Amyloid fibril structure from the vascular variant of systemic AA amyloidosis

Banerjee S, Baur J, Daniel C, Pfeiffer PB, Hitzenberger M, Kuhn L, Wiese S, Bijzet J, Haupt C, Amann KU, Zacharias M, Hazenberg BP, Westermark GT, Schmidt M, Fändrich M (2022)

Publication Type: Journal article

Publication year: 2022

Journal

Nature Communications Nature Publishing Group: Nature Communications

Book Volume: 13

Article Number: 7261

Journal Issue: 1

DOI: 10.1038/s41467-022-34636-4

Abstract

Systemic AA amyloidosis is a debilitating protein misfolding disease in humans and animals. In humans, it occurs in two variants that are called ‘vascular’ and ‘glomerular’, depending on the main amyloid deposition site in the kidneys. Using cryo electron microscopy, we here show the amyloid fibril structure underlying the vascular disease variant. Fibrils purified from the tissue of such patients are mainly left-hand twisted and contain two non-equal stacks of fibril proteins. They contrast in these properties to the fibrils from the glomerular disease variant which are right-hand twisted and consist of two structurally equal stacks of fibril proteins. Our data demonstrate that the different disease variants in systemic AA amyloidosis are associated with different fibril morphologies.

Authors with CRIS profile

Christoph Daniel Department of Nephropathology Kerstin Ute Amann Professur für Nephropathologie

Involved external institutions

Universität Ulm DE Germany (DE) Technische Universität München (TUM) DE Germany (DE) University Medical Center Groningen (UMCG) / Universitair Medisch Centrum Groningen NL Netherlands (NL) Uppsala University SE Sweden (SE)

How to cite

APA:

Banerjee, S., Baur, J., Daniel, C., Pfeiffer, P.B., Hitzenberger, M., Kuhn, L.,... Fändrich, M. (2022). Amyloid fibril structure from the vascular variant of systemic AA amyloidosis. Nature Communications, 13(1). https://doi.org/10.1038/s41467-022-34636-4

MLA:

Banerjee, Sambhasan, et al. "Amyloid fibril structure from the vascular variant of systemic AA amyloidosis." Nature Communications 13.1 (2022).

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