AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils

Akanksha Bansal, Matthias Schmidt, Matthies Rennegarbe, Christian Haupt, Falk Liberta, Sabrina Stecher, Ioana Puscalau-Girtu, Alexander Biedermann and Marcus Fändrich ()
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Akanksha Bansal: Ulm University
Matthias Schmidt: Ulm University
Matthies Rennegarbe: Ulm University
Christian Haupt: Ulm University
Falk Liberta: Ulm University
Sabrina Stecher: Ulm University
Ioana Puscalau-Girtu: Ulm University
Alexander Biedermann: Ulm University
Marcus Fändrich: Ulm University

Nature Communications, 2021, vol. 12, issue 1, 1-9

Abstract: Abstract Systemic AA amyloidosis is a world-wide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from serum amyloid A (SAA) protein. Using cryo electron microscopy we here show that amyloid fibrils which were purified from AA amyloidotic mice are structurally different from fibrils formed from recombinant SAA protein in vitro. Ex vivo amyloid fibrils consist of fibril proteins that contain more residues within their ordered parts and possess a higher β-sheet content than in vitro fibril proteins. They are also more resistant to proteolysis than their in vitro formed counterparts. These data suggest that pathogenic amyloid fibrils may originate from proteolytic selection, allowing specific fibril morphologies to proliferate and to cause damage to the surrounding tissue.

Date: 2021
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DOI: 10.1038/s41467-021-21129-z

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