PDB-9pvy:
Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I L90P amyloidosis patient
Method: EM (helical sym.) / Resolution: 2.15 Å

71897

9pvz

EMDB-71897, PDB-9pvz:
Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I R173P amyloidosis patient
Method: EM (helical sym.) / Resolution: 2.3 Å

71898

9pw3

EMDB-71898, PDB-9pw3:
Cryo-EM structure of renal amyloid fibril from a variant apolipoprotein A-I R173P amyloidosis patient
Method: EM (helical sym.) / Resolution: 2.73 Å

74399

9zld

EMDB-74399, PDB-9zld:
Cryo-EM structure of hepatic amyloid fibril from a variant ATTRV122delta, single filament morphology
Method: EM (helical sym.) / Resolution: 2.9 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Apolipoprotein A-I / AApoAI / L90P / Amyloidosis. / R173P / cardiac / kidney / ATTR / Systemic amyloidosis / V122delta / amyloid

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