Nature CommunicationsBiochemistryPeer-reviewed journal article
Structure of ATTRv-F64S fibrils isolated from skin tissue of a living patient
Jun YuiD, Xuefeng ZhangiD, Sandra PintoniD, Elena VacchiiD, Andrea CavalliiD, Matteo PecoraroiD, Giorgia MelliiD, Andreas BolandiD
Abstract
Amyloid transthyretin-derived (ATTR) amyloidosis is a degenerative, systemic disease characterized by transthyretin fibril deposition in organs like the heart, kidneys, liver, and skin. We report the first cryo-EM structure of transthyretin fibrils isolated from skin tissue of a living patient carrying a rare genetic mutation (ATTRv F64S). The structure adopts a highly conserved fold previously observed in other ATTR fibrils from different tissues or genetic variants. Mass spectrometry was used to evaluate fibril content and identify post-translational modifications. The structural consistency between ATTR filaments validates non-invasive skin biopsy as a diagnostic tool.
- organism: human
- assay: cryo-EM
- assay: proteomics
- research focus: protein structure prediction
- research focus: cell type annotation
- research focus: differential expression
- approach: experimental assay
- approach: microscopy & imaging analysis
- Citations
- 3
- FWCI
- 0.90
- Field percentile
- top 27%
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