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Structural basis for transthyretin amyloid formation in vitreous body of the eye
Umeå University, Faculty of Science and Technology, Department of Chemistry.ORCID iD: 0000-0002-9500-5917
Umeå University, Faculty of Science and Technology, Department of Chemistry.ORCID iD: 0000-0003-0864-9798
Umeå University, Faculty of Science and Technology, Department of Chemistry.ORCID iD: 0000-0001-7301-8445
Umeå University, Faculty of Science and Technology, Department of Chemistry.ORCID iD: 0000-0003-3492-3287
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2021 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 12, no 1, article id 7141Article in journal (Refereed) Published
Abstract [en]

Amyloid transthyretin (ATTR) amyloidosis is characterized by the abnormal accumulation of ATTR fibrils in multiple organs. However, the structure of ATTR fibrils from the eye is poorly understood. Here, we used cryo-EM to structurally characterize vitreous body ATTR fibrils. These structures were distinct from previously characterized heart fibrils, even though both have the same mutation and type A pathology. Differences were observed at several structural levels: in both the number and arrangement of protofilaments, and the conformation of the protein fibril in each layer of protofilaments. Thus, our results show that ATTR protein structure and its assembly into protofilaments in the type A fibrils can vary between patients carrying the same mutation. By analyzing and matching the interfaces between the amino acids in the ATTR fibril with those in the natively folded TTR, we are able to propose a mechanism for the structural conversion of TTR into a fibrillar form.

Place, publisher, year, edition, pages
Nature Publishing Group, 2021. Vol. 12, no 1, article id 7141
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-190576DOI: 10.1038/s41467-021-27481-4ISI: 000728313100019PubMedID: 34880242Scopus ID: 2-s2.0-85120856247OAI: oai:DiVA.org:umu-190576DiVA, id: diva2:1621585
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Swedish Research Council, 2015-03607Available from: 2021-12-20 Created: 2021-12-20 Last updated: 2023-03-28Bibliographically approved

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Iakovleva, IrinaHall, MichaelOelker, MelanieSandblad, LindaAnan, IntissarSauer-Eriksson, A. Elisabeth

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Iakovleva, IrinaHall, MichaelOelker, MelanieSandblad, LindaAnan, IntissarSauer-Eriksson, A. Elisabeth
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Department of ChemistryWallenberg Centre for Molecular Medicine at Umeå University (WCMM)Section of Medicine
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Nature Communications
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)Biochemistry and Molecular Biology

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