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-Structure paper
タイトル | AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 1013, Year 2021 |
掲載日 | 2021年2月12日 |
著者 | Akanksha Bansal / Matthias Schmidt / Matthies Rennegarbe / Christian Haupt / Falk Liberta / Sabrina Stecher / Ioana Puscalau-Girtu / Alexander Biedermann / Marcus Fändrich / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:33579941 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 2.73 - 3.5 Å |
構造データ | EMDB-11162: amyloid fibril morphology i (in vitro) from murine SAA1 protein EMDB-11163, PDB-6zcg: EMDB-11164, PDB-6zch: |
由来 |
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キーワード | PROTEIN FIBRIL / systemic amyloidosis / misfolding disease / inflammation / prion |