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

Systemic AA amyloidosis is a protein misfolding disease caused by the formation of amyloid fibrils from serum amyloid A (SAA) protein. Here, the authors present the cryo-EM structures of AA amyloid fibrils isolated from mouse tissue and in vitro formed fibrils, which differ in their structures and t...

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Main Authors: Akanksha Bansal, Matthias Schmidt, Matthies Rennegarbe, Christian Haupt, Falk Liberta, Sabrina Stecher, Ioana Puscalau-Girtu, Alexander Biedermann, Marcus Fändrich
Format: Article
Language:English
Published: Nature Portfolio 2021-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-21129-z
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author Akanksha Bansal
Matthias Schmidt
Matthies Rennegarbe
Christian Haupt
Falk Liberta
Sabrina Stecher
Ioana Puscalau-Girtu
Alexander Biedermann
Marcus Fändrich
author_facet Akanksha Bansal
Matthias Schmidt
Matthies Rennegarbe
Christian Haupt
Falk Liberta
Sabrina Stecher
Ioana Puscalau-Girtu
Alexander Biedermann
Marcus Fändrich
author_sort Akanksha Bansal
collection DOAJ
description Systemic AA amyloidosis is a protein misfolding disease caused by the formation of amyloid fibrils from serum amyloid A (SAA) protein. Here, the authors present the cryo-EM structures of AA amyloid fibrils isolated from mouse tissue and in vitro formed fibrils, which differ in their structures and they also show that the ex vivo fibrils are more resistant to proteolysis than the in vitro fibrils and propose that pathogenic amyloid fibrils might originate from proteolytic selection.
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spelling doaj.art-15b5d0653a7f4fee9b6e4b37a7961e1e2022-12-21T20:29:24ZengNature PortfolioNature Communications2041-17232021-02-011211910.1038/s41467-021-21129-zAA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrilsAkanksha Bansal0Matthias Schmidt1Matthies Rennegarbe2Christian Haupt3Falk Liberta4Sabrina Stecher5Ioana Puscalau-Girtu6Alexander Biedermann7Marcus Fändrich8Institute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversitySystemic AA amyloidosis is a protein misfolding disease caused by the formation of amyloid fibrils from serum amyloid A (SAA) protein. Here, the authors present the cryo-EM structures of AA amyloid fibrils isolated from mouse tissue and in vitro formed fibrils, which differ in their structures and they also show that the ex vivo fibrils are more resistant to proteolysis than the in vitro fibrils and propose that pathogenic amyloid fibrils might originate from proteolytic selection.https://doi.org/10.1038/s41467-021-21129-z
spellingShingle Akanksha Bansal
Matthias Schmidt
Matthies Rennegarbe
Christian Haupt
Falk Liberta
Sabrina Stecher
Ioana Puscalau-Girtu
Alexander Biedermann
Marcus Fändrich
AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
Nature Communications
title AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
title_full AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
title_fullStr AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
title_full_unstemmed AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
title_short AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
title_sort aa amyloid fibrils from diseased tissue are structurally different from in vitro formed saa fibrils
url https://doi.org/10.1038/s41467-021-21129-z
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