Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis

Matthias Schmidt, Sebastian Wiese, Volkan Adak, Jonas Engler, Shubhangi Agarwal, Günter Fritz, Per Westermark, Martin Zacharias and Marcus Fändrich ()
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Matthias Schmidt: Ulm University
Sebastian Wiese: Ulm University
Volkan Adak: Ulm University
Jonas Engler: Ulm University
Shubhangi Agarwal: University of Hohenheim
Günter Fritz: University of Hohenheim
Per Westermark: Uppsala University
Martin Zacharias: Technical University Munich
Marcus Fändrich: Ulm University

Nature Communications, 2019, vol. 10, issue 1, 1-9

Abstract: Abstract ATTR amyloidosis is one of the worldwide most abundant forms of systemic amyloidosis. The disease is caused by the misfolding of transthyretin protein and the formation of amyloid deposits at different sites within the body. Here, we present a 2.97 Å cryo electron microscopy structure of a fibril purified from the tissue of a patient with hereditary Val30Met ATTR amyloidosis. The fibril consists of a single protofilament that is formed from an N-terminal and a C-terminal fragment of transthyretin. Our structure provides insights into the mechanism of misfolding and implies the formation of an early fibril state from unfolded transthyretin molecules, which upon proteolysis converts into mature ATTR amyloid fibrils.

Date: 2019
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DOI: 10.1038/s41467-019-13038-z

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